FCGR3A-mediated phagocytosis (Homo sapiens)

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47, 62594311, 17, 25, 29, 3018, 4832, 456, 462, 9, 14, 49, 50, 6134, 3710, 33, 571, 8, 15, 17, 22...4226, 42, 533, 6010, 27, 4456, 64581213, 21, 24, 35, 40...19, 20, 39, 5152, 582, 9, 14, 49, 50, 615, 74331, 55554, 544, 16, 23, 36, 48...Leishmaniacytosolphagocytic cupHostcytosolCRK:DOCK180:ELMO1,ELMO2IGLV2-23(1-?) IGLV3-25(1-?) IGKV2D-30 PTK2 FGR ATPIGHG2 Ig kappa chain V-I region Gal Ig kappa chain V-I region Daudi Ig lambda chain V region 4A Ig lambda chain V region 4A p-Y151,S,T-WASF1 Ig kappa chain V-I region Gal Ig kappa chain V-III region VG p-Y151,S,T-WASF3 IGLV2-11(1-?) IGKV2-28 IGLV7-43(1-?) ARPC5 IGLV3-16(1-?) p-Y150,S343,T346-WASF2 Ig lambda chain V-I region NEW Ig kappa chain V-I region HK101 p-Y160,Y171-CD3G FCGR3A IGKV2-28 IGLC3 Ig kappa chain V-I region AG IGLV3-22(1-?) ARPC1A IGLC6 Ig lambda chain V-III region LOI Ig kappa chain V-I region Gal Ig kappa chain V-I region Wes ADPABI1 Ig kappa chain V-III region B6 IgH heavy chain V-III region VH26 precursor IGLV7-43(1-?) Ig heavy chain V-III region BUT IGLV(23-?) Ig lambda chain V-II region MGC WIPF1 Ig kappa chain V-I region AU IGHV(1-?) Ig heavy chain V-III region TRO NCKAP1L IGLV3-12(1-?) IGKV2-28 Ig heavy chain V-III region BUT Ig lambda chain V-VI region AR MYO10 IGLV3-22(1-?) LPG1G2 IGHG4 Ig kappa chain V-III region B6 Ig lambda chain V-I region VOR SH3 domain proteinsIGLV1-40(1-?) WASF1 IGHG4 IGLV2-11(1-?) CDC42:GTP:p-Y-WASP/p-Y-WASL:WIP:SH3 proteinsIGLC7 IgH heavy chain V-III region VH26 precursor SRC-1 p-Y160,Y171-CD3G IGLV5-45(1-?) Ig kappa chain V-I region DEE PI(4,5)P2 ARPC1B IGHG3 IGLV3-27(1-?) Ig kappa chain V-II region FR IGLC1 Ig lambda chain V-II region TOG p-T,Y MAPK dimersIg lambda chain V-II region BOH Ig kappa chain V-I region Wes Ig heavy chain V-II region ARH-77 IGKV3D-20 IGLV3-25(1-?) IGKC IGLV3-12(1-?) GDPIGHG3 CYFIP1 Ig lambda chain V-I region NEWM Ig lambda chain V-I region HA Ig kappa chain V-II region Cum IGLV2-23(1-?) ADP Ig lambda chain V-II region MGC IGLV3-27(1-?) IGLV1-44(1-?) Ig lambda chain V-II region NEI IGHV7-81(1-?) Ig lambda chain V-I region NEW Ig lambda chain V-VI region AR IGLV3-16(1-?) IGLV3-27(1-?) Ig heavy chain V-III region WEA IGKV3D-20 Ig lambda chain V-I region VOR IGKV3D-20 IGLV1-40(1-?) IGKV4-1(21-?) PIP3:VAV1,2,3IGKC Ig lambda chain V-IV region Bau WAS CDC42 IGKV1-5(23-?) IGLV3-25(1-?) Ig kappa chain V-I region Wes Ig lambda chain V-II region BOH Ig lambda chain V-III region SH IGLV2-23(1-?) Ig heavy chain V-III region KOL IGLV2-18(1-?) Ig lambda chain V-II region TOG IGLV3-12(1-?) IGKV2D-30 