Fcgamma receptor (FCGR) dependent phagocytosis (Homo sapiens)

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2, 8, 51, 7849, 5923, 655618, 216, 15, 486822, 8633, 64, 8938, 6136, 5766, 7413, 29, 30, 53, 54, 703, 40, 6216, 32, 8724, 8543, 7316, 3227, 50, 6926, 65, 71, 77, 81...47, 9211, 6031, 49, 597410, 20, 25, 28, 39...934, 6737, 8819, 55, 6341, 4581, 8240561, 7, 12, 72, 79...42, 7614, 35, 51, 83, 935, 46, 52, 9017, 75phagocytic cupendoplasmic reticulum lumencytosolIg heavy chain V-III region DOB ACTG1 Ig lambda chain V-II region BOH IGHG1 IGLV3-27(1-?) ARPC1B FCGR1A IGLV3-12(1-?) IGLC6 Ig lambda chain V-III region SH ACTR3 NCKAP1L ARPC1A Ig lambda chain V-VI region AR Ig heavy chain V-II region MCE ACTB(1-375) CDC42 PIK3CB Ig lambda chain V-II region BOH IGHV(1-?) IGKV1-12 IGLV7-43(1-?) ATP IGKV4-1(21-?) IGLV1-40(1-?) p-4Y-PLCG1 p-Y150-WASF2 PCIGLV3-22(1-?) IGKV4-1(21-?) IGLV3-22(1-?) IGLV3-25(1-?) ELMO2 H2OIg kappa chain V-III region POM Ig kappa chain V-I region AU IGLV1-36(1-?) IGLV2-11(1-?) ATP IGLV11-55(1-?) Ig kappa chain V-I region AG Ig kappa chain V-I region Gal GTP IGLV10-54(1-?) Ig kappa chain V-III region POM Ig kappa chain V-I region Gal Ig kappa chain V region EV15 Ig heavy chain V-II region NEWM IGLV1-44(1-?) Ig heavy chain V-III region BRO WIP family proteinsGTP IGLV4-69(1-?) p-Y173-VAV3 Ig heavy chain V-III region CAM Ig heavy chain V-III region TRO Ig heavy chain V-III region KOL Ca2+IGKC Ig heavy chain V-II region OU IGLV11-55(1-?) p-Y160,Y171-CD3G Ig lambda chain V-I region VOR Ig lambda chain V-IV region Bau Ig kappa chain V-III region VG WAS Ig kappa chain V-II region RPMI 6410 IGKV4-1(21-?) Ig heavy chain V-II region ARH-77 Ig lambda chain V-I region VOR ARPC3 IGLV3-25(1-?) IGLV1-36(1-?) PI3KIg kappa chain V-I region AG RAC1:GTPIg heavy chain V-III region KOL Ig kappa chain V-II region RPMI 6410 IGLV4-69(1-?) IGLV3-22(1-?) FCGR1A Ig lambda chain V-IV region Bau IGKV2D-30 IGKV1-5(23-?) Ig heavy chain V-I region HG3 Ig heavy chain V-II region WAH IGLV8-61(1-?) WIPF1 Ig heavy chain V-II region OU Ig kappa chain V-I region AG p-Y160,Y171-CD3G Ig lambda chain V-I region NEWM Ig heavy chain V-II region ARH-77 PLCG1 Ig heavy chain V-III region BUT IGLV4-69(1-?) Ig heavy chain V-III region CAM Ig heavy chain V-III region BRO NCKAP1L Ig lambda chain V-I region NEWM NCKIPSD IGLV4-69(1-?) Ig lambda chain V-I region VOR IGLV5-37(1-?) IGKV1-12 MyosinNCKAP1 CYFIP2 VAV2 IGLV5-45(1-?) WIPF1 IGLV2-18(1-?) Ig heavy chain V-II region OU IGHG3 Ig heavy chain V-II region OU ARPC4 p-Y150,S343,T346-WASF2 IGLC6 H2OIg kappa chain V-I region BAN ADP IGLV3-22(1-?) IGHV1-2 IGLV11-55(1-?) RAC1 Ig kappa chain V-II region FR IGKV1-12 Ig lambda chain V-I region NEW IGLV(23-?) IGHG3 IGKV1-5(23-?) PI(4,5)P2Ig heavy chain V-III region JON CDC42:GTP:WASP/N-WASP:WIP:SH3 proteinsIGHG4 p-Y256-WASL FCGR3A WIPF2 IGLV1-44(1-?) IGHG3 Ig lambda chain V-IV region Hil Ig heavy chain V-III region BUT Ig lambda chain V-I region VOR F-actin MYO9B IGLV3-25(1-?) IGLV3-16(1-?) Ig kappa chain V region EV15 Ig heavy chain V-II region OU Ca2+IGLC7 ATPIGLV3-25(1-?) ACTB(1-375) FCGR1A IGKC Ig kappa chain V-III region POM Ig heavy chain V-III region TRO NCKAP1L IGHG2 IGHG4 Ig lambda chain V-IV region Hil PLC gamma1,2Ig kappa chain V-I region Daudi Ig lambda chain V-III region SH LYN Ig kappa chain V-I region Gal IGLV2-11(1-?) p-Y160,Y171-CD3G IGLV4-69(1-?) Ig kappa chain V-III region VG BRK1 Ig heavy chain V-I region EU IGKV3D-20 IGHG2 Ig lambda chain V-IV region Hil Ig heavy chain V-III region KOL p-4Y-PLCG1Ig lambda chain V-I region NEW IGKC p-Y150,S343,T346-WASF2 p-6Y-CD247 IGHG4 IGKV2D-30 IGHV(1-?) IGKVA18(21-?) I(1,4,5)P3 Antigen Ig heavy chain V-III region DOB ATPNCK1 NCKAP1 IGHV1-2 ADPIg kappa chain V region EV15 PLDIGLV7-46(1-?) IGLV7-43(1-?) IGHV(1-?) Ig kappa chain V-III region POM FCGR2A IGLC1 VAV3 IGLV3-16(1-?) Ig heavy chain V-II region WAH CYFIP2 IGKV3D-20 IGLV2-33(1-?) Ig kappa chain V-II region FR IGKVA18(21-?) Ig kappa chain V region EV15 IGLV3-16(1-?) Antigen IGLV3-16(1-?) IGLV1-40(1-?) IGLV10-54(1-?) IGLV5-37(1-?) Ig kappa chain V-I region Wes IGLV7-43(1-?) Ig lambda chain V-I region HA Ig heavy chain V-II region MCE Ig kappa chain V-II region RPMI 6410 WIPF2 Ig heavy chain V-II region NEWM IGLV8-61(1-?) Ig kappa chain V-I region HK101 IGLV1-40(1-?) GTPARPC1B CD3G IGKC IGLC3 IgH heavy chain V-III region VH26 precursor Ig lambda chain V-II region MGC IGLV3-22(1-?) Ig heavy chain V-III region KOL IGHG2 Ig lambda chain V-II region TOG Ig kappa chain V-I region Wes Ig kappa chain V-I region Daudi GTP Ig heavy chain V-III region DOB ARPC4 CYFIP1 IGKVA18(21-?) Ig lambda chain V-II region MGC IGKV2-28 BRK1 WIPF1 IGHV1-2 Ig lambda chain V-IV region Hil N-WASP Ig lambda chain V-IV region Bau IGLV3-12(1-?) IGLV11-55(1-?) IGLC1 Ig heavy chain V-III region JON IGLV2-23(1-?) PCIg kappa chain V region EV15 NCK1 Ig heavy chain V-I region HG3 Motherfilament:branchingcomplex:daughterfilamentIg heavy chain V-III region BUT MYH2 NCKIPSD IGLV3-27(1-?) RAC1 IGLV3-27(1-?) IGLV10-54(1-?) IGLV5-45(1-?) FCGR3A IGLV2-11(1-?) Ig heavy chain V-III region JON pLIMK dimer:HSP-90FCGRIA:CD3GhomodimerIGLV1-36(1-?) IGLV2-23(1-?) Ig kappa chain V-III region VG BTK IGKV2D-30 ABI1 ARPC4 FCGR1A Ig kappa chain V-I region Wes G-actinWIPF1 Ig kappa chain V-I region HK101 Ig lambda chain V-II region NEI Ig lambda chain V-III region SH IGLV4-3(1-?) IGHG1 Ig lambda chain V-II region MGC NCKIPSD FCGR3A IGLV1-36(1-?) IGKV2D-30 IGLV3-12(1-?) Antigen ACTR3 Ig heavy chain V-II region WAH PTK2 GTP IGLC6 Ig heavy chain V-II region MCE IGHV7-81(1-?) ITPR3 IGKC CDC42 Ig heavy chain V-II region ARH-77 IGHG2 Ig kappa chain V-III region B6 CDC42:GTP:WASP/N-WASPIg kappa chain V-I region AG Ig heavy chain V-III region BRO Ig kappa chain V region EV15 GTP IGHV(1-?) Ig kappa chain V-I region AU Ig kappa chain V-I region AU IGKV2-28 IGLV11-55(1-?) IGKC Ig heavy chain V-II region ARH-77 PI(3,4,5)P3 IgH heavy chain V-III region VH26 precursor Ig lambda chain V-II region MGC IGKV2-28 PKC-delta/epsilonp-4S-ABI2 RAC1 IGLV3-25(1-?) IGLV3-12(1-?) ABI2 IGLV11-55(1-?) Ig lambda chain V-IV region Hil N-WASP IGKV1-12 Ig lambda chain V-VI region AR IGLV5-37(1-?) PAIg lambda chain V-IV region Kern Ig kappa chain V-I region BAN GTP Ig kappa chain V-III region POM p-Y288,Y304-FCGR2A PI(3,4,5)P3 IGHG1 ARPC4 ADPIGLV1-40(1-?) IGKV1-5(23-?) IGKV3D-20 FCGR3A IGLC6 Ig kappa chain V-III region POM ADPIg lambda chain V-VI region AR IGLC6 Antigen Ig kappa chain V-I region BAN IGLV3-25(1-?) SRC-1 Ig heavy chain V-I region HG3 IGLV3-27(1-?) IGHV7-81(1-?) Ig lambda chain V-III region SH Ig lambda chain V-VI region AR WAS Ig kappa chain V-III region VG ACTR3 BAIAP2 Ig lambda chain V-I region NEW Ig lambda chain V-IV region Kern IGHV(1-?) Ig kappa chain V-II region FR ARPC3 F-actin Ig heavy chain V-II region MCE Ig kappa chain V-I region AG IGLV2-33(1-?) Ig kappa chain V-I region Wes Ig heavy chain V-III region CAM IGLV4-3(1-?) IGLV8-61(1-?) Ig lambda chain V region 4A IGLV7-46(1-?) Ig kappa chain V-III region B6 Ig kappa chain V-I region BAN Ig heavy chain V-III region JON Antigen Ig heavy chain V-III region JON Ig lambda chain V-IV region Kern IGLV4-3(1-?) Ig heavy chain V-III region TRO Ig kappa chain V-III region VG ARPC2 Ig lambda chain V-VI region AR p-6Y-CD247 ADPIGLV3-27(1-?) IGKV3D-20 VAV1,2,3Ig kappa chain V-III region POM Ig kappa chain V-II region Cum FCGR1A p-6Y-SYK IGLC1 Ig heavy chain V-II region MCE FCGRIIIA:CD3G/CD3ZdimersIGLV2-18(1-?) IGHV(1-?) IGLC2 p-Y291-WAS WIPF1 Ig lambda chain V-IV region Kern GRB2-1 IGLV3-27(1-?) IGLV2-23(1-?) IGKC IGKV2D-30 IGLV4-60(1-?) IGLV11-55(1-?) p-Y151,S,T-WASF3 Ig kappa chain V-III region VG MYH9 WASF2 IGHV7-81(1-?) Ig lambda chain V-I region NEWM CDC42 DAGsIGLV2-23(1-?) IGHV1-2 ITPR:I(1,4,5)P3tetramerIg heavy chain V-III region BUT Ig lambda chain V-I region NEWM Ig lambda chain V-III region LOI ARPC2 FCGR3A Ig kappa chain V-III region B6 IGLV11-55(1-?) IGLV4-3(1-?) ARPC3 Ig lambda chain V-I region VOR Ig kappa chain V-I region HK101 p-Y151,S,T-WASF3 WASP/N-WASPIg heavy chain V-III region BRO Ig lambda chain V-II region NEI IGHG1 Ig heavy chain V-III region WEA Antigen PI(3,4,5)P3 Ig kappa chain V-I region DEE CYFIP1 Ig heavy chain V-III region JON Ig kappa chain V-I region Wes Ig lambda chain V-I region NEW IGLC6 Ig kappa chain V-I region BAN IGLV1-36(1-?) IGHV1-2 PAK1 CYFIP2 p-Y288,Y304-FCGR2A Ig kappa chain V-I region DEE Ig heavy chain V-II region MCE IGKV2D-30 Ig heavy chain V-III region WEA Ig lambda chain V-IV region Hil Ig kappa chain V-I region AU p-Y,S,T-WRC:IRSp53/58:RAC1:GTP:PIP3IGLV2-11(1-?) Ig kappa chain V region EV15 IGHV(1-?) Ig kappa chain V-I region AU p-T,Y MAPK dimersIg kappa chain V-I region DEE IGLV7-46(1-?) WIPF2 IGLV5-45(1-?) IGHV1-2 SH3 domain proteinsp-6Y-SYK Ig lambda chain V-II region MGC Ig lambda chain V-II region TOG VAV2 p-6Y-SYK Ig heavy chain V-II region MCE IGLC1 IGLV3-27(1-?) ADPIg heavy chain V-III region BUT p-Y753,Y759,Y1217-PLCG2 Ig heavy chain V-II region WAH IGLV7-46(1-?) IGKV2-28 ARPC5 IGLV3-12(1-?) IGLV8-61(1-?) WAVE2, WASP,N-WASP:ARP2/3complex:G-actinIGLC1 Ig kappa chain V-I region HK101 p-Y291-WAS PiIGLV1-40(1-?) FCGR1A Ig heavy chain V-II region OU IGLV3-16(1-?) RAC1:GTP,CDC42:GTP:PAK1Ig kappa chain V-I region AU IGLC3 IGLV7-46(1-?) IGHG1 Ig lambda chain V-I region NEWM ATPIg lambda chain V-VI region AR IGHV7-81(1-?) Ig heavy chain V-III region TRO NCKIPSD PIK3R1 IGHV(1-?) Ig heavy chain V-III region CAM Ig lambda chain V-II region TOG Ig lambda chain V-I region HA Ig lambda chain V-IV region Kern IGLC2 IGKV1-12 Ig heavy chain V-III region BUT p-5S-ABI1 IGLC1 IGLC1 Ig heavy chain V-III region WEA LIMK1IGLV1-44(1-?) ACTR2 Ig heavy chain V-III region BUT IGLV2-18(1-?) RAC1 IGKV2-28 IGLC3 CDC42 IGLC2 p-Y150-WASF2 Ig heavy chain V-II region OU Ig kappa chain V-I region Wes Ig kappa chain V-I region BAN Ig lambda chain V-IV region Kern Ig heavy chain V-II region OU Ig heavy chain V-III region TRO IGKV4-1(21-?) IGLV7-46(1-?) IGHG2 IGLV2-33(1-?) ATPIGKV1-5(23-?) p-Y160,Y171-CD3G IGKV3D-20 IGLV4-69(1-?) Ig heavy chain V-III region KOL IGLV1-44(1-?) Ig heavy chain V-III region WEA IGLC1 IGLV10-54(1-?) IGLV4-69(1-?) ITPR3 Ig heavy chain V-II region ARH-77 Ig kappa chain V-I region AG Ig kappa chain V-III region B6 IGLV2-23(1-?) IGKV4-1(21-?) IGKVA18(21-?) IGKV4-1(21-?) CDC42 Ig lambda chain V-VI region AR p-6Y-CD247 Ig kappa chain V-II region FR IGLC2 Ig kappa chain V-I region AU IgH heavy chain V-III region VH26 precursor Ig lambda chain V-I region VOR ADP Ig lambda chain V-IV region Hil Ig lambda chain V-I region NEWM ARPC1A RAC1:GDPIGLV1-44(1-?) IGLC6 Ig kappa chain V-I region DEE IGLV1-44(1-?) ARPC3 IGLV(23-?) ATPIg lambda chain V-II region BOH ATP IGLV5-37(1-?) Ig kappa chain V-I region HK101 Ig lambda chain V-IV region Kern Ig kappa chain V-I region BAN Ig lambda chain V-I region NEWM IGHV1-2 IGLC7 Ig kappa chain V-I region Gal Ig heavy chain V-III region CAM Ig lambda chain V-III region LOI IGLV2-23(1-?) CDC42:GDPIg lambda chain V-IV region Hil Ig lambda chain V-I region VOR Ig heavy chain V-III region DOB Ig heavy chain V-III region WEA Ig heavy chain V-II region ARH-77 IGKC IGKV2-28 Ig heavy chain V-III region KOL p-Y288,Y304-FCGR2A IGHG1 IGLV(23-?) ATP BAIAP2 Ig kappa chain V-II region Cum ADPIGLC2 IGLV4-69(1-?) IGLV(23-?) p-Y151,S,T-WASF3 IGLV7-46(1-?) Ig lambda chain V-I region VOR IGLV7-46(1-?) IGLV4-60(1-?) IGKV2-28 CRK IGKC Ig heavy chain V-III region BUT GRB2-1 IGLV11-55(1-?) IGLV3-25(1-?) Antigen IGHV7-81(1-?) Ig kappa chain V-I region DEE Ig lambda chain V-II region MGC Ig lambda chain V-III region SH Ig lambda chain V-III region SH Ig heavy chain V-III region WEA GTPIGKVA18(21-?) p-Y160,Y171-CD3G IGKV2D-30 IGLV3-16(1-?) BRK1 NCKAP1 IGLV1-36(1-?) Ig lambda chain V-II region BOH Ig lambda chain V-II region BOH Ig heavy chain V-III region JON Ig lambda chain V-IV region Hil p-6Y-CD247 Ig heavy chain V-III region JON PI(3,4)P2NCK1 Ig lambda chain V region 4A IGKV3D-20 IGLC2 Ig heavy chain V-I region EU Ig heavy chain V-I region EU IGLV1-44(1-?) Ig kappa chain V-I region HK101 Ig kappa chain V-I region HK101 MYO1C ARPC1A Ig kappa chain V-III region POM Ig lambda chain V-I region HA clusteredIgG-Ag:p-FCGRs:SYKIGLV3-27(1-?) IGLV5-45(1-?) ACTR2 NCK1 IGLV10-54(1-?) IGKV4-1(21-?) Ig heavy chain V-I region HG3 Ig heavy chain V-I region EU Ig lambda chain V-I region NEW IGLV1-36(1-?) IGLV10-54(1-?) Ig heavy chain V-III region DOB Ig heavy chain V-II region ARH-77 Ig kappa chain V-I region Daudi Ig kappa chain V-II region RPMI 6410 Ig kappa chain V-II region FR IGLV5-45(1-?) Ig kappa chain V-II region Cum Ig kappa chain V-II region Cum IGKV2D-30 p-S3-CFL1 GRB2-1 Ig kappa chain V-II region RPMI 6410 IGLV5-37(1-?) Ig kappa chain V-I region Gal Ig kappa chain V-III region POM Ig kappa chain V-I region DEE Ig lambda chain V-I region NEW IGHG4 Ig heavy chain V-III region KOL IGHV(1-?) IGKV1-5(23-?) WAVE2, WASP, N-WASPIGLV3-22(1-?) IGLV2-18(1-?) CDC42:GTP:p-Y-WASP/p-Y-WASL:WIP:SH3 proteinsIGLC7 IGLV2-18(1-?) Ig heavy chain V-III region CAM Ig heavy chain V-I region EU Ig heavy chain V-II region NEWM Ig lambda chain V-I region HA Ig kappa chain V-III region VG IGLV1-44(1-?) IGHG3 IGKC IGLC3 FCGR1A Ig lambda chain V-III region SH Ig lambda chain V-IV region Bau ARPC5 Ig kappa chain V-I region AU IGKC Ig heavy chain V-II region MCE p-Y291-WAS Ig kappa chain V-II region Cum ADPIGHG3 IGLC7 FCGR3A IGLV10-54(1-?) IGLV4-69(1-?) IGLV5-45(1-?) IGLV3-25(1-?) clusteredIgG-Ag:p-FCGRsIg kappa chain V-II region FR Ig kappa chain V-I region DEE Ig kappa chain V-I region Wes Ig heavy chain V-III region CAM CFL1IGLC3 PIK3R1 ITPR2 Ig lambda chain V-I region HA FCGR1A IGKVA18(21-?) Ig lambda chain V-IV region Bau MYO10 IGHV1-2 Ig kappa chain V-I region Gal Ig heavy chain V-I region EU CDC42 IGLV3-12(1-?) ATP ATPIg kappa chain V-I region BAN Ig lambda chain V-VI region AR IGHG3 IGLV(23-?) IGLC3 Ig kappa chain V-I region DEE IGLV7-43(1-?) Ig heavy chain V-II region NEWM Ig lambda chain V-I region HA IgH heavy chain V-III region VH26 precursor Ig kappa chain V-II region RPMI 6410 IGKV2-28 Ig heavy chain V-I region EU Ig kappa chain V-II region RPMI 6410 Ig lambda chain V-IV region Hil IGLC3 clusteredIgG-Ag:p-FCGRs:p-6Y-SYK:PLCGIGLV1-40(1-?) IGLV2-23(1-?) IGLV8-61(1-?) IGLC7 Ig lambda chain V-III region SH IGKV3D-20 IGKV3D-20 Ig lambda chain V-III region LOI ARPC1B IGLV1-36(1-?) p-Y288,Y304-FCGR2A IGLC1 Ig kappa chain V-I region DEE Ig lambda chain V-I region NEW Ig lambda chain V-III region SH IGLV1-40(1-?) IGLV3-27(1-?) IGLV10-54(1-?) Ig kappa chain V-I region Daudi IGLV2-33(1-?) CD247-1 WIPF2 Ig lambda chain V-VI region AR IGLV4-60(1-?) PI(4,5)P2 Ig lambda chain V-III region LOI Ig kappa chain V-I region HK101 IGLV7-43(1-?) IGHG4 IGLC2 IGHV7-81(1-?) ATPp-S144,T423-PAK1IGLV(23-?) ABI2 Ig kappa chain V-I region BAN Ig heavy chain V-II region NEWM BRK1 p-T185,Y187-MAPK1 Ig kappa chain V-I region BAN IGLC7 IGLV1-36(1-?) WIPF3 Ig heavy chain V-III region CAM GTP Ig lambda chain V-I region HA IgG-Ag:FCGRIIAIg kappa chain V-II region RPMI 6410 IGKVA18(21-?) CYFIP2 IGLV1-36(1-?) Ig lambda chain V-I region NEWM ARPC1A Ig lambda chain V-III region LOI Ig heavy chain V-II region NEWM Ig heavy chain V-III region BRO Ig lambda chain V-II region NEI ARPC5 Ig heavy chain V-II region WAH IGLV4-3(1-?) IGKV2-28 Ig kappa chain V-I region BAN Ig heavy chain V-I region EU MYO1C Ig kappa chain V-III region B6 Ig lambda chain V-IV region Hil ADPIg heavy chain V-III region BUT p-Y151-WASF1 Ig kappa chain V region EV15 Ig heavy chain V-III region JON p-4S-ABI2 Ig kappa chain V-II region Cum ABI1 Ig lambda chain V-II region TOG Ig kappa chain V region EV15 IGKV2-28 IP3 receptorhomotetramerIg heavy chain V-I region HG3 Ig kappa chain V-I region AU ADP Ig heavy chain V-II region OU IGLC7 IGKV1-12 p-Y151,S,T-WASF3 IGLV5-37(1-?) IGKVA18(21-?) Ig heavy chain V-III region TRO IGLC1 Ig lambda chain V-II region TOG Ig lambda chain V-IV region Bau SYK Ig heavy chain V-II region ARH-77 ARPC3 Ig heavy chain V-II region WAH IGKV1-5(23-?) IGHG3 PAK1 dimerIg lambda chain V-II region BOH CYFIP1 Ig heavy chain V-II region ARH-77 PI(4,5)P2Ig heavy chain V-I region HG3 Ig lambda chain V-IV region Kern IGLV3-22(1-?) IGLV4-3(1-?) WIPF2 Ig kappa chain V-I region AU IGKV1-12 Ig lambda chain V-III region LOI ARPC1A Antigen Ig heavy chain V-III region JON IGKV2D-30 FYN CYFIP1 Ig lambda chain V-III region LOI Ig lambda chain V-I region VOR RAC1 ACTG1 IGHG1 Ig kappa chain V-I region DEE IGHG2 Ig lambda chain V-I region NEW Ig kappa chain V-III region POM Ig kappa chain V-I region HK101 PLCG2 F-actinPhosphatidatephosphataseIg heavy chain V-II region MCE FCGR1A Ig lambda chain V-I region VOR Ig kappa chain V-I region AG Ig lambda chain V-VI region AR Ig lambda chain V-IV region Bau Ig lambda chain V-II region MGC ACTR2 IGKV1-12 PLCG1 Ig heavy chain V-I region HG3 Ig heavy chain V-I region EU Ig kappa chain V-II region Cum Ig heavy chain V-III region JON p-Y288,Y304-FCGR2A IGKV2D-30 Antigen IGKV3D-20 p-Y151,S,T-WASF1 Ig kappa chain V-II region FR Ig kappa chain V-I region DEE Ig kappa chain V-I region Wes Active LIMK1p-Y288,Y304-FCGR2A IGLV8-61(1-?) IGLV2-23(1-?) IGLV5-45(1-?) IGLV3-16(1-?) BAIAP2Ig heavy chain V-II region NEWM ATPIg kappa chain V-I region Daudi IGKC IGKV1-5(23-?) CYFIP2 IGLV7-43(1-?) Ig heavy chain V-III region BRO Ig heavy chain V-I region HG3 Ig kappa chain V-I region Daudi IGLV8-61(1-?) IGKVA18(21-?) p-6Y-SYK IGLC6 IGLV4-3(1-?) IgG-Ag:FCGRIA:CD3GhomodimerIGHG4 IGLV3-22(1-?) Ig lambda chain V-II region MGC Ig lambda chain V-III region LOI Ig kappa chain V-I region Daudi IGLV4-3(1-?) Ig heavy chain V-III region WEA Ig heavy chain V-III region CAM ATPPiIGLV2-18(1-?) Ig kappa chain V-I region Daudi ACTR2 PLD1 Ig heavy chain V-II region NEWM IGLV7-43(1-?) IGLV11-55(1-?) F-actin IGLV3-22(1-?) Ig heavy chain V-III region DOB IGHV(1-?) Ig heavy chain V-III region TRO IGKVA18(21-?) IGLC2 Ig heavy chain V-II region WAH IGLC7 BAIAP2 p-Y151-WASF3 Ig heavy chain V-I region HG3 IGHG1 IGKV1-12 Ig kappa chain V-I region HK101 IGKV1-5(23-?) NCKAP1L IGLC6 IGLV4-3(1-?) IGHG3 NCK1 Ig kappa chain V-III region B6 IGKV3D-20 Ig kappa chain V-I region AU IgH heavy chain V-III region VH26 precursor Ig kappa chain V-II region FR Ig heavy chain V-III region BUT WIPF3 Ig lambda chain V-I region NEW Ig kappa chain V-II region Cum Ig heavy chain V-II region OU Ig lambda chain V-II region TOG Ig lambda chain V-I region VOR ARPC2 IGKV1-5(23-?) IGKV3D-20 IGLV4-3(1-?) Ig kappa chain