ACTR2 Ig lambda chain V-VI region AR IGHV7-81(1-?) Ig heavy chain V-II region MCE Ig heavy chain V-II region OU Ig heavy chain V-II region NEWM IgH heavy chain V-III region VH26 precursor Ig heavy chain V-II region MCE Ig lambda chain V-I region NEWM Ig lambda chain V-I region VOR IGLV3-16(1-?) Ig kappa chain V-I region HK101 CYFIP2 IGLV3-16(1-?) Ig heavy chain V-III region CAM Ig kappa chain V-II region Cum IGKVA18(21-?) F-actinIg kappa chain V-I region AU Ig lambda chain V-IV region Bau IGLV8-61(1-?) Ig kappa chain V-III region B6 Ig lambda chain V-I region NEWM Ig kappa chain V-II region Cum NCKAP1 IGLV7-46(1-?) IGLC6 p-Y150-WASF2 CYFIP1 IGLC6 CDC42 IGLC1 IGKV2D-30 IGKV2D-30 IGKV3D-20 IGLV3-22(1-?) IGLV2-18(1-?) WIPF2 ACTB(1-375) Ig kappa chain V-I region AG IGLV2-33(1-?) Ig kappa chain V-III region B6 Ig lambda chain V region 4A Ig heavy chain V-I region EU ATP ARPC5 Ig kappa chain V-I region DEE IGLV4-3(1-?) BTK ACTG1 IGLV4-69(1-?) CRK IGLV1-40(1-?) p-5S-ABI1 FCGR3A ARPC3 IGHG3 p-4S-ABI2 IGLC2 IGLV4-60(1-?) Ig lambda chain V-III region LOI CYFIP2 LPG1G2 VAV3 IGLV2-33(1-?) Ig lambda chain V-I region VOR WIPF1 WIPF1 IGLV1-40(1-?) ELMO2 IGLV7-46(1-?) IGHG2 IGLV1-40(1-?) Ig lambda chain V-IV region Kern Ig kappa chain V-I region Daudi IGLV5-37(1-?) IGLV11-55(1-?) IGLV11-55(1-?) IGLC3 p-Y256-WASL Lma amastigote surface IGLV2-23(1-?) Ig heavy chain V-III region DOB FYN Ig kappa chain V-II region RPMI 6410 Ig kappa chain V region EV15 ARPC3 Ig heavy chain V-III region WEA IGHV1-2 IGKV2-28 IGLV7-43(1-?) Ig lambda chain V-III region LOI Ig heavy chain V-II region MCE ARPC2 Ig heavy chain V-I region HG3 IGLV11-55(1-?) IGLV1-36(1-?) IGLV5-45(1-?) p-Y151-WASF3 GRB2-1 IGLV10-54(1-?) Ig heavy chain V-II region OU IGLC1 Ig lambda chain V-III region LOI Lma amastigote surface IGLV1-36(1-?) Ig lambda chain V-III region LOI IGLV2-23(1-?) Ig heavy chain V-III region WEA ARPC4 Ig lambda chain V-I region VOR Ig kappa chain V region EV15 IGKVA18(21-?) IgG:Lmaantigens:FCGR3A:p-CD3 dimers:p-6Y-SYKPI(3,4,5)P3 IGHG3 ABI2 IGKC IGHG1 IGLV5-45(1-?) IGKV1-5(23-?) BRK1 Ig kappa chain V-I region AG IGLV1-44(1-?) Ig heavy chain V-II region MCE ATP Ig lambda chain V-I region NEW IGLC3 CYFIP1 IGHV(1-?) p-4S-ABI2 Ig lambda chain V-I region NEW Ig kappa chain V-II region Cum IGLV10-54(1-?) IGLV8-61(1-?) Ig kappa chain V-III region VG IGLV10-54(1-?) IGLV7-43(1-?) Ig heavy chain V-II region ARH-77 IGLV1-36(1-?) Ig lambda chain V-IV region Bau IGHG2 CD3G IGLC2 Ig heavy chain V-II region OU NCKIPSD Ig lambda chain V-I region HA ACTR2 Ig lambda chain V-II region NEI Lma amastigote surface IGHG1 IgH heavy chain V-III region VH26 precursor Ig heavy chain V-II region MCE VAV2 Ig heavy chain V-II region OU IGLV4-69(1-?) N-WASP IGLC1 IGLV2-11(1-?) p-T185,Y187-MAPK1 IGHG4 ACTR3 Ig kappa chain V-III region B6 Ig heavy chain V-III region TRO Ig heavy chain V-III region DOB NCKIPSD IGKVA18(21-?) p-6Y-CD247 Ig heavy chain V-II region NEWM Ig heavy chain V-II region NEWM Ig lambda chain V-I region HA CYFIP2 IGHV1-2 Ig kappa chain V-II region FR Ig kappa chain V-II region RPMI 6410 IGLV3-16(1-?) Ig lambda chain V-II region BOH RAC1 Ig kappa chain V-I region AU ARPC2 Ig heavy chain V-III region KOL Ig kappa chain V-II region RPMI 6410 CRK ABI1 ARPC5 BAIAP2 Ig lambda chain V-I region VOR Ig kappa chain V-I region AG PI(3,4,5)P3 PI(3,4,5)P3 Ig heavy chain V-III region JON ACTG1 NCKAP1 IGLC7 FCGR3A Ig kappa chain V-I region Wes Ig lambda chain V-II region BOH Ig heavy chain V-II region ARH-77 ATP ELMO1 IGLV7-43(1-?) Ig heavy chain V-I region EU Ig kappa chain V-II region RPMI 6410 IGLV3-16(1-?) IGLV7-43(1-?) GRB2-1 Ig kappa chain V-II region Cum N-WASP Ig kappa chain V-I region BAN Ig lambda chain V-III region SH IGHG3 RAC1 Ig kappa chain V-I region Daudi Ig lambda chain V-IV region Hil IGLC1 Ig heavy chain V-III region CAM Ig lambda chain V-IV region Kern IGLV7-46(1-?) IGKC IGLV5-37(1-?) IGLV2-11(1-?) IGHV1-2 IGLV7-43(1-?) CYFIP1 IGLV2-11(1-?) Ig lambda chain V-II region TOG ACTR3 ARPC2 YES1 WIPF1 Ig kappa chain V-I region BAN p-Y173-VAV3 IGLV1-36(1-?) IGLV8-61(1-?) ACTR2 p-6Y-SYK PI(4,5)P2 IGLV4-69(1-?) LPG1G2 Ig lambda chain V-IV region Hil Ig kappa chain V-II region RPMI 6410 Ig heavy chain V-III region JON Ig lambda chain V-I region NEW IGLC3 IGLV7-43(1-?) IGLV3-22(1-?) Ig lambda chain V-I region HA IGKV3D-20 N-WASP Ig lambda chain V-III region SH IGLV8-61(1-?) ARPC1B Ig heavy chain V-II region OU Ig lambda chain V-I region NEWM ACTR3 IGHG1 IGKV4-1(21-?) IGLC7 IGLV5-37(1-?) VAV2 p-Y291-WAS p-Y151,S,T-WASF3 Ig lambda chain V-I region NEW Ig lambda chain V-I region VOR G-actinCYFIP2 Ig kappa chain V-I region AU Ig heavy chain V-III region WEA IGKV2-28 ACTG1 Ig heavy chain V-I region HG3 CDC42 Ig heavy chain V-III region KOL IGHG2 IGHG3 BAIAP2 IGKVA18(21-?) Ig lambda chain V-III region SH CD3G CD247-1 Ig heavy chain V-III region DOB IGKV1-12 Ig kappa chain V-I region DEE Ig kappa chain V-I region BAN CDC42 Ig lambda chain V-II region NEI Ig heavy chain V-III region CAM MYO9B IGKV1-12 CDC42:GTPIg heavy chain V-II region NEWM PI(4,5)P2:WASP/N-WASPIGLC3 Ig kappa chain V-I region Wes IGHV1-2 IGLV2-11(1-?) IGLV4-3(1-?) IGHV1-2 Ig heavy chain V-II region MCE ATP IGLV(23-?) WAVE2, WASP, N-WASPGTP Src family kinases(SFKs)IGLV3-25(1-?) IGHG1 WIPF2 