V-III region VG PLD2 Ig kappa chain V-I region AG p-S,T508-LIMK1 NCKAP1L ITPR2 Ig lambda chain V-VI region AR Ig kappa chain V-II region FR WASF3 PI3K:p-6Y-SYKIGHG1 p-Y-WRC:IRSp53/58:RAC1:GTP:PIP3CDC42 BRK1 Ig lambda chain V-IV region Bau Ig kappa chain V-I region AG Ig heavy chain V-III region BRO IGLV2-18(1-?) RAC1 Ig heavy chain V-I region EU IGLC2 PIK3CA IGKC FCGR3A Ig lambda chain V-I region NEWM Ig heavy chain V-I region EU IGLV11-55(1-?) Ig heavy chain V-II region MCE Ig lambda chain V-II region BOH p-6Y-SYK IGLV3-12(1-?) ARPC1A IGLV3-16(1-?) IGLV4-60(1-?) Ig heavy chain V-III region CAM FCGR1A IGKVA18(21-?) p-Y150-WASF2 IGHV(1-?) IGKV3D-20 PI(3,4,5)P3 Ig lambda chain V-II region TOG Ig heavy chain V-III region BRO Ig heavy chain V-II region MCE NCKAP1 Ig lambda chain V region 4A Ig heavy chain V-II region ARH-77 IGLV7-46(1-?) IGLV4-3(1-?) IGLV7-43(1-?) Ig heavy chain V-II region NEWM Antigen IGLV1-40(1-?) IGLV4-69(1-?) Ig heavy chain V-III region JON Ig heavy chain V-II region OU Ig kappa chain V-I region Wes Ig kappa chain V-III region VG PAK1Ig kappa chain V-I region Gal IGLC6 Ig kappa chain V-I region AG Ig heavy chain V-III region TRO Ig kappa chain V-III region POM Ig kappa chain V-II region FR CDC42:GTPIg lambda chain V-III region SH ATPIGLC3 Ig heavy chain V-II region WAH YES1 Ig kappa chain V-I region Wes IGLV3-16(1-?) IGLV2-18(1-?) Ig heavy chain V-III region CAM IGKV4-1(21-?) clusteredIgG-Ag:p-FCGRsIg heavy chain V-I region EU IGLV5-45(1-?) IGLV(23-?) Ig lambda chain V-III region LOI Ig kappa chain V-III region POM ADPIGLV3-12(1-?) IGHV7-81(1-?) GDP FCGR1A FCGR2AIGLV3-25(1-?) NF2IGLV5-37(1-?) p-6Y-CD247 Ig lambda chain V-II region BOH Ig heavy chain V-III region KOL IGHG4 Ig lambda chain V-VI region AR Ig kappa chain V-II region RPMI 6410 IGLV2-33(1-?) IGLC2 Ig heavy chain V-III region TRO IGLC6 p-Y151,S,T-WASF1 IGLV1-40(1-?) ACTR2 IGLV4-60(1-?) Ig kappa chain V-II region Cum IGLV7-43(1-?) p-6Y-CD247 Myosin-X dimerIGLC3 IGLV(23-?) Ig heavy chain V-I region HG3 IGLV2-33(1-?) ITPR1 Ig lambda chain V-I region HA IGLV2-11(1-?) Motherfilament:ARP2/3:actin:ADPIg heavy chain V-II region NEWM Ig kappa chain V-III region VG IGLV10-54(1-?) clusteredIgG-Ag:FCGRsIg kappa chain V-I region Daudi IGHG3 Ig kappa chain V-III region VG Ig heavy chain V-III region KOL IGLV2-23(1-?) ARPC3 IGLV4-60(1-?) p-5S-ABI1 Ig kappa chain V-II region Cum WAVE RegulatoryComplexIGLV5-37(1-?) IGKV4-1(21-?) Ig lambda chain V-II region BOH Ig heavy chain V-I region HG3 IGLC3 IGKV4-1(21-?) Ig kappa chain V-II region RPMI 6410 IGLV3-16(1-?) IGLV3-25(1-?) Ig heavy chain V-III region WEA Ig lambda chain V-II region NEI Ig heavy chain V-II region WAH IGLV1-40(1-?) CYFIP2 IGLV3-27(1-?) Ig heavy chain V-II region NEWM Antigen IGLC7 WIPF3 Ig kappa chain V-I region AG Ig kappa chain V-II region FR Ig kappa chain V-III region B6 ARPC3 IGHV1-2 IGLV3-25(1-?) Ig heavy chain V-III region BUT N-WASP IGHV(1-?) Ig heavy chain V-III region TRO DAGsPI(4,5)P2 Ig lambda chain V-III region SH PAK1 Unknown GEFp-6Y-CD247 p-Y150-WASF2 IGLV2-11(1-?) Ig lambda chain V-I region VOR IGHG3 Ig lambda chain V-I region HA p-4Y-PLCG1 Ig kappa chain V-I region BAN IGLV2-11(1-?) IGLC3 Ig heavy chain V-I region HG3 ARPC2 Ig lambda chain V-II region NEI Ig heavy chain V-I region EU ATP RAC1 IGLV4-60(1-?) IGLV2-23(1-?) IGLV7-43(1-?) IGHG2 IGLV1-40(1-?) Ig kappa chain V-I region Wes IGLV10-54(1-?) p-Y151,S,T-WASF1 Ig kappa chain V-III region VG IGLV7-43(1-?) Ig lambda chain V-II region NEI Ig kappa chain V-I region Gal Ig kappa chain V-II region RPMI 6410 I(1,4,5)P3Ig heavy chain V-III region WEA Ig lambda chain V-III region LOI IGLV1-44(1-?) p-Y150,S343,T346-WASF2 p-T507,S645,S664-PRKCD(1-676) CDC42:GTP, RAC1:GTPIg kappa chain V-III region B6 Ig lambda chain V-II region TOG MYH9 IGKV4-1(21-?) IGLV4-69(1-?) Ig kappa chain V-II region RPMI 6410 WIPF3 Ig heavy chain V-II region ARH-77 ACTB(1-375) p-6Y-CD247 clusteredIgG-Ag:p-FCGRs:p-6Y-SYK:p-VAVIg kappa chain V-I region AU Ig kappa chain V-II region Cum IGLV8-61(1-?) Src family kinases(SFKs)WIPF2 IGLV3-22(1-?) IGLV3-22(1-?) H2OFCGR3A Ig heavy chain V-II region ARH-77 BRK1 ABI2 IGLV1-44(1-?) Ig lambda chain V-II region BOH GTP IGLC1 Antigen p-PLCGIGLV2-33(1-?) ARPC5 IgH heavy chain V-III region VH26 precursor IGLV4-60(1-?) Ig heavy chain V-II region ARH-77 Ig heavy chain V-II region NEWM IGLV5-37(1-?) p-S,T508-LIMK1 IGLV1-44(1-?) Ig kappa chain V-II region Cum IGLV3-25(1-?) ARPC5 IGLV2-23(1-?) Ig heavy chain V-III region BUT IGKV1-5(23-?) p-Y172-VAV2 p-Y753,Y759,Y1217-PLCG2 Ig lambda chain V-I region NEWM IGLV7-46(1-?) HSP90AB1 IGLV3-16(1-?) Ig heavy chain V-III region CAM Ig lambda chain V-I region VOR Ig lambda chain V-I region NEWM Ig heavy chain V-III region WEA BRK1 IGKV2-28 IGLV2-23(1-?) IGLV4-60(1-?) Ig lambda chain V-II region TOG HSP90AA1,HSP90AB1IGLV1-44(1-?) IGKV2D-30 WASF1 IGLC7 IGLC3 MYH2 ABI1 IGHV1-2 p-T508-LIMK1IGLV1-36(1-?) IGKV1-5(23-?) IGKV1-12 IGLC2 Ig kappa chain V-I region Gal I(1,4,5)P3 IGLV3-25(1-?) IGLV5-45(1-?) IGKV2-28 IGLV7-46(1-?) Ig lambda chain V-I region HA Ig kappa chain V-III region VG Ig heavy chain V-III region CAM IGLC3 IGLV4-60(1-?) Ig kappa chain V-I region BAN WIPF3 Ig lambda chain V-IV region Bau IGLC1 IGLV3-25(1-?) IGKV3D-20 Ig lambda chain V-IV region Hil IGKV1-5(23-?) IGLV1-36(1-?) IGLV2-11(1-?) Ig heavy chain V-III region DOB Ig kappa chain V-III region POM Ig lambda chain V-I region NEW IGLV4-69(1-?) IGLV5-37(1-?) ITPR2 IGLV3-22(1-?) IGLV3-27(1-?) IGLV5-37(1-?) IGLC7 Ig kappa chain V-I region DEE Ig heavy chain V-III region BRO IGHG2 G-actinIg lambda chain V-IV region Bau ADPACTR3 p-Y256-WASL Ig lambda chain V-IV region Hil Ig lambda chain V-II region NEI FCGR1A IGLV3-25(1-?) PiIg kappa chain V-II region RPMI 6410 IGKV1-12 IGLV8-61(1-?) IGLV7-43(1-?) IGLV4-3(1-?) IGLV2-23(1-?) IGLV2-23(1-?) Ig lambda chain V-I region NEWM WASF1 IGLV1-40(1-?) IGLC2 Ig lambda chain V-VI region AR Ig lambda chain V-II region NEI Ig kappa chain V-II region Cum Ig kappa chain V region EV15 WASF2 Ig heavy chain V-III region TRO Ig kappa chain V-III region B6 IGLV2-33(1-?) p-Y150,S343,T346-WASF2 IGLV1-44(1-?) IGHG3 Ig lambda chain V-I region NEW IGLV3-22(1-?) IGHG4 Ig kappa chain V-I region Wes IGLV11-55(1-?) GDPIGKV2D-30 Ig kappa chain V-III region VG NCKAP1 BAIAP2 ACTG1 IGHV1-2 Ig kappa chain V-I region Gal Ig lambda chain V-I region NEWM Ig heavy chain V-II region ARH-77 ACTR2 Ig lambda chain V-II region TOG Ig heavy chain V-III region BUT Ig kappa chain V region EV15 Ig heavy chain V-III region TRO IGLC7 VAV1 Ig heavy chain V-II region WAH Ig lambda chain V-II region NEI pCofilin: ActiveLIMK-1PLD3 ARPC4 Ig heavy chain V-III region BRO PRKCD IGHV1-2 IgH heavy chain V-III region VH26 precursor IGLV2-23(1-?) IGLV7-43(1-?) AHCYL1:NAD+:ITPR1:I(1,4,5)P3 tetramerIGLV5-45(1-?) Ig lambda chain V-II region MGC IGLV2-18(1-?) Ig heavy chain V-III region CAM ABI2 Ig heavy chain V-II region WAH Ig heavy chain V-III region DOB IGLV3-12(1-?) Ig kappa chain V-I region Gal Ig lambda chain V region 4A Ig kappa chain V-III region B6 IGHV1-2 IGHG1 IGHG4 p-Y151-WASF1 IGLV11-55(1-?) Ig kappa chain V-I region HK101 Ig lambda chain V-I region HA IGLV(23-?) Ig lambda chain V-IV region Kern FCGR3A Ig lambda chain V region 4A Antigen p-5S-ABI1 IGLV2-33(1-?) Ig lambda chain V region 4A IGLV4-60(1-?) ABI2 Ig kappa chain V-I region DEE IGLV4-3(1-?) IGLV7-46(1-?) IGKV1-5(23-?) IGKV1-12 IGLV10-54(1-?) Ig kappa chain V-I region Gal Ig lambda chain V-I region HA IGHG1 clusteredIgG-Ag:p-FCGRsIg kappa chain V-III region POM Ig heavy chain V-III region WEA Ig heavy chain V-III region DOB Ig lambda chain V-II region TOG Ig lambda chain V-IV region Kern IGLV10-54(1-?) Ig lambda chain V-II region BOH Ig heavy chain V-III region DOB Ig lambda chain V-III region SH Ig lambda chain V-I region NEWM ARPC1B PI(3,4,5)P3 IGHV1-2 Ig lambda chain V-II region TOG Ig kappa chain V-II region RPMI 6410 Ig kappa chain V-II region RPMI 6410 p-Y288,Y304-FCGR2A FCGR3A PLCG2 IGLV1-40(1-?) p-6Y-CD247 IGLV1-36(1-?) AHCYL1 PIK3CB HCK IGLV10-54(1-?) Ig heavy chain V-III region KOL IGLV1-36(1-?) IGHV7-81(1-?) IGLV10-54(1-?) MYO9B IGLV3-12(1-?) ATPIg lambda chain V-IV region Bau IGHG1 IGHG2 IGLV1-44(1-?) ABI1 p-Y174-VAV1 Ig kappa chain V-I region BAN Ig lambda chain V-III region LOI ELMO1 CDC42 ABI2 BAIAP2 ARPC2 PI(3,4,5)P3FCGR3A Ig kappa chain V region EV15 Ig lambda chain V-III region SH IGLV5-37(1-?) PLA2G6Antigen p-Y151,S,T-WASF1 Ig heavy chain V-III region JON Ig lambda chain V-IV region Kern PI(4,5)P2 PI(3,4,5)P3FCGR1A IGKV1-12 IGLV7-46(1-?) ARPC2 Ig lambda chain V-II region BOH p-Y160,Y171-CD3G ARPC1B Ig lambda chain V region 4A Ig lambda chain V-I region NEWM NCKAP1 IGLC7 Ig lambda chain V-III region LOI IGLV(23-?) IGLV3-12(1-?) IGLV5-37(1-?) Ig lambda chain V-II region NEI IGLV2-11(1-?) Ig lambda chain V-II region MGC Ig kappa chain V-II region FR ITPR3 Ig heavy chain V-III region JON p-Y256-WASL IGLV2-18(1-?) p-Y288,Y304-FCGR2A GTP IGKV1-12 Ig kappa chain V-I region Wes IGLV11-55(1-?) Ig heavy chain V-II region NEWM IGLV2-33(1-?) GRB2-1 FCGR3A ITPR1 IGLV8-61(1-?) ARPC1B IGLV11-55(1-?) IGLC6 IGLV8-61(1-?) IGLV5-37(1-?) PLD4 IGLC6 Ig kappa chain V-I region Daudi Ig lambda chain V-II region NEI ARPC4 ITPR1 FGR Ig kappa chain V-III region B6 Ig heavy chain V-I region HG3 IGHV7-81(1-?) ATPIg lambda chain V-VI region AR IGHV7-81(1-?) F-actin Ig lambda chain V region 4A IgH heavy chain V-III region VH26 precursor ABI1 IGLV11-55(1-?) Ig kappa chain V-I region Daudi p-5S-ABI1 Ig kappa chain V-II region Cum Ig heavy chain V-III region BRO IGHV7-81(1-?) IGLV5-45(1-?) IGHG2 Ig lambda chain V-III region LOI ACTR3 Ig lambda chain V-II region NEI IGLV4-3(1-?) Ig lambda chain V-I region HA Ig kappa chain V-III region B6 Ig kappa chain V-II region FR Ig heavy chain V-III region DOB VAV1 Ig lambda chain V-I region NEW IGLV(23-?) IGLV5-45(1-?) PI(4,5)P2 p-4S-ABI2 IGHV(1-?) IGHV7-81(1-?) IGHG2 IGLC2 FCGR1A IGHG2 Ig lambda chain V region 4A Ig kappa chain V-III region VG IGLV7-46(1-?) Ig heavy chain V-II region MCE p-Y151-WASF1 Ig heavy chain V-III region DOB Ig kappa chain V-II region Cum CD3G IGKV4-1(21-?) IGHG3 Ig lambda chain V-III region SH Antigen Ig kappa chain V-I region DEE IGKV2D-30 clusteredIgG-Ag:p-FCGRs:p-6Y-SYK:VAVIGLV4-60(1-?) Motherfilament:branchingcomplexIGHG2 IGLV2-33(1-?) ARPC1A IGLV1-44(1-?) IGLV4-69(1-?) GTP Ig lambda chain V-IV region Bau IGLV4-69(1-?) IGHG3 IGHG2 IGKV2-28 Ig kappa chain V-III region B6 CDC42 ATP IGKVA18(21-?) IGLV4-69(1-?) WAS IGLV3-12(1-?) Ig heavy chain V-II region WAH NCKAP1L SYKIg kappa chain V-II region FR FCGR2A Ig heavy chain V-III region DOB IGLV3-27(1-?) p-Y151-WASF3 Ig kappa chain V-I region Gal IGHV(1-?) Ig lambda chain V-I region VOR IGLV2-18(1-?) IGLV3-16(1-?) IGLV(23-?) Ig heavy chain V-II region OU Antigen:IgGCD3G ARPC5 CYFIP1 p-Y160,Y171-CD3G p-Y160,Y171-CD3G IGLV8-61(1-?) Ig lambda chain V-I region HA Ig kappa chain V-I region HK101 ARPC5 Ig kappa chain V-I region Daudi IGKV4-1(21-?) IGLV3-12(1-?) DOCK1 IGLC2 Ig heavy chain V-III region KOL Ig lambda chain V-IV region Hil Ig heavy chain V-II region WAH IGLC1 IGLC3 Ig heavy chain V-II region MCE Ig kappa chain V-I region AG IGHG2 Ig heavy chain V-II region OU IGLV7-43(1-?) BAIAP2 IGLV2-11(1-?) Ig kappa chain V-III region VG Ig heavy chain V-III region WEA p-Y151-WASF1 Myosin-Actinfilamentsp-Y160,Y171-CD3G IGLV3-25(1-?) CYFIP2 ATP Ig heavy chain V-III region WEA CD3G IGHG2 Ig lambda chain V-II region MGC PI(3,4,5)P3 IGKVA18(21-?) Ig kappa chain V-I region HK101 Ig heavy chain V-II region MCE Ig heavy chain V-III region CAM Ig kappa chain V-I region Wes Ig heavy chain V-I region HG3 IGLV2-11(1-?) IGKV3D-20 IGHG4 ACTB(1-375) IGLV3-22(1-?) MYO5A RAC1 IGLV2-18(1-?) IGHG1 CD247-1 Ig kappa chain V-I region Wes IGKVA18(21-?) Ig lambda chain V region 4A IGLV5-45(1-?) IGKV1-5(23-?) IGLV8-61(1-?) IGLV2-18(1-?) Ig lambda chain V-I region HA ATPIg heavy chain V-II region WAH IGLV2-11(1-?) Ig kappa chain V region EV15 Ig heavy chain V-III region KOL LPCIg lambda chain V-IV region Bau IGLC7 IGLV5-45(1-?) Ig heavy chain V-II region ARH-77 Ig heavy chain V-II region WAH CRKII:DOCK180:ELMOcomplex recruitedto phagocytic cupPI(4,5)P2 IGLV4-60(1-?) Ig heavy chain V-II region WAH Ig kappa chain V-I region AU NAD+ NCKAP1L PI(4,5)P2 IGLV1-36(1-?) IgH heavy chain V-III region VH26 precursor Ig heavy chain V-II region MCE IGLV4-69(1-?) Ig kappa chain V-I region AU IGLV2-33(1-?) Ig lambda chain V-II region BOH Ig lambda chain V-II region NEI IGHV(1-?) Ig lambda chain V region 4A Ig kappa chain V-I region Daudi IGLC3 p-T566,T710,S729-PRKCE Ig kappa chain V-I region Gal IGLC2 Ig heavy chain V-III region BUT IGKV4-1(21-?) Ig kappa chain V-II region FR Ig heavy chain V-III region BRO F-actin IGLV1-40(1-?) Ig lambda chain V region 4A IGLC7 IgH heavy chain V-III region VH26 precursor IGLV1-40(1-?) IGKC p-6Y-SYK Ig heavy chain V-II region OU ACTG1 GRB2-1 IgH heavy chain V-III region VH26 precursor Ig lambda chain V-II region MGC IGLV7-46(1-?) Ig lambda chain V-I region HA Ig kappa chain V-I region AG ChoMYO10 PRKCE IGLC1 WRC:IRSp53/58:RAC1:GTP:PIP3IGKV2D-30 IGLV8-61(1-?) Ig kappa chain V region EV15 IGLV1-40(1-?) Ig kappa chain V-I region DEE Ig heavy chain V-III region BRO HSP90AA1 IGLV(23-?) IGHV7-81(1-?) Ig lambda chain V-II region TOG Ig heavy chain V-III region BUT IGLV8-61(1-?) Ig heavy chain V-I region EU IGLV7-43(1-?) IGHV1-2 IgH heavy chain V-III region VH26 precursor IGLC1 IGKV1-5(23-?) Ig heavy chain V-I region HG3 Ig kappa chain V-I region AU ADPIGLV(23-?) Ig lambda chain V-III region LOI IGKV2-28 FCGR3A Ig lambda chain V region 4A PPAPDC1A RAC1 CYFIP1 IGLV2-33(1-?) FCGR3A Ig heavy chain V-III region CAM Ig lambda chain V-II region MGC IGKV2-28 ACTG1 NCKIPSD p-4S-ABI2 IGKV1-12 ADPIGHG1 IGLV1-44(1-?) IGKV1-12 Ig kappa chain V-I region HK101 Ig heavy chain V-III region KOL Ig kappa chain V-I region BAN GDP Ig heavy chain V-III region KOL IGLC2 IgH heavy chain V-III region VH26 precursor RAC1 MYO5A ABL1PIK3CA Ig lambda chain V-I region VOR Ig lambda chain V-IV region Kern Ig lambda chain V-IV region Bau IGKV1-5(23-?) Ig heavy chain V-III region WEA Antigen Ig heavy chain V-III region BUT IGHV(1-?) IGLV3-27(1-?) IGLV3-22(1-?) HSP90AB1 PI(3,4)P2 CD3G PPAPDC1B Ig heavy chain V-III region JON DOCK1 Ig lambda chain V-IV region Kern IGLV7-43(1-?) IGLC1 ARPC4 Ig kappa chain V-I region AG Ig lambda chain V-II region MGC IGLV4-3(1-?) CD247-1 IGKV3D-20 ADPIg lambda chain V-I region NEW Ig heavy chain V-III region KOL IGLV3-22(1-?) IGKC ACTB(1-375) p-Y160,Y171-CD3G Phospho-PKC-delta/epsilonIGLV8-61(1-?) GTP IGLV2-11(1-?) Ig lambda chain V-III region SH IGHV7-81(1-?) Ig heavy chain V-II region OU IGLV10-54(1-?) Ig kappa chain V region EV15 Ig heavy chain V-III region DOB PI(3,4,5)P3IGKV2-28 GRB2-1 HSP90AA1 Ig heavy chain V-III region TRO ARP2/3 complex (ATPbound)ELMO2 IGLV1-36(1-?) IGLV2-18(1-?) IGLV2-33(1-?) IGHG4 IGHG3 Ig kappa chain V-III region B6 Src-kinasesIg kappa chain V-III region B6 IGHV7-81(1-?) Ig heavy chain V-I region EU Ig heavy chain V-II region NEWM p-Y256-WASL Ig lambda chain V-IV region Hil Ig heavy chain V-III region TRO IGHG4 clusteredIgG-Ag:p-FCGRs:p-6Y-SYK:p-3Y-PLCGIGLV2-11(1-?) IGLV3-12(1-?) Ig lambda chain V-I region NEW GTP p-Y288,Y304-FCGR2A GTP Ig kappa chain V-I region BAN IGLV3-16(1-?) PIK3R2 IGLV2-18(1-?) IGLV2-33(1-?) Ig heavy chain V-II region MCE H2OIGKV3D-20 PI(4,5)P2IGHG4 p-Y291-WAS p-Y160,Y171-CD3G NCK1 CDC42 clusteredIgG-Ag:p-FCGRs:p-6Y-SYKIg lambda chain V region 4A Ig kappa chain V-I region Daudi Ig kappa chain V-II region FR IGKV4-1(21-?) IGLV2-33(1-?) VAV3 Ig lambda chain V-II region MGC Ig heavy chain V-III region DOB IGKC Ig lambda chain V-IV region Bau IGLV(23-?) Actin filament boundMyosin-XIg kappa chain V-I region HK101 IGLV2-11(1-?) Ig lambda chain V-III region SH IGLV3-16(1-?) IGLV2-18(1-?) IGLC6 Ig heavy chain V-III region TRO Ig lambda chain V-II region BOH Ig kappa chain V-II region RPMI 6410 Ig heavy chain V-II region NEWM IgH heavy chain V-III region VH26 precursor Ig lambda chain V-IV region Hil IGLV3-27(1-?) Ig heavy chain V-I region EU IGKV4-1(21-?) Ig lambda chain V-III region LOI Ig heavy chain V-III region DOB Ig lambda chain V-VI region AR Ig heavy chain V-II region ARH-77 Ig lambda chain V-II region TOG ARAIg lambda chain V-I region VOR IGLV7-46(1-?) Ig kappa chain V-I region HK101 Ig lambda chain V-VI region AR Ig kappa chain V-I region AG Ig heavy chain V-III region WEA CRK:DOCK180:ELMO1,ELMO2Ig kappa chain V-I region Wes IGHG3 IGHV7-81(1-?) Ig heavy chain V-III region JON p-T508-LIMK1 WIPF1 p-Y151-WASF3 ACTR3 Ig kappa chain V-I region Gal Ig heavy chain V-III region BRO Ig heavy chain V-II region NEWM IGHV1-2 Ig heavy chain V-III region TRO Ig kappa chain V-I region Daudi Ig heavy chain V-III region BRO Ig kappa chain V-III region B6 IGHG4 IGLC6 Ig kappa chain V-I region AG Ig lambda chain V region 4A IGLC6 PI(3,4,5)P3 Ig kappa chain V-III region POM Ig lambda chain V-II region NEI p-6Y-SYK IGLV5-37(1-?) Ig lambda chain V region 4A IGLV4-60(1-?) WIPF3 IgH heavy chain V-III region VH26 precursor PIK3R2 p-6Y-CD247 IGLC3 Ig heavy chain V-II region OU ATPIGLV2-23(1-?) NCKIPSD Ig lambda chain V-IV region Kern Ig lambda chain V-I region NEW Ig kappa chain V-III region POM IGHG1 p-Y288,Y304-FCGR2A Ig heavy chain V-I region HG3 Ig kappa chain V region EV15 p-Y151-WASF3 p-T202,Y204-MAPK3 IGLV5-45(1-?) ACTR2 IGHG1 Ig lambda chain V-I region NEWM IgG-Ag:FCGRIIIA:CD3G/CD3Z dimersIGLV5-37(1-?) Ig lambda chain V-II region TOG Ig kappa chain V-I region DEE Ig lambda chain V-II region TOG Ig lambda chain V-II region MGC Ig lambda chain V-IV region Kern IGHG3 ACTR3 IGLV3-27(1-?) IGHG4 Ig lambda chain V-II region NEI Ig lambda chain V-IV region Bau IgH heavy chain V-III region VH26 precursor p-6Y-CD247 Ig lambda chain V-II region BOH IGLV5-45(1-?) Ig heavy chain V-III region KOL IGLV3-27(1-?) Ig kappa chain V-I region Gal IGLV3-16(1-?) IGHG4 IGKVA18(21-?) CYFIP1 ARPC2 IGKV2D-30 IGLV4-60(1-?) NCKAP1 ATPIg heavy chain V-III region BRO IGLV3-16(1-?) PI(3,4,5)P3 ATP IGKV2D-30 WASF3 ABI1 Ig heavy chain V-III region WEA IGLV3-12(1-?) IGLV(23-?) Ig kappa chain V-I region Daudi IGLV2-11(1-?) IGLV4-60(1-?) Ig lambda chain V-II region BOH GDPIGLV4-3(1-?) IGLC7 Ig lambda chain V-I region NEW Ig lambda chain V-II region NEI p-Y288,Y304-FCGR2A ELMO1 Ig kappa chain V-I region AU IGLV10-54(1-?) Ig lambda chain V-IV region Kern IGLV3-12(1-?) CRK ARPC1B Ig lambda chain V-III region LOI IGKVA18(21-?) Ig kappa chain V-II region Cum 80, 87480804