IGKV3D-20 IGLC3 IGLV10-54(1-?) Ig kappa chain V-III region B6 Ig lambda chain V-II region NEI Ig kappa chain V-I region HK101 ACTB(1-375) GDPIg heavy chain V-III region BRO IGLV2-23(1-?) IGLV7-46(1-?) BRK1 ATP Ig kappa chain V-I region Gal p-6Y-SYK Ig heavy chain V-II region NEWM Ig lambda chain V-I region NEW Ig lambda chain V-IV region Hil IGLV4-3(1-?) p-Y151,S,T-WASF1 NCK1 Ig heavy chain V-I region HG3 IGKC Ig lambda chain V-II region TOG IGLV11-55(1-?) IGLV10-54(1-?) WASF2 Ig kappa chain V-I region DEE IGLV3-27(1-?) Unknown GEFIg heavy chain V-III region CAM Ig kappa chain V-III region POM ADP IGLV4-3(1-?) IGKV2D-30 IGKC Ig lambda chain V-I region HA IGHV(1-?) ACTB(1-375) IGLC1 Ig lambda chain V region 4A Ig kappa chain V-I region HK101 IGLV2-33(1-?) IGLV5-37(1-?) IGLV1-40(1-?) IGLV2-33(1-?) Ig lambda chain V-II region MGC IGHG3 Ig kappa chain V-III region POM IGLV4-60(1-?) p-6Y-CD247 Ig kappa chain V-I region Gal IGKV1-5(23-?) Ig kappa chain V-I region BAN ADPIGKV2D-30 Ig kappa chain V-I region BAN Ig kappa chain V region EV15 IGLC7 IGLV3-25(1-?) Ig heavy chain V-III region BRO ABI1 IGLV11-55(1-?) Ig lambda chain V-II region NEI IGKV1-5(23-?) NCK1 ABI2 Ig lambda chain V region 4A Ig heavy chain V-III region CAM IGLV7-46(1-?) p-Y-WRC:IRSp53/58:RAC1:GTP:PIP3IGLV5-45(1-?) Ig kappa chain V-III region POM ABI1 IGLV1-44(1-?) Ig kappa chain V-I region HK101 F-actin NCKAP1 Ig heavy chain V-II region NEWM IgGGRB2-1 IGLV7-43(1-?) IGKV2D-30 IGLC6 NCKIPSD Ig lambda chain V-II region MGC IGKV1-12 Ig kappa chain V-III region B6 Ig heavy chain V-III region KOL IGHV1-2 ARPC2 p-6Y-CD247 IGLV4-69(1-?) IGKV3D-20 Ig kappa chain V-III region B6 IGHV1-2 IGHV(1-?) ATPIg kappa chain V-III region POM IGLV5-37(1-?) Ig lambda chain V-III region SH IGLC6 IGKVA18(21-?) IGLV1-44(1-?) NCK1 Ig lambda chain V-VI region AR IGLV1-40(1-?) ARPC1B IGHG4 IGKV4-1(21-?) Ig kappa chain V-II region Cum IGLV2-11(1-?) Ig lambda chain V-III region SH p-5S-ABI1 IGLC7 IGLV3-12(1-?) ATPIgH heavy chain V-III region VH26 precursor IGHG1 Ig heavy chain V-III region CAM Ig heavy chain V-II region ARH-77 Ig lambda chain V-I region NEWM Ig kappa chain V-III region POM IgG:Lmaantigens:FCGR3A:p-CD3 dimersMYO10 Ig kappa chain V-II region RPMI 6410 NCKAP1L MYH2 NCK1 GRB2-1 p-6Y-CD247 VAV1,2,3Ig kappa chain V region EV15 Ig heavy chain V-III region CAM IGKV1-5(23-?) p-Y150,S343,T346-WASF2 Ig kappa chain V-I region HK101 WAVE RegulatoryComplexIg lambda chain V-IV region Kern Ig kappa chain V-I region AU Ig lambda chain V-I region NEW ATPIGKV1-12 IGLC2 Ig heavy chain V-III region DOB IGLV8-61(1-?) IGLV3-27(1-?) IGKV2-28 p-Y151,S,T-WASF3 Ig kappa chain V-III