Description

Phagocytosis is one of the important innate immune responses that function to eliminate invading infectious agents. Monocytes, macrophages, and neutrophils are the professional phagocytic cells. Phagocytosis is a complex process involving the recognition of invading foreign particles by specific types of phagocytic receptors and the subsequent internalization of the particles. Fc gamma receptors (FCGRs) are among the best studied phagocytic receptors that bind to Fc portion of immunoglobulin G (IgG). Through their antigen binding F(ab) end, antibodies bind to specific antigen while their constant (Fc) region binds to FCGRs on phagocytes. The clustering of FCGRs by IgG antibodies on the phagocyte initiates a variety of signals, which lead, through the reorganisation of actin cytoskeleton and membrane remodelling, to the formation of pseudopod and phagosome. Fc gamma receptors are classified into three classes: FCGRI, FCGRII and FCGRIII. Each class of these FCGRs consists of several individual isoforms. Among all these isoforms FCGRI, FCGRIIA and FCGRIIIA, are able to mediate phagocytosis (Joshi et al. 2006, Garcia Garcia & Rosales 2002, Nimmerjahn & Ravetch 2006). View original pathway at Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 2029480
Reactome-version 
Reactome version: 75
Reactome Author 
Reactome Author: Garapati, Phani Vijay

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Bibliography

View all...
  1. Crowley MT, Costello PS, Fitzer-Attas CJ, Turner M, Meng F, Lowell C, Tybulewicz VL, DeFranco AL.; ''A critical role for Syk in signal transduction and phagocytosis mediated by Fcgamma receptors on macrophages.''; PubMed Europe PMC Scholia
  2. Joshi T, Butchar JP, Tridandapani S.; ''Fcgamma receptor signaling in phagocytes.''; PubMed Europe PMC Scholia
  3. Mendoza MC, Er EE, Zhang W, Ballif BA, Elliott HL, Danuser G, Blenis J.; ''ERK-MAPK drives lamellipodia protrusion by activating the WAVE2 regulatory complex.''; PubMed Europe PMC Scholia
  4. Matsuda M, Paterson HF, Rodriguez R, Fensome AC, Ellis MV, Swann K, Katan M.; ''Real time fluorescence imaging of PLC gamma translocation and its interaction with the epidermal growth factor receptor.''; PubMed Europe PMC Scholia
  5. Suzuki T, Kono H, Hirose N, Okada M, Yamamoto T, Yamamoto K, Honda Z.; ''Differential involvement of Src family kinases in Fc gamma receptor-mediated phagocytosis.''; PubMed Europe PMC Scholia
  6. Robinson JM, Badwey JA.; ''Rapid association of cytoskeletal remodeling proteins with the developing phagosomes of human neutrophils.''; PubMed Europe PMC Scholia
  7. Durden DL, Liu YB.; ''Protein-tyrosine kinase p72syk in Fc gamma RI receptor signaling.''; PubMed Europe PMC Scholia
  8. García-García E, Rosales C.; ''Signal transduction during Fc receptor-mediated phagocytosis.''; PubMed Europe PMC Scholia
  9. Carpenter G, Ji Q.; ''Phospholipase C-gamma as a signal-transducing element.''; PubMed Europe PMC Scholia
  10. Ho HY, Rohatgi R, Ma L, Kirschner MW.; ''CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family.''; PubMed Europe PMC Scholia
  11. Suetsugu S, Kurisu S, Oikawa T, Yamazaki D, Oda A, Takenawa T.; ''Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac.''; PubMed Europe PMC Scholia
  12. Matsuda M, Park JG, Wang DC, Hunter S, Chien P, Schreiber AD.; ''Abrogation of the Fc gamma receptor IIA-mediated phagocytic signal by stem-loop Syk antisense oligonucleotides.''; PubMed Europe PMC Scholia
  13. Callebaut I, Cossart P, Dehoux P.; ''EVH1/WH1 domains of VASP and WASP proteins belong to a large family including Ran-binding domains of the RanBP1 family.''; PubMed Europe PMC Scholia
  14. Indik ZK, Hunter S, Huang MM, Pan XQ, Chien P, Kelly C, Levinson AI, Kimberly RP, Schreiber AD.; ''The high affinity Fc gamma receptor (CD64) induces phagocytosis in the absence of its cytoplasmic domain: the gamma subunit of Fc gamma RIIIA imparts phagocytic function to Fc gamma RI.''; PubMed Europe PMC Scholia
  15. Dharmawardhane S, Brownson D, Lennartz M, Bokoch GM.; ''Localization of p21-activated kinase 1 (PAK1) to pseudopodia, membrane ruffles, and phagocytic cups in activated human neutrophils.''; PubMed Europe PMC Scholia
  16. Law CL, Chandran KA, Sidorenko SP, Clark EA.; ''Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk.''; PubMed Europe PMC Scholia
  17. Leverrier Y, Okkenhaug K, Sawyer C, Bilancio A, Vanhaesebroeck B, Ridley AJ.; ''Class I phosphoinositide 3-kinase p110beta is required for apoptotic cell and Fcgamma receptor-mediated phagocytosis by macrophages.''; PubMed Europe PMC Scholia
  18. Edberg JC, Redecha PB, Salmon JE, Kimberly RP.; ''Human Fc gamma RIII (CD16). Isoforms with distinct allelic expression, extracellular domains, and membrane linkages on polymorphonuclear and natural killer cells.''; PubMed Europe PMC Scholia
  19. Kusner DJ, Hall CF, Jackson S.; ''Fc gamma receptor-mediated activation of phospholipase D regulates macrophage phagocytosis of IgG-opsonized particles.''; PubMed Europe PMC Scholia
  20. Moreau V, Frischknecht F, Reckmann I, Vincentelli R, Rabut G, Stewart D, Way M.; ''A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization.''; PubMed Europe PMC Scholia
  21. Wirthmueller U, Kurosaki T, Murakami MS, Ravetch JV.; ''Signal transduction by Fc gamma RIII (CD16) is mediated through the gamma chain.''; PubMed Europe PMC Scholia
  22. Lennartz MR.; ''Phospholipases and phagocytosis: the role of phospholipid-derived second messengers in phagocytosis.''; PubMed Europe PMC Scholia
  23. Kovar DR.; ''Arp2/3 ATP hydrolysis: to branch or to debranch?''; PubMed Europe PMC Scholia
  24. Diakonova M, Bokoch G, Swanson JA.; ''Dynamics of cytoskeletal proteins during Fcgamma receptor-mediated phagocytosis in macrophages.''; PubMed Europe PMC Scholia
  25. Fukuoka M, Suetsugu S, Miki H, Fukami K, Endo T, Takenawa T.; ''A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42.''; PubMed Europe PMC Scholia
  26. Egile C, Rouiller I, Xu XP, Volkmann N, Li R, Hanein D.; ''Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions.''; PubMed Europe PMC Scholia
  27. Koyasu S.; ''The role of PI3K in immune cells.''; PubMed Europe PMC Scholia
  28. Kato M, Miki H, Kurita S, Endo T, Nakagawa H, Miyamoto S, Takenawa T.; ''WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation.''; PubMed Europe PMC Scholia
  29. Higgs HN, Pollard TD.; ''Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex.''; PubMed Europe PMC Scholia
  30. Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK.; ''Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein.''; PubMed Europe PMC Scholia
  31. Bernard O, Ganiatsas S, Kannourakis G, Dringen R.; ''Kiz-1, a protein with LIM zinc finger and kinase domains, is expressed mainly in neurons.''; PubMed Europe PMC Scholia
  32. Dusi S, Donini M, Della Bianca V, Rossi F.; ''Tyrosine phosphorylation of phospholipase C-gamma 2 is involved in the activation of phosphoinositide hydrolysis by Fc receptors in human neutrophils.''; PubMed Europe PMC Scholia
  33. Van den Herik-Oudijk IE, Capel PJ, van der Bruggen T, Van de Winkel JG.; ''Identification of signaling motifs within human Fc gamma RIIa and Fc gamma RIIb isoforms.''; PubMed Europe PMC Scholia
  34. Beemiller P, Zhang Y, Mohan S, Levinsohn E, Gaeta I, Hoppe AD, Swanson JA.; ''A Cdc42 activation cycle coordinated by PI 3-kinase during Fc receptor-mediated phagocytosis.''; PubMed Europe PMC Scholia
  35. Duchemin AM, Ernst LK, Anderson CL.; ''Clustering of the high affinity Fc receptor for immunoglobulin G (Fc gamma RI) results in phosphorylation of its associated gamma-chain.''; PubMed Europe PMC Scholia
  36. Lennartz MR, Lefkowith JB, Bromley FA, Brown EJ.; ''Immunoglobulin G-mediated phagocytosis activates a calcium-independent, phosphatidylethanolamine-specific phospholipase.''; PubMed Europe PMC Scholia
  37. Takenawa T, Miki H.; ''WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell movement.''; PubMed Europe PMC Scholia
  38. Parrini MC, Lei M, Harrison SC, Mayer BJ.; ''Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.''; PubMed Europe PMC Scholia
  39. Carlier MF, Nioche P, Broutin-L'Hermite I, Boujemaa R, Le Clainche C, Egile C, Garbay C, Ducruix A, Sansonetti P, Pantaloni D.; ''GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex.''; PubMed Europe PMC Scholia
  40. Leng Y, Zhang J, Badour K, Arpaia E, Freeman S, Cheung P, Siu M, Siminovitch K.; ''Abelson-interactor-1 promotes WAVE2 membrane translocation and Abelson-mediated tyrosine phosphorylation required for WAVE2 activation.''; PubMed Europe PMC Scholia
  41. Edwards DC, Sanders LC, Bokoch GM, Gill GN.; ''Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics.''; PubMed Europe PMC Scholia
  42. Newton AC.; ''Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions.''; PubMed Europe PMC Scholia
  43. Cox D, Berg JS, Cammer M, Chinegwundoh JO, Dale BM, Cheney RE, Greenberg S.; ''Myosin X is a downstream effector of PI(3)K during phagocytosis.''; PubMed Europe PMC Scholia
  44. Aspenström P.; ''The WASP-binding protein WIRE has a role in the regulation of the actin filament system downstream of the platelet-derived growth factor receptor.''; PubMed Europe PMC Scholia
  45. Aizawa H, Wakatsuki S, Ishii A, Moriyama K, Sasaki Y, Ohashi K, Sekine-Aizawa Y, Sehara-Fujisawa A, Mizuno K, Goshima Y, Yahara I.; ''Phosphorylation of cofilin by LIM-kinase is necessary for semaphorin 3A-induced growth cone collapse.''; PubMed Europe PMC Scholia
  46. Huang ZY, Barreda DR, Worth RG, Indik ZK, Kim MK, Chien P, Schreiber AD.; ''Differential kinase requirements in human and mouse Fc-gamma receptor phagocytosis and endocytosis.''; PubMed Europe PMC Scholia
  47. Wu X, Suetsugu S, Cooper LA, Takenawa T, Guan JL.; ''Focal adhesion kinase regulation of N-WASP subcellular localization and function.''; PubMed Europe PMC Scholia
  48. Knaus UG, Wang Y, Reilly AM, Warnock D, Jackson JH.; ''Structural requirements for PAK activation by Rac GTPases.''; PubMed Europe PMC Scholia
  49. Bernard O.; ''Lim kinases, regulators of actin dynamics.''; PubMed Europe PMC Scholia
  50. Marshall JG, Booth JW, Stambolic V, Mak T, Balla T, Schreiber AD, Meyer T, Grinstein S.; ''Restricted accumulation of phosphatidylinositol 3-kinase products in a plasmalemmal subdomain during Fc gamma receptor-mediated phagocytosis.''; PubMed Europe PMC Scholia
  51. Indik ZK, Park JG, Hunter S, Schreiber AD.; ''The molecular dissection of Fc gamma receptor mediated phagocytosis.''; PubMed Europe PMC Scholia
  52. Huang MM, Indik Z, Brass LF, Hoxie JA, Schreiber AD, Brugge JS.; ''Activation of Fc gamma RII induces tyrosine phosphorylation of multiple proteins including Fc gamma RII.''; PubMed Europe PMC Scholia
  53. Rohatgi R, Ma L, Miki H, Lopez M, Kirchhausen T, Takenawa T, Kirschner MW.; ''The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly.''; PubMed Europe PMC Scholia
  54. Bompard G, Caron E.; ''Regulation of WASP/WAVE proteins: making a long story short.''; PubMed Europe PMC Scholia
  55. Iyer SS, Barton JA, Bourgoin S, Kusner DJ.; ''Phospholipases D1 and D2 coordinately regulate macrophage phagocytosis.''; PubMed Europe PMC Scholia
  56. Lee WL, Cosio G, Ireton K, Grinstein S.; ''Role of CrkII in Fcgamma receptor-mediated phagocytosis.''; PubMed Europe PMC Scholia
  57. Tay HK, Melendez AJ.; ''Fcgamma RI-triggered generation of arachidonic acid and eicosanoids requires iPLA2 but not cPLA2 in human monocytic cells.''; PubMed Europe PMC Scholia
  58. Rohatgi R, Nollau P, Ho HY, Kirschner MW, Mayer BJ.; ''Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway.''; PubMed Europe PMC Scholia
  59. Li R, Soosairajah J, Harari D, Citri A, Price J, Ng HL, Morton CJ, Parker MW, Yarden Y, Bernard O.; ''Hsp90 increases LIM kinase activity by promoting its homo-dimerization.''; PubMed Europe PMC Scholia
  60. Miki H, Suetsugu S, Takenawa T.; ''WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac.''; PubMed Europe PMC Scholia
  61. Chong C, Tan L, Lim L, Manser E.; ''The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.''; PubMed Europe PMC Scholia
  62. Nakanishi O, Suetsugu S, Yamazaki D, Takenawa T.; ''Effect of WAVE2 phosphorylation on activation of the Arp2/3 complex.''; PubMed Europe PMC Scholia
  63. Corrotte M, Chasserot-Golaz S, Huang P, Du G, Ktistakis NT, Frohman MA, Vitale N, Bader MF, Grant NJ.; ''Dynamics and function of phospholipase D and phosphatidic acid during phagocytosis.''; PubMed Europe PMC Scholia
  64. Mitchell MA, Huang MM, Chien P, Indik ZK, Pan XQ, Schreiber AD.; ''Substitutions and deletions in the cytoplasmic domain of the phagocytic receptor Fc gamma RIIA: effect on receptor tyrosine phosphorylation and phagocytosis.''; PubMed Europe PMC Scholia
  65. Le Clainche C, Pantaloni D, Carlier MF.; ''ATP hydrolysis on actin-related protein 2/3 complex causes debranching of dendritic actin arrays.''; PubMed Europe PMC Scholia
  66. Deckert M, Tartare-Deckert S, Couture C, Mustelin T, Altman A.; ''Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product.''; PubMed Europe PMC Scholia
  67. Massol P, Montcourrier P, Guillemot JC, Chavrier P.; ''Fc receptor-mediated phagocytosis requires CDC42 and Rac1.''; PubMed Europe PMC Scholia
  68. Xu X, Chong AS.; ''Vav in natural killer cells is tyrosine phosphorylated upon cross-linking of Fc gamma RIIIA and is constitutively associated with a serine/threonine kinase.''; PubMed Europe PMC Scholia
  69. Scott CC, Dobson W, Botelho RJ, Coady-Osberg N, Chavrier P, Knecht DA, Heath C, Stahl P, Grinstein S.; ''Phosphatidylinositol-4,5-bisphosphate hydrolysis directs actin remodeling during phagocytosis.''; PubMed Europe PMC Scholia
  70. Park H, Cox D.; ''Cdc42 regulates Fc gamma receptor-mediated phagocytosis through the activation and phosphorylation of Wiskott-Aldrich syndrome protein (WASP) and neural-WASP.''; PubMed Europe PMC Scholia
  71. Mullins RD, Heuser JA, Pollard TD.; ''The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments.''; PubMed Europe PMC Scholia
  72. Kiener PA, Rankin BM, Burkhardt AL, Schieven GL, Gilliland LK, Rowley RB, Bolen JB, Ledbetter JA.; ''Cross-linking of Fc gamma receptor I (Fc gamma RI) and receptor II (Fc gamma RII) on monocytic cells activates a signal transduction pathway common to both Fc receptors that involves the stimulation of p72 Syk protein tyrosine kinase.''; PubMed Europe PMC Scholia
  73. Chavrier P.; ''May the force be with you: Myosin-X in phagocytosis.''; PubMed Europe PMC Scholia
  74. Hall AB, Gakidis MA, Glogauer M, Wilsbacher JL, Gao S, Swat W, Brugge JS.; ''Requirements for Vav guanine nucleotide exchange factors and Rho GTPases in FcgammaR- and complement-mediated phagocytosis.''; PubMed Europe PMC Scholia
  75. Moon KD, Post CB, Durden DL, Zhou Q, De P, Harrison ML, Geahlen RL.; ''Molecular basis for a direct interaction between the Syk protein-tyrosine kinase and phosphoinositide 3-kinase.''; PubMed Europe PMC Scholia
  76. Wang QJ.; ''PKD at the crossroads of DAG and PKC signaling.''; PubMed Europe PMC Scholia
  77. Amann KJ, Pollard TD.; ''The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments.''; PubMed Europe PMC Scholia
  78. Nimmerjahn F, Ravetch JV.; ''Fcgamma receptors: old friends and new family members.''; PubMed Europe PMC Scholia
  79. Agarwal A, Salem P, Robbins KC.; ''Involvement of p72syk, a protein-tyrosine kinase, in Fc gamma receptor signaling.''; PubMed Europe PMC Scholia
  80. Kim YJ, Sekiya F, Poulin B, Bae YS, Rhee SG.; ''Mechanism of B-cell receptor-induced phosphorylation and activation of phospholipase C-gamma2.''; PubMed Europe PMC Scholia
  81. Millard TH, Sharp SJ, Machesky LM.; ''Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex.''; PubMed Europe PMC Scholia
  82. Le Clainche C, Carlier MF.; ''Regulation of actin assembly associated with protrusion and adhesion in cell migration.''; PubMed Europe PMC Scholia
  83. Ernst LK, Duchemin AM, Anderson CL.; ''Association of the high-affinity receptor for IgG (Fc gamma RI) with the gamma subunit of the IgE receptor.''; PubMed Europe PMC Scholia
  84. Tsang E, Giannetti AM, Shaw D, Dinh M, Tse JK, Gandhi S, Ho H, Wang S, Papp E, Bradshaw JM.; ''Molecular mechanism of the Syk activation switch.''; PubMed Europe PMC Scholia
  85. Swanson JA, Johnson MT, Beningo K, Post P, Mooseker M, Araki N.; ''A contractile activity that closes phagosomes in macrophages.''; PubMed Europe PMC Scholia
  86. Takeuchi M, Harigai M, Momohara S, Ball E, Abe J, Furuichi K, Kamatani N.; ''Cloning and characterization of DPPL1 and DPPL2, representatives of a novel type of mammalian phosphatidate phosphatase.''; PubMed Europe PMC Scholia
  87. Sekiya F, Poulin B, Kim YJ, Rhee SG.; ''Mechanism of tyrosine phosphorylation and activation of phospholipase C-gamma 1. Tyrosine 783 phosphorylation is not sufficient for lipase activation.''; PubMed Europe PMC Scholia
  88. Zalevsky J, Lempert L, Kranitz H, Mullins RD.; ''Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities.''; PubMed Europe PMC Scholia
  89. Brooks DG, Qiu WQ, Luster AD, Ravetch JV.; ''Structure and expression of human IgG FcRII(CD32). Functional heterogeneity is encoded by the alternatively spliced products of multiple genes.''; PubMed Europe PMC Scholia
  90. Strzelecka A, Kwiatkowska K, Sobota A.; ''Tyrosine phosphorylation and Fcgamma receptor-mediated phagocytosis.''; PubMed Europe PMC Scholia
  91. Ghazizadeh S, Bolen JB, Fleit HB.; ''Tyrosine phosphorylation and association of Syk with Fc gamma RII in monocytic THP-1 cells.''; PubMed Europe PMC Scholia
  92. Cory GO, Garg R, Cramer R, Ridley AJ.; ''Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein.''; PubMed Europe PMC Scholia
  93. van Vugt MJ, Heijnen IA, Capel PJ, Park SY, Ra C, Saito T, Verbeek JS, van de Winkel JG.; ''FcR gamma-chain is essential for both surface expression and function of human Fc gamma RI (CD64) in vivo.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
118475view20:32, 27 May 2021FinterlyRemoved incorrect and duplicated openControlledVocabulary PW:0000234
114947view16:47, 25 January 2021ReactomeTeamReactome version 75
113391view11:46, 2 November 2020ReactomeTeamReactome version 74
112853view13:31, 12 October 2020DeSlFixing ontology tag error
112849view13:02, 12 October 2020DeSlOntology Term : 'innate immune response pathway' added !
112596view15:57, 9 October 2020ReactomeTeamReactome version 73
101512view11:37, 1 November 2018ReactomeTeamreactome version 66
101048view21:19, 31 October 2018ReactomeTeamreactome version 65
100579view19:52, 31 October 2018ReactomeTeamreactome version 64
100128view16:38, 31 October 2018ReactomeTeamreactome version 63
99678view15:07, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99271view12:45, 31 October 2018ReactomeTeamreactome version 62
94053view13:54, 16 August 2017ReactomeTeamreactome version 61
93681view11:30, 9 August 2017ReactomeTeamreactome version 61
89466view13:21, 15 September 2016Mkutmonfix ontology tag annotation
87448view13:50, 22 July 2016MkutmonOntology Term : 'PW:0000234' added !
86805view09:26, 11 July 2016ReactomeTeamreactome version 56
83122view10:02, 18 November 2015ReactomeTeamVersion54
81461view12:59, 21 August 2015ReactomeTeamVersion53
76936view08:20, 17 July 2014ReactomeTeamFixed remaining interactions
76641view12:01, 16 July 2014ReactomeTeamFixed remaining interactions
75971view10:02, 11 June 2014ReactomeTeamRe-fixing comment source
75674view10:59, 10 June 2014ReactomeTeamReactome 48 Update
75029view13:54, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74673view08:44, 30 April 2014ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
ABI1 ProteinQ8IZP0 (Uniprot-TrEMBL)
ABI2 ProteinQ9NYB9 (Uniprot-TrEMBL)
ABL1ProteinP00519 (Uniprot-TrEMBL)
ACTB(1-375) ProteinP60709 (Uniprot-TrEMBL)
ACTG1 ProteinP63261 (Uniprot-TrEMBL)
ACTR2 ProteinP61160 (Uniprot-TrEMBL)
ACTR3 ProteinP61158 (Uniprot-TrEMBL)
ADP MetaboliteCHEBI:456216 (ChEBI)
ADPMetaboliteCHEBI:456216 (ChEBI)
AHCYL1 ProteinO43865 (Uniprot-TrEMBL)
AHCYL1:NAD+:ITPR1:I(1,4,5)P3 tetramerComplexR-HSA-5226920 (Reactome)
ARAMetaboliteCHEBI:15843 (ChEBI)
ARP2/3 complex (ATP bound)ComplexR-HSA-1861670 (Reactome)
ARPC1A ProteinQ92747 (Uniprot-TrEMBL)
ARPC1B ProteinO15143 (Uniprot-TrEMBL)
ARPC2 ProteinO15144 (Uniprot-TrEMBL)
ARPC3 ProteinO15145 (Uniprot-TrEMBL)
ARPC4 ProteinP59998 (Uniprot-TrEMBL)
ARPC5 ProteinO15511 (Uniprot-TrEMBL)
ATP MetaboliteCHEBI:30616 (ChEBI)
ATPMetaboliteCHEBI:30616 (ChEBI)
Actin filament bound Myosin-XComplexR-HSA-1861625 (Reactome)
Active LIMK1ComplexR-HSA-419630 (Reactome)
Antigen R-ALL-173548 (Reactome)
Antigen:IgGComplexR-HSA-173552 (Reactome)
BAIAP2 ProteinQ9UQB8 (Uniprot-TrEMBL)
BAIAP2ProteinQ9UQB8 (Uniprot-TrEMBL)
BRK1 ProteinQ8WUW1 (Uniprot-TrEMBL)
BTK ProteinQ06187 (Uniprot-TrEMBL)
CD247-1 ProteinP20963-1 (Uniprot-TrEMBL)
CD3G ProteinP09693 (Uniprot-TrEMBL)
CDC42 ProteinP60953 (Uniprot-TrEMBL)
CDC42:GDPComplexR-HSA-418830 (Reactome)
CDC42:GTP, RAC1:GTPComplexR-HSA-389778 (Reactome)
CDC42:GTP:WASP/N-WASP:WIP:SH3 proteinsComplexR-HSA-2197683 (Reactome)
CDC42:GTP:WASP/N-WASPComplexR-HSA-442584 (Reactome)
CDC42:GTP:p-Y-WASP/p-Y-WASL:WIP:SH3 proteinsComplexR-HSA-2197680 (Reactome)
CDC42:GTPComplexR-HSA-182921 (Reactome)
CFL1ProteinP23528 (Uniprot-TrEMBL)
CRK ProteinP46108 (Uniprot-TrEMBL)
CRK:DOCK180:ELMO1,ELMO2ComplexR-HSA-2029141 (Reactome)
CRKII:DOCK180:ELMO