region POM BAIAP2 LYN Ig lambda chain V-IV region Hil Ig kappa chain V region EV15 NCKAP1 Ig heavy chain V-III region WEA IGLV11-55(1-?) Ig lambda chain V-I region NEWM IGKV1-12 IGLC2 Ig heavy chain V-II region WAH Ig heavy chain V-I region HG3 MYO9B Ig heavy chain V-III region BUT IGLV4-69(1-?) Ig heavy chain V-III region JON p-Y151-WASF3 ARPC1B WAS p-6Y-CD247 Ig kappa chain V-I region DEE ARPC1A ABI2 Ig heavy chain V-II region MCE Ig heavy chain V-I region EU Ig heavy chain V-II region ARH-77 RAC1 IGHG2 IGLV3-12(1-?) CDC42 IGLV4-3(1-?) IGKV2D-30 IGLC2 Ig heavy chain V-III region BRO Ig kappa chain V region EV15 Ig kappa chain V-I region BAN IGLV1-36(1-?) IGKV1-12 ACTB(1-375) IGHG3 RAC1:GTPIg heavy chain V-II region ARH-77 Ig lambda chain V-III region SH Ig heavy chain V-III region JON Ig kappa chain V region EV15 IGHG2 BRK1 Ig kappa chain V-I region Wes BRK1 IgH heavy chain V-III region VH26 precursor IGHG1 Ig heavy chain V-III region BRO Myosin-ActinfilamentsIg heavy chain V-II region WAH Ig lambda chain V-IV region Bau IGLV7-46(1-?) Ig heavy chain V-I region HG3 Ig heavy chain V-I region HG3 IGLV4-60(1-?) ARPC1A IGLV2-11(1-?) IGLC1 IGLV3-25(1-?) IGLV2-23(1-?) IGLV3-25(1-?) IGLV3-12(1-?) Ig kappa chain V-I region AU Lma amastigote surface Ig lambda chain V-II region BOH IGHG2 ACTR3 IGLV3-22(1-?) p-5S-ABI1 Ig kappa chain V-III region B6 IGLV1-36(1-?) Ig kappa chain V-I region Daudi IGKV4-1(21-?) Ig kappa chain V-II region FR CDC42 IGLV1-44(1-?) IGLV2-18(1-?) Ig lambda chain V region 4A ACTR2 p-Y150-WASF2 LPG1G2 Ig heavy chain V-I region HG3 Ig lambda chain V-III region LOI Ig lambda chain V-I region HA IGLV3-12(1-?) Ig heavy chain V-II region NEWM IGKV2-28 Ig heavy chain V-III region DOB Ig lambda chain V-IV region Bau IGLV4-69(1-?) Ig lambda chain V-II region TOG Ig kappa chain V-II region FR IGLC2 FCGR3A IGKV1-5(23-?) PI(3,4,5)P3 Ig heavy chain V-III region TRO IGKV3D-20 Ig heavy chain V-III region WEA Ig kappa chain V-III region POM Ig heavy chain V-II region NEWM Ig heavy chain V-III region BRO IGLC7 LYN p-Y150,S343,T346-WASF2 GTP Ig kappa chain V-I region AU IgH heavy chain V-III region VH26 precursor IGLC2 SRC-1 ADP IGLV3-25(1-?) ARPC3 Ig lambda chain V-IV region Bau Ig lambda chain V-I region VOR Ig lambda chain V region 4A Ig kappa chain V-I region BAN ARPC3 CYFIP2 Ig heavy chain V-III region TRO Ig kappa chain V-I region AG IGLV4-69(1-?) Ig lambda chain V-III region SH PI(4,5)P2 IGLV5-37(1-?) IGLC1 Lma amastigotesurfaceARPC5 HCK p-Y174-VAV1 Ig heavy chain V-III region BUT Ig lambda chain V-II region MGC IGLC1 IGKV2-28 Ig kappa chain V-I region Wes PI(4,5)P2 p-Y151-WASF1 PiIg heavy chain