complex recruited

to phagocytic cup		ComplexR-HSA-2029130 (Reactome)
CYFIP1 ProteinQ7L576 (Uniprot-TrEMBL)
CYFIP2 ProteinQ96F07 (Uniprot-TrEMBL)
Ca2+MetaboliteCHEBI:29108 (ChEBI)
ChoMetaboliteCHEBI:15354 (ChEBI)
DAGsMetaboliteCHEBI:18035 (ChEBI)
DOCK1 ProteinQ14185 (Uniprot-TrEMBL)
ELMO1 ProteinQ92556 (Uniprot-TrEMBL)
ELMO2 ProteinQ96JJ3 (Uniprot-TrEMBL)
F-actin R-HSA-201877 (Reactome)
F-actinR-HSA-201877 (Reactome)
FCGR1A ProteinP12314 (Uniprot-TrEMBL)
FCGR2A ProteinP12318 (Uniprot-TrEMBL)
FCGR2AProteinP12318 (Uniprot-TrEMBL)
FCGR3A ProteinP08637 (Uniprot-TrEMBL)
FCGRIA:CD3G homodimerComplexR-HSA-2029093 (Reactome)
FCGRIIIA:CD3G/CD3Z dimersComplexR-HSA-2029097 (Reactome)
FGR ProteinP09769 (Uniprot-TrEMBL)
FYN ProteinP06241 (Uniprot-TrEMBL)
G-actinComplexR-HSA-201857 (Reactome)
GDP MetaboliteCHEBI:17552 (ChEBI)
GDPMetaboliteCHEBI:17552 (ChEBI)
GRB2-1 ProteinP62993-1 (Uniprot-TrEMBL)
GTP MetaboliteCHEBI:15996 (ChEBI)
GTPMetaboliteCHEBI:15996 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HCK ProteinP08631 (Uniprot-TrEMBL)
HSP90AA1 ProteinP07900 (Uniprot-TrEMBL)
HSP90AA1,HSP90AB1ComplexR-HSA-419619 (Reactome)
HSP90AB1 ProteinP08238 (Uniprot-TrEMBL)
I(1,4,5)P3 MetaboliteCHEBI:16595 (ChEBI)
I(1,4,5)P3MetaboliteCHEBI:16595 (ChEBI)
IGHG1 ProteinP01857 (Uniprot-TrEMBL)
IGHG2 ProteinP01859 (Uniprot-TrEMBL)
IGHG3 ProteinP01860 (Uniprot-TrEMBL)
IGHG4 ProteinP01861 (Uniprot-TrEMBL)
IGHV(1-?) ProteinA2KUC3 (Uniprot-TrEMBL)
IGHV1-2 ProteinP23083 (Uniprot-TrEMBL)
IGHV7-81(1-?) ProteinQ6PIL0 (Uniprot-TrEMBL)
IGKC ProteinP01834 (Uniprot-TrEMBL)
IGKV1-12 ProteinA0A0C4DH73 (Uniprot-TrEMBL)
IGKV1-5(23-?) ProteinP01602 (Uniprot-TrEMBL)
IGKV2-28 ProteinA0A075B6P5 (Uniprot-TrEMBL)
IGKV2D-30 ProteinA0A075B6S6 (Uniprot-TrEMBL)
IGKV3D-20 ProteinA0A0C4DH25 (Uniprot-TrEMBL)
IGKV4-1(21-?) ProteinP06312 (Uniprot-TrEMBL)
IGKVA18(21-?) ProteinA2NJV5 (Uniprot-TrEMBL)
IGLC1 ProteinP0CG04 (Uniprot-TrEMBL)
IGLC2 ProteinP0DOY2 (Uniprot-TrEMBL)
IGLC3 ProteinP0DOY3 (Uniprot-TrEMBL)
IGLC6 ProteinP0CF74 (Uniprot-TrEMBL)
IGLC7 ProteinA0M8Q6 (Uniprot-TrEMBL)
IGLV(23-?) ProteinA2NXD2 (Uniprot-TrEMBL)
IGLV1-36(1-?) ProteinQ5NV67 (Uniprot-TrEMBL)
IGLV1-40(1-?) ProteinQ5NV69 (Uniprot-TrEMBL)
IGLV1-44(1-?) ProteinQ5NV81 (Uniprot-TrEMBL)
IGLV10-54(1-?) ProteinQ5NV86 (Uniprot-TrEMBL)
IGLV11-55(1-?) ProteinQ5NV87 (Uniprot-TrEMBL)
IGLV2-11(1-?) ProteinQ5NV84 (Uniprot-TrEMBL)
IGLV2-18(1-?) ProteinQ5NV65 (Uniprot-TrEMBL)
IGLV2-23(1-?) ProteinQ5NV89 (Uniprot-TrEMBL)
IGLV2-33(1-?) ProteinQ5NV66 (Uniprot-TrEMBL)
IGLV3-12(1-?) ProteinQ5NV85 (Uniprot-TrEMBL)
IGLV3-16(1-?) ProteinQ5NV64 (Uniprot-TrEMBL)
IGLV3-22(1-?) ProteinQ5NV75 (Uniprot-TrEMBL)
IGLV3-25(1-?) ProteinQ5NV90 (Uniprot-TrEMBL)
IGLV3-27(1-?) ProteinQ5NV91 (Uniprot-TrEMBL)
IGLV4-3(1-?) ProteinQ5NV61 (Uniprot-TrEMBL)
IGLV4-60(1-?) ProteinQ5NV79 (Uniprot-TrEMBL)
IGLV4-69(1-?) ProteinQ5NV92 (Uniprot-TrEMBL)
IGLV5-37(1-?) ProteinQ5NV68 (Uniprot-TrEMBL)
IGLV5-45(1-?) ProteinQ5NV82 (Uniprot-TrEMBL)
IGLV7-43(1-?) ProteinQ5NV80 (Uniprot-TrEMBL)
IGLV7-46(1-?) ProteinQ5NV83 (Uniprot-TrEMBL)
IGLV8-61(1-?) ProteinQ5NV62 (Uniprot-TrEMBL)
IP3 receptor homotetramerComplexR-HSA-169686 (Reactome)
ITPR1 ProteinQ14643 (Uniprot-TrEMBL)
ITPR2 ProteinQ14571 (Uniprot-TrEMBL)
ITPR3 ProteinQ14573 (Uniprot-TrEMBL)
ITPR:I(1,4,5)P3 tetramerComplexR-HSA-169696 (Reactome)
Ig heavy chain V-I region EU ProteinP01742 (Uniprot-TrEMBL)
Ig heavy chain V-I region HG3 ProteinP01743 (Uniprot-TrEMBL)
Ig heavy chain V-II region ARH-77 ProteinP06331 (Uniprot-TrEMBL)
Ig heavy chain V-II region MCE ProteinP01817 (Uniprot-TrEMBL)
Ig heavy chain V-II region NEWM ProteinP01825 (Uniprot-TrEMBL)
Ig heavy chain V-II region OU ProteinP01814 (Uniprot-TrEMBL)
Ig heavy chain V-II region WAH ProteinP01824 (Uniprot-TrEMBL)
Ig heavy chain V-III region BRO ProteinP01766 (Uniprot-TrEMBL)
Ig heavy chain V-III region BUT ProteinP01767 (Uniprot-TrEMBL)
Ig heavy chain V-III region CAM ProteinP01768 (Uniprot-TrEMBL)
Ig heavy chain V-III region DOB ProteinP01782 (Uniprot-TrEMBL)
Ig heavy chain V-III region JON ProteinP01780 (Uniprot-TrEMBL)
Ig heavy chain V-III region KOL ProteinP01772 (Uniprot-TrEMBL)
Ig heavy chain V-III region TRO ProteinP01762 (Uniprot-TrEMBL)
Ig heavy chain V-III region WEA ProteinP01763 (Uniprot-TrEMBL)
Ig kappa chain V region EV15 ProteinP06315 (Uniprot-TrEMBL)
Ig kappa chain V-I region AG ProteinP01593 (Uniprot-TrEMBL)
Ig kappa chain V-I region AU ProteinP01594 (Uniprot-TrEMBL)
Ig kappa chain V-I region BAN ProteinP04430 (Uniprot-TrEMBL)
Ig kappa chain V-I region DEE ProteinP01597 (Uniprot-TrEMBL)
Ig kappa chain V-I region Daudi ProteinP04432 (Uniprot-TrEMBL)
Ig kappa chain V-I region Gal ProteinP01599 (Uniprot-TrEMBL)
Ig kappa chain V-I region HK101 ProteinP01601 (Uniprot-TrEMBL)
Ig kappa chain V-I region Wes ProteinP01611 (Uniprot-TrEMBL)
Ig kappa chain V-II region Cum ProteinP01614 (Uniprot-TrEMBL)
Ig kappa chain V-II region FR ProteinP01615 (Uniprot-TrEMBL)
Ig kappa chain V-II region RPMI 6410 ProteinP06310 (Uniprot-TrEMBL)
Ig kappa chain V-III region B6 ProteinP01619 (Uniprot-TrEMBL)
Ig kappa chain V-III region POM ProteinP01624 (Uniprot-TrEMBL)
Ig kappa chain V-III region VG ProteinP04433 (Uniprot-TrEMBL)
Ig lambda chain V region 4A ProteinP04211 (Uniprot-TrEMBL)
Ig lambda chain V-I region HA ProteinP01700 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEW ProteinP01701 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEWM ProteinP01703 (Uniprot-TrEMBL)
Ig lambda chain V-I region VOR ProteinP01699 (Uniprot-TrEMBL)
Ig lambda chain V-II region BOH ProteinP01706 (Uniprot-TrEMBL)
Ig lambda chain V-II region MGC ProteinP01709 (Uniprot-TrEMBL)
Ig lambda chain V-II region NEI ProteinP01705 (Uniprot-TrEMBL)
Ig lambda chain V-II region TOG ProteinP01704 (Uniprot-TrEMBL)
Ig lambda chain V-III region LOI ProteinP80748 (Uniprot-TrEMBL)
Ig lambda chain V-III region SH ProteinP01714 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Bau ProteinP01715 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Hil ProteinP01717 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Kern ProteinP01718 (Uniprot-TrEMBL)
Ig lambda chain V-VI region AR ProteinP01721 (Uniprot-TrEMBL)
IgG-Ag:FCGRIA:CD3G homodimerComplexR-HSA-2029132 (Reactome)
IgG-Ag:FCGRIIAComplexR-HSA-1861689 (Reactome)
IgG-Ag:FCGRIIIA:CD3G/CD3Z dimersComplexR-HSA-2029163 (Reactome)
IgH heavy chain V-III region VH26 precursor ProteinP01764 (Uniprot-TrEMBL)
LIMK1ProteinP53667 (Uniprot-TrEMBL)
LPCMetaboliteCHEBI:17504 (ChEBI)
LYN ProteinP07948 (Uniprot-TrEMBL)
MYH2 ProteinQ9UKX2 (Uniprot-TrEMBL)
MYH9 ProteinP35579 (Uniprot-TrEMBL)
MYO10 ProteinQ9HD67 (Uniprot-TrEMBL)
MYO1C ProteinO00159 (Uniprot-TrEMBL)
MYO5A ProteinQ9Y4I1 (Uniprot-TrEMBL)
MYO9B ProteinQ13459 (Uniprot-TrEMBL)
Mother filament:ARP2/3:actin:ADPComplexR-HSA-2197686 (Reactome)
Mother

filament:branching complex:daughter

filament		ComplexR-HSA-1861699 (Reactome)
Mother

filament:branching

complex		ComplexR-HSA-2029140 (Reactome)
Myosin-Actin filamentsComplexR-HSA-2029139 (Reactome)
Myosin-X dimerComplexR-HSA-1861665 (Reactome)
MyosinComplexR-HSA-2029109 (Reactome)
N-WASP ProteinO00401 (Uniprot-TrEMBL)
NAD+ MetaboliteCHEBI:57540 (ChEBI)
NCK1 ProteinP16333 (Uniprot-TrEMBL)
NCKAP1 ProteinQ9Y2A7 (Uniprot-TrEMBL)
NCKAP1L ProteinP55160 (Uniprot-TrEMBL)
NCKIPSD ProteinQ9NZQ3 (Uniprot-TrEMBL)
NF2ProteinP35240 (Uniprot-TrEMBL)
PAMetaboliteCHEBI:16337 (ChEBI)
PAK1 ProteinQ13153 (Uniprot-TrEMBL)
PAK1 dimerComplexR-HSA-445002 (Reactome)
PAK1ProteinQ13153 (Uniprot-TrEMBL)
PCMetaboliteCHEBI:16110 (ChEBI)
PI(3,4)P2 MetaboliteCHEBI:16152 (ChEBI)
PI(3,4)P2MetaboliteCHEBI:16152 (ChEBI)
PI(3,4,5)P3 MetaboliteCHEBI:16618 (ChEBI)
PI(3,4,5)P3MetaboliteCHEBI:16618 (ChEBI)
PI(4,5)P2 MetaboliteCHEBI:18348 (ChEBI)
PI(4,5)P2MetaboliteCHEBI:18348 (ChEBI)
PI3K:p-6Y-SYKComplexR-HSA-2029149 (Reactome)
PI3KComplexR-HSA-74693 (Reactome)
PIK3CA ProteinP42336 (Uniprot-TrEMBL)
PIK3CB ProteinP42338 (Uniprot-TrEMBL)
PIK3R1 ProteinP27986 (Uniprot-TrEMBL)
PIK3R2 ProteinO00459 (Uniprot-TrEMBL)
PKC-delta/epsilonComplexR-HSA-198276 (Reactome)
PLA2G6ProteinO60733 (Uniprot-TrEMBL)
PLC gamma1,2ComplexR-HSA-1169089 (Reactome)
PLCG1 ProteinP19174 (Uniprot-TrEMBL)
PLCG2 ProteinP16885 (Uniprot-TrEMBL)
PLD1 ProteinQ13393 (Uniprot-TrEMBL)
PLD2 ProteinO14939 (Uniprot-TrEMBL)
PLD3 ProteinQ8IV08 (Uniprot-TrEMBL)
PLD4 ProteinQ96BZ4 (Uniprot-TrEMBL)
PLDComplexR-HSA-2029102 (Reactome)
PPAPDC1A ProteinQ5VZY2 (Uniprot-TrEMBL)
PPAPDC1B ProteinQ8NEB5 (Uniprot-TrEMBL)
PRKCD ProteinQ05655 (Uniprot-TrEMBL)
PRKCE ProteinQ02156 (Uniprot-TrEMBL)
PTK2 ProteinQ05397 (Uniprot-TrEMBL)
Phosphatidate phosphataseComplexR-HSA-2029101 (Reactome)
Phospho-PKC-delta/epsilonComplexR-HSA-198265 (Reactome)
PiMetaboliteCHEBI:43474 (ChEBI)
RAC1 ProteinP63000 (Uniprot-TrEMBL)
RAC1:GDPComplexR-HSA-5674631 (Reactome)
RAC1:GTP,CDC42:GTP:PAK1ComplexR-HSA-2029159 (Reactome)
RAC1:GTPComplexR-HSA-442641 (Reactome)
SH3 domain proteinsComplexR-HSA-2197679 (Reactome)
SRC-1 ProteinP12931-1 (Uniprot-TrEMBL)
SYK ProteinP43405 (Uniprot-TrEMBL)
SYKProteinP43405 (Uniprot-TrEMBL)
Src family kinases (SFKs)ComplexR-HSA-1861597 (Reactome)
Src-kinasesComplexR-HSA-2197681 (Reactome)
Unknown GEFR-HSA-8939797 (Reactome)
VAV1 ProteinP15498 (Uniprot-TrEMBL)
VAV1,2,3ComplexR-HSA-430172 (Reactome)
VAV2 ProteinP52735 (Uniprot-TrEMBL)
VAV3 ProteinQ9UKW4 (Uniprot-TrEMBL)
WAS ProteinP42768 (Uniprot-TrEMBL)
WASF1 ProteinQ92558 (Uniprot-TrEMBL)
WASF2 ProteinQ9Y6W5 (Uniprot-TrEMBL)
WASF3 ProteinQ9UPY6 (Uniprot-TrEMBL)
WASP/N-WASPComplexR-HSA-201892 (Reactome)
WAVE Regulatory ComplexComplexR-HSA-2029154 (Reactome)
WAVE2, WASP,

N-WASP:ARP2/3

complex:G-actin		ComplexR-HSA-442565 (Reactome)
WAVE2, WASP, N-WASPComplexR-HSA-2197675 (Reactome)
WIP family proteinsComplexR-HSA-2197678 (Reactome)
WIPF1 ProteinO43516 (Uniprot-TrEMBL)
WIPF2 ProteinQ8TF74 (Uniprot-TrEMBL)
WIPF3 ProteinA6NGB9 (Uniprot-TrEMBL)
WRC:IRSp53/58:RAC1:GTP:PIP3ComplexR-HSA-2029147 (Reactome)
YES1 ProteinP07947 (Uniprot-TrEMBL)
clustered IgG-Ag:FCGRsComplexR-HSA-2029146 (Reactome)
clustered IgG-Ag:p-FCGRs:SYKComplexR-HSA-2029129 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:PLCGComplexR-HSA-2029137 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:VAVComplexR-HSA-2029133 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:p-3Y-PLCGComplexR-HSA-2029156 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:p-VAVComplexR-HSA-2029131 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYKComplexR-HSA-2029158 (Reactome)
clustered IgG-Ag:p-FCGRsComplexR-HSA-2029128 (Reactome)
clustered IgG-Ag:p-FCGRsComplexR-HSA-2029151 (Reactome)
p-4S-ABI2 ProteinQ9NYB9 (Uniprot-TrEMBL)
p-4Y-PLCG1 ProteinP19174 (Uniprot-TrEMBL)
p-4Y-PLCG1ProteinP19174 (Uniprot-TrEMBL)
p-5S-ABI1 ProteinQ8IZP0 (Uniprot-TrEMBL)
p-6Y-CD247 ProteinP20963-1 (Uniprot-TrEMBL)
p-6Y-SYK ProteinP43405 (Uniprot-TrEMBL)
p-PLCGComplexR-HSA-2029095 (Reactome)
p-S,T508-LIMK1 ProteinP53667 (Uniprot-TrEMBL)
p-S144,T423-PAK1ProteinQ13153 (Uniprot-TrEMBL)
p-S3-CFL1 ProteinP23528 (Uniprot-TrEMBL)
p-T,Y MAPK dimersComplexR-HSA-1268261 (Reactome)
p-T185,Y187-MAPK1 ProteinP28482 (Uniprot-TrEMBL)
p-T202,Y204-MAPK3 ProteinP27361 (Uniprot-TrEMBL)
p-T507,S645,S664-PRKCD(1-676) ProteinQ05655 (Uniprot-TrEMBL)
p-T508-LIMK1 ProteinP53667 (Uniprot-TrEMBL)
p-T508-LIMK1ProteinP53667 (Uniprot-TrEMBL)
p-T566,T710,S729-PRKCE ProteinQ02156 (Uniprot-TrEMBL)
p-Y,S,T-WRC:IRSp53/58:RAC1:GTP:PIP3ComplexR-HSA-2029148 (Reactome)
p-Y-WRC:IRSp53/58:RAC1:GTP:PIP3ComplexR-HSA-2130182 (Reactome)
p-Y150,S343,T346-WASF2 ProteinQ9Y6W5 (Uniprot-TrEMBL)
p-Y150-WASF2 ProteinQ9Y6W5 (Uniprot-TrEMBL)
p-Y151,S,T-WASF1 ProteinQ92558 (Uniprot-TrEMBL)
p-Y151,S,T-WASF3 ProteinQ9UPY6 (Uniprot-TrEMBL)
p-Y151-WASF1 ProteinQ92558 (Uniprot-TrEMBL)
p-Y151-WASF3 ProteinQ9UPY6 (Uniprot-TrEMBL)
p-Y160,Y171-CD3G ProteinP09693 (Uniprot-TrEMBL)
p-Y172-VAV2 ProteinP52735 (Uniprot-TrEMBL)
p-Y173-VAV3 ProteinQ9UKW4 (Uniprot-TrEMBL)
p-Y174-VAV1 ProteinP15498 (Uniprot-TrEMBL)
p-Y256-WASL ProteinO00401 (Uniprot-TrEMBL)
p-Y288,Y304-FCGR2A ProteinP12318 (Uniprot-TrEMBL)
p-Y291-WAS ProteinP42768 (Uniprot-TrEMBL)
p-Y753,Y759,Y1217-PLCG2 ProteinP16885 (Uniprot-TrEMBL)
pCofilin: Active LIMK-1ComplexR-HSA-399878 (Reactome)
pLIMK dimer:HSP-90ComplexR-HSA-419632 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
ABL1mim-catalysisR-HSA-2130194 (Reactome)
ADPArrowR-HSA-198314 (Reactome)
ADPArrowR-HSA-2029268 (Reactome)
ADPArrowR-HSA-2029271 (Reactome)
ADPArrowR-HSA-2029449 (Reactome)
ADPArrowR-HSA-2029453 (Reactome)
ADPArrowR-HSA-2029454 (Reactome)
ADPArrowR-HSA-2029459 (Reactome)
ADPArrowR-HSA-2029460 (Reactome)
ADPArrowR-HSA-2029469 (Reactome)
ADPArrowR-HSA-2130194 (Reactome)
ADPArrowR-HSA-2197698 (Reactome)
ADPArrowR-HSA-399950 (Reactome)
ADPArrowR-HSA-419644 (Reactome)
AHCYL1:NAD+:ITPR1:I(1,4,5)P3 tetramerTBarR-HSA-169683 (Reactome)
ARAArrowR-HSA-2029475 (Reactome)
ARP2/3 complex (ATP bound)R-HSA-442592 (Reactome)
ATPR-HSA-1861595 (Reactome)
ATPR-HSA-198314 (Reactome)
ATPR-HSA-2029268 (Reactome)
ATPR-HSA-2029271 (Reactome)
ATPR-HSA-2029449 (Reactome)
ATPR-HSA-2029453 (Reactome)
ATPR-HSA-2029454 (Reactome)
ATPR-HSA-2029459 (Reactome)
ATPR-HSA-2029460 (Reactome)
ATPR-HSA-2029469 (Reactome)
ATPR-HSA-2029476 (Reactome)
ATPR-HSA-2130194 (Reactome)
ATPR-HSA-2197698 (Reactome)
ATPR-HSA-399950 (Reactome)
ATPR-HSA-419644 (Reactome)
Actin filament bound Myosin-XArrowR-HSA-1861595 (Reactome)
Active LIMK1ArrowR-HSA-419644 (Reactome)
Active LIMK1R-HSA-399950 (Reactome)
Active LIMK1mim-catalysisR-HSA-399950 (Reactome)
Antigen:IgGR-HSA-1861621 (Reactome)
Antigen:IgGR-HSA-2029455 (Reactome)
Antigen:IgGR-HSA-2029457 (Reactome)
BAIAP2R-HSA-2029465 (Reactome)
CDC42:GDPR-HSA-2029445 (Reactome)
CDC42:GTP, RAC1:GTPArrowR-HSA-2029454 (Reactome)
CDC42:GTP, RAC1:GTPR-HSA-2029456 (Reactome)
CDC42:GTP:WASP/N-WASP:WIP:SH3 proteinsArrowR-HSA-2197691 (Reactome)
CDC42:GTP:WASP/N-WASP:WIP:SH3 proteinsR-HSA-2197698 (Reactome)
CDC42:GTP:WASP/N-WASPArrowR-HSA-442586 (Reactome)
CDC42:GTP:WASP/N-WASPR-HSA-2197691 (Reactome)
CDC42:GTP:p-Y-WASP/p-Y-WASL:WIP:SH3 proteinsArrowR-HSA-2197698 (Reactome)
CDC42:GTPArrowR-HSA-2029445 (Reactome)
CDC42:GTPR-HSA-442586 (Reactome)
CFL1R-HSA-399950 (Reactome)
CRK:DOCK180:ELMO1,ELMO2R-HSA-2197697 (Reactome)
CRKII:DOCK180:ELMO

complex recruited

to phagocytic cup		ArrowR-HSA-2197697 (Reactome)
CRKII:DOCK180:ELMO

complex recruited

to phagocytic cup		mim-catalysisR-HSA-2029467 (Reactome)
Ca2+ArrowR-HSA-169683 (Reactome)
Ca2+R-HSA-169683 (Reactome)
ChoArrowR-HSA-2029471 (Reactome)
DAGsArrowR-HSA-167686 (Reactome)
DAGsArrowR-HSA-198314 (Reactome)
DAGsArrowR-HSA-2029468 (Reactome)
F-actinR-HSA-2029466 (Reactome)
FCGR2AR-HSA-1861621 (Reactome)
FCGRIA:CD3G homodimerR-HSA-2029455 (Reactome)
FCGRIIIA:CD3G/CD3Z dimersR-HSA-2029457 (Reactome)
G-actinR-HSA-2029473 (Reactome)
G-actinR-HSA-442592 (Reactome)
GDPArrowR-HSA-2029445 (Reactome)
GDPArrowR-HSA-2029451 (Reactome)
GDPArrowR-HSA-2029467 (Reactome)
GTPR-HSA-2029445 (Reactome)
GTPR-HSA-2029451 (Reactome)
GTPR-HSA-2029467 (Reactome)
H2OR-HSA-167686 (Reactome)
H2OR-HSA-2029468 (Reactome)
H2OR-HSA-2029471 (Reactome)
H2OR-HSA-2029475 (Reactome)
HSP90AA1,HSP90AB1ArrowR-HSA-419644 (Reactome)
HSP90AA1,HSP90AB1R-HSA-419645 (Reactome)
I(1,4,5)P3ArrowR-HSA-167686 (Reactome)
I(1,4,5)P3ArrowR-HSA-169683 (Reactome)
I(1,4,5)P3R-HSA-169680 (Reactome)
IP3 receptor homotetramerR-HSA-169680 (Reactome)
ITPR:I(1,4,5)P3 tetramerArrowR-HSA-169680 (Reactome)
ITPR:I(1,4,5)P3 tetramermim-catalysisR-HSA-169683 (Reactome)
IgG-Ag:FCGRIA:CD3G homodimerArrowR-HSA-2029455 (Reactome)
IgG-Ag:FCGRIIAArrowR-HSA-1861621 (Reactome)
IgG-Ag:FCGRIIIA:CD3G/CD3Z dimersArrowR-HSA-2029457 (Reactome)
LIMK1R-HSA-2029460 (Reactome)
LPCArrowR-HSA-2029475 (Reactome)
Mother filament:ARP2/3:actin:ADPArrowR-HSA-2197690 (Reactome)
Mother filament:ARP2/3:actin:ADPR-HSA-2029473 (Reactome)
Mother