V-III region WEA IGLV1-44(1-?) IGKC p-Y151-WASF1 NCKAP1 IGHG4 ACTR2 VAV3 ARPC1A GTP IGHV7-81(1-?) IGLV11-55(1-?) WASF3 LPG1G2 IGHG4 CYFIP2 Src-kinasesIGLV1-44(1-?) Ig heavy chain V-II region OU Ig kappa chain V-II region FR IGHV7-81(1-?) IGLV2-23(1-?) Ig kappa chain V-III region VG IGHV7-81(1-?) p-Y160,Y171-CD3G Ig lambda chain V-II region MGC IGLV3-12(1-?) ARPC1A GRB2-1 Ig lambda chain V-I region VOR ARPC4 LPG1G2 IGLV3-16(1-?) Ig heavy chain V-II region WAH Ig heavy chain V-I region HG3 IGKV4-1(21-?) Ig lambda chain V-I region NEWM IGHV(1-?) Ig lambda chain V-IV region Bau WIPF3 IGHG1 p-Y150-WASF2 IGHV1-2 Ig kappa chain V-III region VG ATP GTP GDP IGLV5-37(1-?) IGHG3 IGHG2 Ig heavy chain V-III region TRO Ig kappa chain V-II region FR IGKV2-28 Ig heavy chain V-II region WAH CYFIP2 IGLV3-25(1-?) p-Y151-WASF1 IGLC3 IGLV4-3(1-?) p-Y151,S,T-WASF1 PI(3,4,5)P3 Ig lambda chain V-I region HA Ig kappa chain V-I region Wes IGHG2 Ig kappa chain V-II region RPMI 6410 IGLV1-44(1-?) IGKVA18(21-?) Ig heavy chain V-III region BUT Ig kappa chain V-I region Daudi IGLV(23-?) IGLV7-43(1-?) MYH9 NCKAP1L Ig kappa chain V-I region AU IGHG1 IGLV1-44(1-?) VAV1 Ig lambda chain V-II region NEI Ig kappa chain V-III region POM IGLV3-16(1-?) Ig lambda chain V-I region HA IGHV1-2 IGHG4 IGLV4-3(1-?) CDC42 IGHG2 MYO5A Ig kappa chain V-I region BAN CDC42:GTP:WASP/N-WASP:WIP:SH3 proteinsIg lambda chain V-II region TOG Ig heavy chain V-II region NEWM IGLV8-61(1-?) p-Y291-WAS IGLV2-18(1-?) NCK1 IGHV7-81(1-?) ACTG1 IGLV2-33(1-?) SYKIg heavy chain V-I region EU Ig lambda chain V-II region BOH Ig kappa chain V-I region HK101 IGKV1-12 CDC42:GDPIGHV1-2 ARPC5 Ig heavy chain V-I region EU ACTG1 ARPC3 IGLV(23-?) Ig lambda chain V-II region BOH IGLV3-12(1-?) GTP GTP Ig kappa chain V-II region FR Ig heavy chain V-III region BRO Lma amastigote surface IGLV(23-?) Ig heavy chain V-III region KOL GDP WIPF3 Ig lambda chain V-IV region Hil ATP Ig heavy chain V-III region WEA Ig kappa chain V-II region FR IGKVA18(21-?) Ig kappa chain V-I region Daudi IGLV4-3(1-?) Ig heavy chain V-III region BUT Ig kappa chain V-I region Gal IGKV2D-30 Ig heavy chain V-III region WEA ACTR2 IGLV1-40(1-?) IGLC7 PI(3,4,5)P3Ig kappa chain V-II region Cum Ig kappa chain V-I region AG Ig kappa chain V-I region BAN IGLV10-54(1-?) Ig heavy chain V-I region EU IGKV1-5(23-?) IgG:Lmaantigens:FCGR3A:p-CD3 dimers:SYKMYO1C IGLC2 LPG1G2Ig kappa chain V-I region Daudi Ig kappa chain V-III region POM Ig kappa chain V region EV15 IGLV3-27(1-?) WIPF3 IGHV(1-?) IGLV8-61(1-?) Ig kappa chain V-I region Gal p-Y256-WASL Ig kappa chain V-I region DEE GTPPI(4,5)P2RAC1:GDPIGLV10-54(1-?) ARPC2 IGHG4 