filament:branching complex:daughter

filament		ArrowR-HSA-2029473 (Reactome)
Mother

filament:branching complex:daughter

filament		R-HSA-1861595 (Reactome)
Mother

filament:branching complex:daughter

filament		R-HSA-2029476 (Reactome)
Mother

filament:branching

complex		ArrowR-HSA-2029466 (Reactome)
Mother

filament:branching

complex		R-HSA-2197690 (Reactome)
Myosin-Actin filamentsArrowR-HSA-2029476 (Reactome)
Myosin-X dimerR-HSA-1861595 (Reactome)
Myosin-X dimermim-catalysisR-HSA-1861595 (Reactome)
MyosinR-HSA-2029476 (Reactome)
NF2TBarR-HSA-2029456 (Reactome)
PAArrowR-HSA-2029471 (Reactome)
PAK1 dimerR-HSA-2029456 (Reactome)
PAK1ArrowR-HSA-2029456 (Reactome)
PAK1mim-catalysisR-HSA-2029454 (Reactome)
PAR-HSA-2029468 (Reactome)
PCR-HSA-2029471 (Reactome)
PCR-HSA-2029475 (Reactome)
PI(3,4)P2R-HSA-1861595 (Reactome)
PI(3,4,5)P3ArrowR-HSA-2029271 (Reactome)
PI(3,4,5)P3ArrowR-HSA-2029272 (Reactome)
PI(3,4,5)P3R-HSA-2029268 (Reactome)
PI(3,4,5)P3R-HSA-2029458 (Reactome)
PI(3,4,5)P3R-HSA-2029465 (Reactome)
PI(4,5)P2R-HSA-167686 (Reactome)
PI(4,5)P2R-HSA-2029271 (Reactome)
PI(4,5)P2R-HSA-442586 (Reactome)
PI3K:p-6Y-SYKArrowR-HSA-2029273 (Reactome)
PI3K:p-6Y-SYKmim-catalysisR-HSA-2029271 (Reactome)
PI3KR-HSA-2029273 (Reactome)
PKC-delta/epsilonR-HSA-198314 (Reactome)
PKC-delta/epsilonmim-catalysisR-HSA-198314 (Reactome)
PLA2G6mim-catalysisR-HSA-2029475 (Reactome)
PLC gamma1,2R-HSA-2029270 (Reactome)
PLDmim-catalysisR-HSA-2029471 (Reactome)
Phosphatidate phosphatasemim-catalysisR-HSA-2029468 (Reactome)
Phospho-PKC-delta/epsilonArrowR-HSA-198314 (Reactome)
PiArrowR-HSA-1861595 (Reactome)
PiArrowR-HSA-2029468 (Reactome)
PiArrowR-HSA-2029476 (Reactome)
R-HSA-167686 (Reactome) Inositol 1,4,5-triphosphate (IP3) is a second messenger produced by phospholipase C (PLC) metabolism of phosphoinositol 4,5-bisphosphate (PIP2) (Canossa et al. 2001).
R-HSA-169680 (Reactome) The IP3 receptor (IP3R) is an IP3-gated calcium channel. It is a large, homotetrameric protein, similar to other calcium channel proteins such as ryanodine. The four subunits form a 'four-leafed clover' structure arranged around the central calcium channel. Binding of ligands such as IP3 results in conformational changes in the receptor's structure that leads to channel opening.
R-HSA-169683 (Reactome) IP3 promotes the release of intracellular calcium.
R-HSA-1861595 (Reactome) Myosin-X (Myosin 10) is one of the downstream effectors of PI3K in FCGR-phagocytosis and is involved in pseudopod extension and closure of phagocytic cups. It is recruited to the forming phagosome by binding, through its second PH domain to membrane PIP3, a major product of PI3-kinase (Cox et al. 2002). Myosin-X may act as a motor to transport membrane cargo molecules to the forming pseudopods, influencing actin dynamics. It is not understood with certainty how myosin X contributes to the mechanism of pseudopod extension. It selectively binds to actin bundle such that each head may bind, in an ATP-sensitive manner, to two adjacent actin filaments within the actin bundle. Myosin X hydrolyze ATP and converts this chemical energy to mechanical energy moving toward the plus end/barbed end of the actin filament facing towards the tip of the growing pseudopods (Araki 2006, Chavrier 2003, Watanabe et al 2010).
R-HSA-1861621 (Reactome) FCGRII (CD32) is a low-affinity receptor encoded by three different genes (A, B and C) (Brooks et al. 1989). FCGRIIA functions as a single-chain transmembrane receptor containing both the ligand-binding extracellular domain and a signal transducing cytoplasmic domain that contains distinct immunoreceptor tyrosine-based activation motif (ITAM). This ITAM-like domain in FCGRIIA contains two YXXL motifs with a spacer sequence of 12 amino acids instead of the usual 7. Isoform FCGRIIB is expressed in various leukocytes, including human monocytes and, as opposed to the activating Fc receptors it has an immunoreceptor tyrosine-based inhibitory motif (ITIM) and negatively regulates phagocytosis (Van den Herik-Oudijk IE et al. 1995, Mitchell et al. 1994, Tridandapani et al. 2002).
The first step in Fc-gamma receptor (FCGR) phagocytosis is binding and clustering of FCGRs by IgG-coated foreign particles. FCGR are clustered at the cell surface by multivalent antigen-antibody complexes and recruited to lipid raft micro domains; monovalent ligand binding is insufficient to generate a signal. This cross-linking results in the localization of FCGRs into lipid rafts and this may aid in recruiting and complexing with additional signalling proteins associated with lipid rafts (Bournazos et al. 2009, Kwiatkowska & Sobota 2001, Kono et al. 2002). This is followed by phosphorylation of the tyrosine residues within the ITAM located on the cytoplasmic portion of FCGRIIA by membrane-associated tyrosine kinases of the Src family (Mitchell et al. 1994).
R-HSA-198314 (Reactome) Diacylglycerol (DAG) positively regulates the autophosphorylation of protein kinase C-delta (PKC-delta), which stimulates ERK1/2 and triggers neurite outgrowth. DAG also stimulates the translocation of PKC from the cytosol to the plasma membrane. PKC-delta contributes to growth factor specificity and response to neuronal cells by promoting cell-type-specific differences in growth factor signalling. DAG can also activate PKC-epsilon in the same manner (Newton 2001).
R-HSA-2029268 (Reactome) PLCG is tyrosine phosphorylated by either SYK or Src kinases on three tyrosine residues and this phosphorylation enhances the activity of PLCG. Although maximal activation requires binding of PLCG to PIP3 with its plecstrin homology (PH) domain.
R-HSA-2029270 (Reactome) PLCgamma (PLCG) is recruited to FCGR and the phosphorylated Y342 and Y346 in SYK have been reported to be involved in the interaction of PLCG (Law et al. 1996). PLCG accumulates at the phagocytic cup during FCGR, but the exact role of PLCG in the regulation of phagocytosis is not clear. It may be involved in FCGR signaling by activating PKC through DAG production (Garcia-Garcia & Rosales 2002 )
R-HSA-2029271 (Reactome) Activated PI3K phosphorylates phosphatidylinositol (PI) 4-phosphate and PI 4,5-bisphosphate (PIP2) to generate PI 3,4-bisphosphate and PI 3,4,5-triphosphate (PIP3) and these second messengers recruit other signaling proteins containing plecstrin homology (PH) domain. PIP3 rapidly accumulates at sites of phagocytosis and disappears after the phagosome has been sealed off from the plasma membrane.
R-HSA-2029272 (Reactome) Activated PLCG translocates to the plasmamembrane and interacts with the inositol ring of the membrane bound phosphatidylinositol 4,5-bisphosphate (PIP2) with its PH domain. The active enzyme promotes intracelllular signaling by catalysing the hydrolysis of PIP2 to generate the second messengers IP3 and DAG.
R-HSA-2029273 (Reactome) PI3K is one of the downstream effector of activated SYK. The p85 alpha regulatory subunit of PI3K have been shown to interact with SYK and FCGRs, and transient and restricted accumulation of lipid products of the kinase have been observed at sites of the phagosomal cup (Yanagi et al. 1994, Marshall et al. 2001). Leverrier at al. has demonstrated that p110beta is the major class I catalytic isoform required for FCGR-mediated phagocytosis by primary macrophages (Leverrier at al. 2003). p85 alpha subunit interacts with phosphorylated SYK at tyrosine 317 with its C-terminal SH2 domain, whereas other tyrosine residues like 342 and 346 in the linker region may contribute to the interaction with N-terminal SH2 domain (Moon et al, 2005). The main role of PI3K in phagocytosis appears to be the regulation of pseudopod extension necessary for particle internalization and may also regulate phagocytosis through activation of ERK (Garcia-Garcia & Rosales. 2002).
R-HSA-2029445 (Reactome) FCGR mediated phagocytosis requires CDC42 to stimulate actin polymerization, generating the force for phagocytic cup protrusion or pseudopod extension. CDC42 activation is restricted at the advancing edge of the phagocytic cup, where actin is concentrated, and is deactivated at the base of the phagocytic cup (Beemiller et al 2010). The mechanism behind the recruitment and activation of CDC42 during FCGR phagocytosis is unknown. VAV regulates the activation of RAC1 but not CDC42 and the GEF responsible for CDC42 activation during FCGR-mediated phagocytosis remains unidentified (Adam et al 2004, Patel et al 2002).
R-HSA-2029449 (Reactome) Multiple sites of phosphorylation are known to exist in SYK, which both regulate its activity and also serve as docking sites for other proteins. Some of these sites include Y131 of interdomain A, Y323, Y348, and Y352 of interdomain B, and Y525 and Y526 within the activation loop of the kinase domain and Y630 in the C-terminus (Zhang et al. 2002, Lupher et al. 1998, Furlong et al. 1997). Phosphorylation of these tyrosine residues disrupts autoinhibitory interactions and results in kinase activation even in the absence of phosphorylated ITAM tyrosines (Tsang et al. 2008). SYK is primarily phosphorylated by Src family kinases and this acts as an initiating trigger by generating few molecules of activated SYK which are then involved in major SYK autophosphorylation (Hillal et al. 1997).
R-HSA-2029451 (Reactome) The organized movements of membranes and the actin cytoskeleton are coordinated in phagocytosis by small GTPases of the Rho family. Specifically, RAC1 and CDC42 are known to be stimulated upon engagement of FCGR and are essential for the extension of the pseudopods that surround and engulf the phagocytic particle (Scott et al 2005). RAC1 is known to regulate actin dynamics. It is active throughout the phagocytic cup and activated RAC1 is necessary to assemble F actin. However, closing the phagocytic cup requires RAC1 to be deactivated (Naakaya et al 2007). Deletion of RAC1 prevents FCGR mediated phagocytosis (Hall et al 2006). RAC1 activation involves transition from an inactive GDP bound to an active GTP bound state catalysed by guanine exchanges factors (GEFs). VAV has been implicated in the activation of RAC1 (Patel et al 2002).
R-HSA-2029452 (Reactome) SYK is a tyrosine kinase related to ZAP70 that is expressed in all hematopoietic cells and coimmunoprecipitates with the gamma chain associated with FCGRIIIA in macrophages and with FCERI in mast cells. SYK is very important for FCGR phagocytosis and is recruited to these phosphorylated ITAM residues through its two SRC homology 2 (SH2) domains (Agarwal et al. 1993). When SYK kinase expression is inhibited with antisense oligonucleotides both in vitro and in vivo, phagocytosis and inflammation are abolished (Matsuda et al. 1997). The domain structure of SYK comprises a regulatory region at the N-terminus consisting of a pair of SH2 domains separated by an inter-SH2 linker called interdomain A, an SH2-domain-kinase linker termed interdomain B, and a C-terminal kinase domain (Arias-Palomo et al. 2009). In resting state SYK exists in an auto-inhibited conformation by the interactions between the SH2-SH2 regulatory region and the inter-SH2 linker and the catalytic domain. This interdomain interaction reduces the conformational flexibility required by the kinase domain for catalysis (Arias-Palomo et al. 2007). Changes in the orientation of the SH2 domains could control the disruption of the auto inhibitory interactions and the activation of SYK. These movements could be totally or partially induced by the binding to phosphorylated ITAMs and/or phosphorylation of tyrosine residues in interdomain A or B (Arias-Palomo et al. 2009). Tsang et al. suggested that SYK functions as an OR-gate switch with respect to phosphorylation and ITAM binding, as either one stimulus OR the other is sufficient to cause full activation (Tsang et al. 2008).
R-HSA-2029453 (Reactome) VAV proteins exist in an auto-inhibitory state folded in such a way as to inhibit the GEF activity of its DH domain. This folding is mediated through binding of tyrosines in the acidic domain to the DH domain and through binding of the CH domain to the C1 region. Activation of VAV may involve at least three different events to relieve this auto-inhibition. Phosphorylation of the tyrosines in the acidic domain causes them to be displaced from the DH domain, binding of a ligand to the CH domain may cause it to release the C1 domain and binding of PIP3 to PH domain may alter its conformation. VAV1 is phosphorylated on Y174 in the acidic domain, and this is mediated by Syk and Src-family tyrosine kinases. Once activated, VAV1 is then involved in the activation of RAC and CDC42 downstream of FCGR.
R-HSA-2029454 (Reactome) PAK1 needs autophosphorylation for complete activation. PAK1 is autophosphorylated at several sites, but S144 flanking the kinase inhibitor region and T423 within the catalytic domain are the two conserved sites that regulate the catalytic activity (Chong et al. 2001, Parrini et al. 2001).
R-HSA-2029455 (Reactome) FCGRI is coded by three different genes (A, B, and C) and is expressed on most myeloid cells including monocytes, macrophages and dendritic cells (Allen & Seed 1988). FCGRI is a high affinity IgG receptor capable of binding monomeric IgG. FCGRI exists as a complex containing ligand (IgG) binding extracellular alpha-chain and homodimer of signal transducing FcR gamma (CD3G) chains, or a heterodimer of signal transducing FcR gamma and zeta chains (Ernst et al. 1993, Scholl & Geha 1993, van Vugt et al. 1996). The cytoplasmic domain of FCGRI does not have signaling motifs, however it is suggested that the gamma-subunit might be required for generating the phagocytic signal (Duchemin et al. 1994, Indik et al. 1995).
The first step in Fc-gamma receptor (FCGR) phagocytosis is binding and clustering of FCGRs by IgG-coated foreign particles. FCGR are clustered at the cell surface by multivalent antigen-antibody complexes and recruited to lipid raft micro domains; monovalent ligand binding is insufficient to generate a signal. This cross-linking results in the localization of FCGRs into lipid rafts and this may aid in recruiting and complexing with additional signalling proteins associated with lipid rafts (Bournazos et al. 2009, Kwiatkowska & Sobota 2001, Kono et al. 2002). This is followed by phosphorylation of the tyrosine residues with in the immuno tyrosine activation motif (ITAM) located on the cytoplasmic portion of accessory gamma/zeta chains by membrane-associated tyrosine kinases of the Src family (Duchemin et al. 1994, van Vugt et al. 1996).
R-HSA-2029456 (Reactome) PAK1, a downstream effector of CDC42 and RAC1, is found localized in phagosomes. Upon activation, PAK1 phosphorylates LIMK, which directly phosphorylates and inactivates cofilin, a protein that mediates depolymerization of actin filaments. Thus, RAC and CDC42 coordinate actin dynamics by inducing actin polymerization via ARP2/3 on one hand, and inhibiting actin depolyerization via LIMK and cofilin on the other (Garcia-Garcia & Rosales 2002).
PAK1 exists as homodimer in a trans-inhibited conformation. The kinase inhibitory (KI) domain of one PAK1 molecule binds to the C-terminal catalytic domain of the other and inhibits catalytic activity. GTPases RAC1/CDC42 bind the GBD domain of PAK1 thereby altering the conformation of the KI domain, relieving inhibition of its catalytic domain, and allowing PAK1 autophosphorylation that is required for full kinase activity (Parrini et al. 2002, Zhao & Manser 2005).
R-HSA-2029457 (Reactome) FCGRIII (CD16) is a low affinity Fc gamma receptor and is encoded by two genes (A and B), the transmembrane form FCGRIIIA and the GPI anchored FCGRIIIB (Edberg et al. 1989). FCGRIIIA is involved in phagocytosis and is expressed in macrophages and natural killer cells as a multi chain complex consisting of a single alpha chain containing IgG binding domains and a signal transducing gamma and/or zeta dimer (Wirthmuller et al. 1992, Lanier et al. 1989, Garcia Garcia & Rosales 2002). Both gamma and zeta chains contain a conserved immunoreceptor tyrosine based activation motif (ITAM), which has 2 copies of the YXXL sequence (Isakov 1997). However, the gamma chain of FCGRIIIA is approximately sixfold more efficient in mediating phagocytosis than the zeta subunit (Park & Schreiber 1995). Phosphorylation of the conserved tyrosine residues of the ITAM in these accessory proteins is required for the phagocytic signal mediated by FCRGIIIA.
The first step in Fc-gamma receptor (FCGR) phagocytosis is binding and clustering of FCGRs by IgG-coated foreign particles (For this particular pathway the coated foreing particle is the Leishmania parasite). FCGR are clustered at the cell surface by multivalent antigen-antibody complexes and recruited to lipid raft micro domains; monovalent ligand binding is insufficient to generate a signal.
This cross linking results in the localisation of FCGRs into lipid rafts and this may aid in their recruiting and complexing with additional signalling proteins associated with lipid rafts (Kono et al. 2002). This is followed by phosphorylation of the tyrosine residues within the ITAM located on the cytoplasmic portion of accessory gamma/zeta chains by membrane associated tyrosine kinases of the Src family (Park et al. 1993).
R-HSA-2029458 (Reactome) VAV family members are cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho-family GTPases (RAC, RHO and CDC42). VAV1 is found predominantly in hematopoietic cells, whereas VAV2 and VAV3 are more broadly expressed. VAV proteins link the cell surface receptors like FCGR to the intracellular Rho GTPases and the actin cytoskeleton during phagocytosis (Hall et al 2006). Experiments using two-hybrid system suggest that VAV1 with its SH2 domain directly binds to the phosphorylated Y342 of SYK (Deckert et al. 1996). VAV proteins are also recruited to membrane through their PH domain by binding PI(3,4,5)P3 produced by PI3K.
R-HSA-2029459 (Reactome) After cross linking, Fc gamma receptors are sequestered to lipid rafts where they are complexed with some of the tyrosine kinases of Src family and undergo phosphorylation on the tyrosine residues contained in conserved ITAM sequences. At least six out of nine members of the Src family kinases (SRC, FYN, FGR, HCK, YES and LYN ) have been identified in the phagocytic cells and are implicated in the initiation of Fc gamma mediated signaling. (Suzuki et al. 2000, Majeed et al. 2001, Kwiatkowska et al. 2003). Some of these kinases have been found associated with specific receptors. In monocytes HCK and LYN have been found associated with FCGRI (Durden et al. 1995), whereas only HCK with FCGRIIA (Ghazizadeh et al. 1994) while FGR in neutrophils (Hamada et al. 1993) and LCK in NK cells with FCGRIIIA (Pignata et al. 1993)