p-Y160,Y171-CD3G IGLV11-55(1-?) Ig kappa chain V-I region DEE Ig lambda chain V-I region NEWM Ig heavy chain V-II region MCE p-Y,S,T-WRC:IRSp53/58:RAC1:GTP:PIP3IGHG1 Ig heavy chain V-III region KOL Ig lambda chain V-IV region Kern WRC:IRSp53/58:RAC1:GTP:PIP3IGLV2-11(1-?) Ig kappa chain V-I region AG p-4S-ABI2 ARP2/3 complex (ATPbound)Ig kappa chain V-I region Gal MYO1C Ig heavy chain V-II region OU IGKV4-1(21-?) IGLV3-25(1-?) GTP IGLV2-33(1-?) Ig heavy chain V-II region OU IGLV10-54(1-?) ARPC4 Ig lambda chain V-IV region Hil BRK1 WIPF1 IgH heavy chain V-III region VH26 precursor Ig lambda chain V-III region SH F-actin NCKAP1L IGLV1-44(1-?) IGHV1-2 IGLV4-60(1-?) F-actin IGLV2-11(1-?) Ig heavy chain V-I region EU Ig heavy chain V-II region OU Ig lambda chain V-II region TOG ARPC1B Ig lambda chain V-VI region AR Ig kappa chain V-I region AG IGHG4 Ig heavy chain V-III region JON PI(3,4,5)P3 Ig heavy chain V-III region KOL IGLV2-33(1-?) IGLV4-60(1-?) IGLC7 IGLV8-61(1-?) IGLV10-54(1-?) IGLV4-69(1-?) Ig lambda chain V-II region MGC p-Y160,Y171-CD3G FGR Lma amastigote surface IGLV5-37(1-?) ACTR2 Ig lambda chain V-IV region Hil Ig heavy chain V-III region BRO LPG1G2 IGLV1-40(1-?) IGLC3 Ig lambda chain V-III region SH IGHG4 Ig heavy chain V-II region MCE BAIAP2 Ig kappa chain V-I region AG Ig lambda chain V-IV region Hil WAVE2, WASP,N-WASP:ARP2/3complex:G-actinATP IGLV(23-?) IGLV10-54(1-?) Ig lambda chain V-I region NEW Ig kappa chain V-III region B6 IGLV2-18(1-?) WAS IGLC1 Ig lambda chain V-II region TOG NCKAP1L Ig lambda chain V-IV region Kern IGLV5-37(1-?) IGLV4-60(1-?) WIPF3 IGLV3-27(1-?) ABI1 RAC1 PI(3,4)P2Ig kappa chain V-I region DEE PI(4,5)P2 PI(3,4)P2 ATP Motherfilament:ARP2/3:actin:ADPIGHV7-81(1-?) Ig heavy chain V-III region WEA FCGR3A IGLC6 Ig heavy chain V-III region TRO p-6Y-SYK Ig heavy chain V-I region EU Actin filament boundMyosin-XIGLV4-69(1-?) IGLV3-22(1-?) Ig kappa chain V-I region Daudi ABI2 PI(4,5)P2 Ig lambda chain V-IV region Hil Lma amastigote surface IGLC2 Ig heavy chain V-II region ARH-77 IGLV2-18(1-?) IGLC6 Ig lambda chain V-II region NEI Ig lambda chain V region 4A ADPIGHG1 IGLV1-36(1-?) PI(3,4,5)P3 Ig lambda chain V-I region HA Ig lambda chain V-II region TOG WIPF2 IGKV1-5(23-?) Motherfilament:branchingcomplexIg heavy chain V-III region BUT Ig heavy chain V-II region WAH WASF2 Ig kappa chain V-I region Gal p-Y151,S,T-WASF3 IGLC7 ARPC1B p-Y151,S,T-WASF1 p-5S-ABI1 IGLC7 Ig kappa chain V region EV15 IGLV8-61(1-?) IGLV3-25(1-?) IGLC3 Ig kappa chain V-III region VG Ig kappa chain V region EV15 Src family kinases(SFKs)IGLV2-11(1-?) IGLV3-27(1-?) IGKC Ig heavy chain V-III region DOB GDP