The implication of Src kinases in phosphorylation was first supported by pharmacological findings that herbimycin A, a tyrosine kinase inhibitor relatively specific for Src-family kinases, potently suppressed Fc receptor mediated functions (Greenberg et al. 1993, Suzuki et al. 2000). However, their particular involvement in phagocytosis remains unclear, as targeted disruption of single or multiple Src family genes did not result in significant alterations in phagocytosis (Hunter et al. 1993, Fitzer Attas et al. 2000, Suzuki et al. 2000). HCK, FGR and LYN triple-deficient (-/-) macrophages have shown significant delays in FCGR mediated phagocytosis, but these deficiencies do not completly disrupt the process (Fitzer Attas et al. 2000).
Tyrosine residues Y288 and Y304 (Y282 and Y298 according to the literature reference, it is 6 residues shorter compared to uniprot entry due to an alternate initiation codon usage), within ITAM sequence in the cytoplasmic domain of FCGRIIA are the key target sites that are phosphorylated by Src family kinases (Mitchell et al, 1994). In case of FCGRIA and FCGRIIIA the specific tyrosine residues within ITAMs of the associated gamma/zeta chains are phosphorylated by activated Src family kinases (SFKs) (Park et al. 1993).
R-HSA-2029460 (Reactome) LIM kinases are serine protein kinases with a unique combination of two N-terminal LIM motifs, a central PDZ domain, and a C-terminal protein kinase domain. LIMK1 is one of the downstream targets of PAK1 and is activated through phosphorylation by PAK1 on T508 within its activation loop (Edwards et al. 1999, Aizawa et al. 2001). LIM-kinase is responsible for the tight regulation of the activity of cofilin (a protein that depolymerizes actin filaments) and thus maintains the balance between actin assembly and disassembly. Phosphorylated cofilin is inactive, resulting in stabilization of the actin cytoskeleton.
R-HSA-2029465 (Reactome) WASP family verprolin-homologous proteins (WAVEs) function downstream of RAC1 and are involved in activation of the ARP2/3 complex. The resulting actin polymerization mediates the projection of the plasma membrane in lamellipodia and membrane ruffles. WAVEs exist as a pentameric hetero-complex called WAVE Regulatory Complex (WRC). The WRC consists of a WAVE family protein (WASF1, WASF2 or WASF3 - commonly known as WAVE1, WAVE2 or WAVE3), ABI (Abelson-interacting protein), NCKAP1 (NAP1, p125NAP1), CYFIP1 (SRA1) or the closely related CYFIP2 (PIR121), and BRK1 (HSPC300, BRICK). Of the three structurally conserved WAVEs in mammals, the importance of WAVE2 in activation of the ARP2/3 complex and the consequent formation of branched actin filaments is best established. WAVEs in the WRC are intrinsically inactive and are stimulated by RAC1 GTPase and phosphatidylinositols (PIP3). The C-terminal VCA domain of WAVE2 (and likely WAVE1 and WAVE3) which can bind both the ARP2/3 complex and actin monomers (G-actin) is masked in the inactive state. After PIP3 binds to the polybasic region of WAVE2 (and likely WAVE1 and WAVE3) and RAC1:GTP binds to the CYFIP1 (or CYFIP2) subunit of the WRC, allosteric changes most likely occur which allow WAVEs to interact with the ARP2/3 complex. The interactions between WAVEs and RAC1 are indirect. BAIAP2/IRSp53, an insulin receptor substrate, acts as a linker, binding both activated RAC1 and the proline-rich region of WAVE2 (and likely WAVE1 and WAVE3) and forming a trimolecular complex. CYFIP1 (or CYFIP2) in the WAVE regulatory complex binds directly to RAC1:GTP and links it to WAVE2 (and likely WAVE1 and WAVE3) (Derivery et al. 2009, Yamazaki et al. 2006, Takenawa & Suetsugu 2007, Chen et al. 2010, Pollard 2007, Lebensohn & Kirschner 2009).
R-HSA-2029466 (Reactome) Once activated, the ARP2/3 complex nucleates new actin filaments that extend from the sides of pre-existing mother actin filaments at a 70-degree angle to form Y-branched networks (Firat-Karalar & Welch 2010). These branched actin filaments push the cell membrane forward to form a pseudopod. The ARP2/3 complex is composed of two Arps (actin-related proteins), ARP2 and ARP3, and five unique proteins ARPC1, ARPC2, ARPC3, ARPC4 and ARPC5 (Gournier et al. 2001). Both ARP2 and ARP3 subunits bind ATP. There are two proposed models to explain the process of actin nucleation by ARP2/3 complex: the barbed-end branching model and the dendritic nucleation/side branching model (Le Clainche & Carlier 2008).
In barbed-end branching model, the branching/ternary complex (G-actin-WASP/WAVE-Arp2/3 complex) binds to the barbed end of the mother filament. G-actin bound to VCA domain or one of the Arp subunits incorporates into the mother filament at the barbed end, thus positioning ARP2/3 complex to initiate the daughter branch on the side of the mother filament. ARP2/3 nucleates the formation of new actin filament branches, which elongate at the barbed ends (Le Clainche & Carlier 2008, Pantaloni et al 2000, Le Clainche et al. 2003, Egile et al. 2005). In side branching model, the branching complex binds to the side of the mother actin filament mimicking an actin nucleus and initiates a lateral branch (Le Clainche & Carlier 2008, Amann & Pollard 2001).
R-HSA-2029467 (Reactome) RAC1 is activated from inactive GDP-bound state to active GTP-bound form by the GEF activity of DOCK180:ELMO complex.
R-HSA-2029468 (Reactome) Phosphatidic acid phosphatase (PAP) bound to the plasma membrane catalyzes the dephosphorylation of phosphatidic acid (PA), yielding diacylglycerol (DAG) and inorganic phosphate. In humans, Diacylglycerol pyrophosphate (DPPL1 and DPPL2) perform this reaction.
R-HSA-2029469 (Reactome) The ARP2/3 complex shows higher affinity for the phosphorylated VCA domain of WAVE2 than for the unphosphorylated VCA domain. WAVE proteins can be phosphorylated by various kinases. Active ERK (Mitogen activated protein kinase 3) phosphorylates the WAVE regulatory complex (WRC) on multiple serine/threonine sites within the proline-rich domains (PRDs) of WAVE2 and ABI1. Phosphorylation of the PRDs would disrupt their interaction with SH3 and PLP binding domains, potentially altering WRC activation. ERK phosphorylates both S343 and T346 in WAVE2 and S183, S216, S225, S392, and S410 in ABI1. Cumulatively, the phosphorylation of both WAVE2 and ABI in the WAVE regulatory complex (WRC) contributes to the RAC-induced WRC conformational change that exposes the VCA domain, leading to binding and activation of ARP2/3 (Mendoza et al. 2011, Nakanishi et al. 2007). ERK phosphorylation sites in WAVE2 are not strictly conserved in WAVE1 and WAVE3 but, based on the amino acid sequence, other potential ERK phosphorylation sites exist.
R-HSA-2029471 (Reactome) Phospholipase D (PLD) catalyses the hydrolysis of the membrane phospholipid, phosphatidylcholine (PC) to generate choline and metabolically active phosphatidic acid (PA) (Lennartz 1999). Pharmacological inhibition studies show that PLD participates in FCGR-mediated phagocytosis (Kusner et al. 1996). There is an increase in the activity of PLD following the activation of phagocytosis via FCGR (Kusner et al. 1999). Following activation of FCGR, PLD translocates to the plasma membrane at the phagocytic cup and generate PA. This PA can be converted to DAG through the action of phosphatidic acid phosphatase-1 (PAP-1). Thus activation of PLD may be an additional pathway leading to PKC activation.
The two isoforms PLD1 and PLD2 are both shown to be essential for the formation of phagosome at different stages. PLD1 is localized on the endosomal/lysosomal compartment and PLD2 is localized at the plasma membrane. PLD2 may be linked to phagosome formation whereas PLD1 may be involved in the focal exocytosis at the plasma membrane and also in the maturation process (Carrotte et al. 2006).
R-HSA-2029473 (Reactome) ATP bound G-actin monomers are added to the fast growing barbed ends of both mother and daughter filaments. The polymerization of these filaments drives membrane protrusion. In the process of phagocytosis, pseudopodia extend around the antibody-bound particle to form the phagocytic cup. This elongation continues until the filament reaches steady state equilibrium with free G-actin monomers (Millard et al. 2004, Le Clainche et al. 2008).
R-HSA-2029475 (Reactome) Several members of phospholipase A (PLA) are involved in phagocytosis. Macrophages express three classes of PLA2: secreted Ca-dependent (sPLA2), cytosolic Ca-dependent (cPLA2) and cytosolic Ca-independent (iPLA2) of which iPLA2 is involved in FCGR mediated arachidonic acid (AA) production. Aggregation of FCGR triggers phosphorylation and membrane translocation of iPLA2. Protein kinase C (PKC), ERK and p38MAPK seems to regulate iPLA2 in monocytes, neutrophils and macrophages. Phosphorylated iPLA2 then mediates production of AA and lysoophospholipids from phosphatidylcholine. iPLA2 inhibitors (bromoenol lactone) block AA release and phagocytosis which can be restored upon addition of exogenous AA, suggesting a critical role for iPLA2 in FCGR phagocytosis (Lennartz et al. 1993, Tay & Melendez). Release of AA by activated iPLA2 changes the physical characteristic of the membrane which may facilitate pseudopod extension.
R-HSA-2029476 (Reactome) In addition to the membrane remodeling for pseudopod extension, particle internalization requires a contractility force pulling the forming phagosome into the cytoplasm. Myosin motor proteins are the actin-binding proteins, with ATPase activity move along actin fibers, and produce the driving force for phagosome formation and transport. Several myosin motors including myosins IC, II, V, IXb are involved in FCGR-mediated phagocytosis as force generators and actin-based transport motors (Swanson et al. 1999). Nonmuscle myosin II, is a motor protein known to generate intracellular contractile forces and tension by associating with F-actin. It has been observed to localize around forming phagosomes and suggested a role in phagocytic-cup squeezing during FCGR-mediated phagocytosis. Each myosin II motor protein exists as a complex consisting of two copies each of myosin II heavy chain (MHC), essential light chains (ELC), and myosin regulatory light chain (MRLC). Selective inhibition of myosin II by ML-7, a myosin light-chain kinase (MLCK) inhibitor, prevents phagocytic cup closure, but not pseudopod extension for the formation of phagocytic cups in FCGR-mediated phagocytosis (Grooves et al. 2008, Araki 2006). Tight ring of actin filaments within the elongating pseudopodia squeezes the deformable particles. In the classical zipper model for phagocytosis, the pseudopod extends over the IgG-coated particles, in which FCGRs in the phagocyte plasma membrane interact sequentially with Fc portions of IgG molecules zippering the membrane along the particle. This sequential IgG-FCGR binding might not occur by itself, but requires forced zipper closure, where myosin-II contractile activity may promote the binding between the FCGR and its ligands, to facilitate the efficient extension and subsequent closure of phagocytic cups (Araki 2006, ). Myosin IC mediates the purse-string-like contraction that closes phagosomes. Myosin-V has been implicated in membrane trafficking events (Swanson et al. 1999).
R-HSA-2130194 (Reactome) Abelson interactor-1 (ABL) tyrosine kinase phosphorylates the strictly conserved tyrosine 150 in WAVE2 (Y151 in WAVE1 and WAVE3) (Leng et al. 2003, Chen et al. 2010).
R-HSA-2197690 (Reactome) After incorporation at the branch, the actin bound to VCA domain of WASP/WAVE undergoes ATP hydrolysis and this destabilizes its interaction with WASP/WAVE. This dissociates the branched junction from the membrane-bound WASP/WAVE (Kovar 2006).
R-HSA-2197691 (Reactome) WASP interacting proteins (WIP) family includes WIPF1 (WIP), WIPF2 (WIRE,WICH) and WIPF3 (CR16, corticosteroids and regional expression-16). WIPs share a specific proline rich sequence that interacts with the WH1 domain of WASP and N-WASP (WASL). WIPs form heterocomplexes with WASPs and may contribute to the WASP protein stability (Aspenstrom 2002, Kato et al. 2002, Ho et al. 2001, Moreau et al. 2000).
SH3 domain containing adaptor proteins like GRB2 (Carlier et al. 2000), NCK (Rohatgi et al. 2001) and WISH (DIP/SPIN90) (Fukuoka et al. 2001) bind to the proline rich domain in WASPs and activate the ARP2/3 complex. By binding simultaneously to N-WASP and the ARP2/3 complex, GRB2 works synergistically with CDC42 in the activation of ARP2/3 complex-mediated actin assembly (Carlier et al. 2000).
R-HSA-2197697 (Reactome) Macrophages lacking all the three isoforms of VAV did not affect FCGR-mediated phagocytosis suggesting that RAC1 is regulated by GEFs other than VAV downstream of the FCGR (Hall et al 2006). DOCK180, a member of GEFs, is found to be involved in the activation of RAC1. DOCK180 associates with the adaptor protein CRKII and the complex is found to accumulate at the phagocytic cup. DOCK180 is recruited to the sites of phagocytosis by binding to SH3 domain of CRKII through its proline-rich motif (Hasegawa et al 1996). CRKII is likely recruited to the activated FCGR complex by binding phosphorylated ITAM tyrosines on the receptor or through other phosphotyrosines on ancillary proteins that are recruited to the receptor complex (Lee et al 2007). Unlike the usual GEFs, DOCK180 does not contain the conserved Dbl homology (DH) domain. Instead, it has a DHR-2 or DOCKER domain capable of loading RAC with GTP (Brugnera et al 2002). Binding of DOCK180 to RAC alone is insufficient for GTP loading, and a DOCK180-ELMO interaction is required. ELMO1, as well as ELMO2, form a complex with DOCK180 and they function together as a bipartite GEF to optimally activate RAC (Gumienny et al 2001, Brugnera et al 2002).
R-HSA-2197698 (Reactome) WASP is phosphorylated on Tyr291 (Cory et al. 2002) and N-WASP (WASL) on Tyr256 (Wu et al. 2004) by Src family of tyrosine kinases and this phosphorylation may release the autoinhibitory intramolecular interactions. The phosphorylation seems to be enhanced by the activation of CDC42. WASP phosphorylation and binding of CDC42 have a synergistic effect on the activation of the ARP2/3 complex (Takenawa & Suetsugu 2007). In N-WASP, the phosphorylation may reduce its nuclear translocation and may sustain it in its functional site in the cytoplasm (Wu et al. 2004).
R-HSA-399950 (Reactome) The EPHB2-FAK pathway partially promotes dendritic spine stability through LIMK-mediated cofilin (CFL1) phosphorylation (Shi et al. 2009). CFL1 is a member of the ADF (actin-depolymerizing factor) protein family that is involved in regulating actin dynamics in the growth cone. It binds to actin in a one-to-one molar ratio, and stimulates both the severing of actin filaments and depolymerization of actin subunits from the actin filament end. Activated LIMK phosphorylates CFL1 on the conserved serine 3 residue located near the actin-binding site. After phosphorylation, CFL1 is inactive, loses its affinity for actin and dissociates from G-actin monomers. Once freed, ADP-actin monomers can exchange ADP with cytoplasmic ATP, ready for reincorporation at the barbed end of a growing filament (Gungabissoon & Bamburg 2003).
R-HSA-419644 (Reactome) Binding of Hsp90 to the LIMK proteins protects them from degradation and promotes their dimer formation and transphosphorylation. It is estimated that LIMK1 contains at least 5 phospho-amino acids primarily phospho-serines, in its kinase domain. The positions of these serine residues are not known. Transphosphorylation of these serine residues in LIMK1 increases its stability.
R-HSA-419645 (Reactome) After phosphorylation on Thr 508, LIMK undergoes homodimerization. Homodimer formation is promoted by the binding of heat shock protein 90 (Hsp90) to a short sequence in the kinase domain of LIMKs. LIMKs are further phosphorylated after homodimer formation and transphosphorylation of the kinase domain.
R-HSA-442586 (Reactome) Wiskott-Aldrich syndrome protein (WASP) and Neural-WASP (N-WASP, WASL) proteins are scaffolds that transduce signals from cell surface receptors to the activation of the ARP2/3 complex and actin polymerization. WASP and N-WASP possess a central GTPase binding domain (GBD) and an NH2-terminal WASP homology domain 1 (WH1) followed by a basic region (B), and a C-terminal VCA region that contains: a V domain (verprolin homology/WASP homology 2), a C domain (connecting), and an A motif (acidic). The VCA region is responsible for binding to and activating the ARP2/3 complex (Bompard & Caron 2004, Callebaut et al 1998). Under resting conditions, WASP and N-WASP are maintained in an autoinhibited state via interaction of the GBD and the VCA domains. This prevents access of the ARP2/3 complex and G-actin to the VCA region. Activated CDC42 binds to the GBD region of WASPs and this interaction releases the VCA region from autoinhibition, enabling binding of the ARP2/3 complex and stimulating actin polymerization (Kim et al 2000, Park & Cox 2009). Phosphoinositides (PtdIns(4,5)P2) interact with the basic (B) region in WASPs and this interaction is important for activation of the WASPs and the ARP2/3 complex (Higgs & Pollard 2000).
R-HSA-442592 (Reactome) Once WASPs (WASP and N-WASP) and WAVEs (WAVE2 and probably WAVE1 and WAVE3) are activated, their VCA region becomes available for binding to the ARP2/3 complex and actin monomer (G-actin). The actin monomer binds to the V domain and ARP2/3 complex binds to the CA domain. The simultaneous binding of G-actin and the ARP2/3 complex to the VCA region contributes to the activation of the ARP2/3-complex-mediated actin polymerization. The VCA module acts as a platform on which an actin monomer binds to the ARP2/3 complex to trigger actin polymerization (Takenawa & Suetsugu 2007).
RAC1:GDPR-HSA-2029451 (Reactome)
RAC1:GDPR-HSA-2029467 (Reactome)
RAC1:GTP,CDC42:GTP:PAK1ArrowR-HSA-2029456 (Reactome)
RAC1:GTP,CDC42:GTP:PAK1R-HSA-2029454 (Reactome)
RAC1:GTPArrowR-HSA-2029451 (Reactome)
RAC1:GTPArrowR-HSA-2029467 (Reactome)
RAC1:GTPR-HSA-2029465 (Reactome)
SH3 domain proteinsR-HSA-2197691 (Reactome)
SYKR-HSA-2029452 (Reactome)
Src family kinases (SFKs)mim-catalysisR-HSA-2029459 (Reactome)
Src-kinasesmim-catalysisR-HSA-2197698 (Reactome)
Unknown GEFmim-catalysisR-HSA-2029445 (Reactome)
VAV1,2,3R-HSA-2029458 (Reactome)
WASP/N-WASPR-HSA-442586 (Reactome)
WAVE Regulatory ComplexR-HSA-2029465 (Reactome)
WAVE2, WASP,

N-WASP:ARP2/3

complex:G-actin		ArrowR-HSA-442592 (Reactome)
WAVE2, WASP,

N-WASP:ARP2/3

complex:G-actin		R-HSA-2029466 (Reactome)
WAVE2, WASP, N-WASPArrowR-HSA-2197690 (Reactome)
WAVE2, WASP, N-WASPR-HSA-442592 (Reactome)
WIP family proteinsR-HSA-2197691 (Reactome)
WRC:IRSp53/58:RAC1:GTP:PIP3ArrowR-HSA-2029465 (Reactome)
WRC:IRSp53/58:RAC1:GTP:PIP3R-HSA-2130194 (Reactome)
clustered IgG-Ag:FCGRsR-HSA-2029459 (Reactome)
clustered IgG-Ag:p-FCGRs:SYKArrowR-HSA-2029452 (Reactome)
clustered IgG-Ag:p-FCGRs:SYKR-HSA-2029449 (Reactome)
clustered IgG-Ag:p-FCGRs:SYKmim-catalysisR-HSA-2029449 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:PLCGArrowR-HSA-2029270 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:PLCGR-HSA-2029268 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:PLCGmim-catalysisR-HSA-2029268 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:VAVArrowR-HSA-2029458 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:VAVR-HSA-2029453 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:p-3Y-PLCGArrowR-HSA-2029268 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:p-3Y-PLCGR-HSA-2029272 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:p-VAVArrowR-HSA-2029453 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:p-VAVmim-catalysisR-HSA-2029451 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYKArrowR-HSA-2029272 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYKArrowR-HSA-2029449 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYKR-HSA-2029270 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYKR-HSA-2029273 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYKR-HSA-2029458 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYKR-HSA-2197697 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYKmim-catalysisR-HSA-2029453 (Reactome)
clustered IgG-Ag:p-FCGRsArrowR-HSA-2029459 (Reactome)
clustered IgG-Ag:p-FCGRsArrowR-HSA-2029476 (Reactome)
clustered IgG-Ag:p-FCGRsR-HSA-2029452 (Reactome)
clustered IgG-Ag:p-FCGRsR-HSA-2029476 (Reactome)
p-4Y-PLCG1mim-catalysisR-HSA-167686 (Reactome)
p-PLCGArrowR-HSA-2029272 (Reactome)
p-S144,T423-PAK1ArrowR-HSA-2029454 (Reactome)
p-S144,T423-PAK1mim-catalysisR-HSA-2029460 (Reactome)
p-T,Y MAPK dimersmim-catalysisR-HSA-2029469 (Reactome)
p-T508-LIMK1ArrowR-HSA-2029460 (Reactome)
p-T508-LIMK1R-HSA-419645 (Reactome)
p-Y,S,T-WRC:IRSp53/58:RAC1:GTP:PIP3ArrowR-HSA-2029469 (Reactome)
p-Y-WRC:IRSp53/58:RAC1:GTP:PIP3ArrowR-HSA-2130194 (Reactome)
p-Y-WRC:IRSp53/58:RAC1:GTP:PIP3R-HSA-2029469 (Reactome)
pCofilin: Active LIMK-1ArrowR-HSA-399950 (Reactome)
pLIMK dimer:HSP-90ArrowR-HSA-419645 (Reactome)
pLIMK dimer:HSP-90R-HSA-419644 (Reactome)
pLIMK dimer:HSP-90mim-catalysisR-HSA-419644 (Reactome)
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