Ig kappa chain V-I region Wes IGHV7-81(1-?) Ig lambda chain V-I region HA Ig lambda chain V-IV region Hil VAV2 Ig kappa chain V-III region POM Ig heavy chain V-II region ARH-77 Ig lambda chain V-IV region Kern ATPBAIAP2 IGLV3-12(1-?) Ig heavy chain V-III region WEA DOCK1 Ig lambda chain V-VI region AR IGKV1-5(23-?) Ig lambda chain V-II region MGC IGHG2 Ig heavy chain V-III region CAM BAIAP2 Ig heavy chain V-II region OU Ig kappa chain V-I region AG GTP Ig kappa chain V-I region AU Ig heavy chain V-III region JON Ig heavy chain V-II region ARH-77 Ig lambda chain V-I region NEWM BRK1 Ig heavy chain V-II region MCE Ig heavy chain V-III region DOB IGLV5-45(1-?) Ig lambda chain V-III region LOI IGHV(1-?) GRB2-1 Ig lambda chain V-II region NEI IGLV1-36(1-?) IGKV1-5(23-?) Ig kappa chain V-I region Wes Ig heavy chain V-II region WAH Ig heavy chain V-III region KOL IGLV2-18(1-?) F-actin IGHV(1-?) Ig lambda chain V-II region BOH G-actinARPC3 IGLV5-45(1-?) p-Y150-WASF2 HCK RAC1 ABI2 Ig kappa chain V-I region BAN Ig heavy chain V-III region JON Ig heavy chain V-III region JON Ig lambda chain V-IV region Bau Ig kappa chain V-I region HK101 IGLV3-22(1-?) Ig kappa chain V-I region HK101 IGLV5-37(1-?) IGLV5-45(1-?) Ig lambda chain V-II region BOH IGLV4-60(1-?) NCKIPSD ELMO2 WASF3 Ig heavy chain V-III region DOB Ig lambda chain V-I region NEWM Ig heavy chain V-III region TRO Ig heavy chain V-III region DOB ATPIg kappa chain V-III region B6 GTP Ig lambda chain V-II region TOG NCKAP1 p-Y256-WASL Ig lambda chain V-I region NEW IGKV1-12 IGLV1-36(1-?) Ig lambda chain V-II region TOG RAC1 IGKV4-1(21-?) Ig kappa chain V-I region DEE Ig lambda chain V-IV region Kern Myosin-X dimerIGLV3-22(1-?) Ig lambda chain V-VI region AR Ig lambda chain V-IV region Bau ABL1Ig heavy chain V-II region MCE Ig lambda chain V-I region VOR Ig lambda chain V-VI region AR NCK1 Ig lambda chain V-VI region AR Ig lambda chain V-I region HA Ig kappa chain V-I region Gal FCGR3A Ig heavy chain V-II region WAH WIPF2 NCKIPSD IGLV4-69(1-?) IGHV7-81(1-?) Ig kappa chain V-III region POM CYFIP1 Ig kappa chain V-III region VG Ig heavy chain V-III region TRO IGKV2D-30 IGKC IgG:Leishmaniasurface:p-FCGR3A:p-6Y-SYK:CRKII:DOCK180:ELMOIGLV3-22(1-?) ATPIGLC6 IGLV4-60(1-?) Ig lambda chain V-II region TOG IGKV1-12 RAC1 WIPF1 Ig lambda chain V-II region NEI IGLV2-11(1-?) IGLC2 ACTR3 Ig heavy chain V-III region JON IGHV(1-?) p-Y151-WASF3 Ig heavy chain V-I region EU FYN Ig heavy chain V-I region HG3 IGLV2-33(1-?) YES1 IGKV1-5(23-?) Ig lambda chain V-II region MGC Ig lambda chain V-II region BOH Ig kappa chain V-I region Wes Ig lambda chain V region 4A Ig kappa chain V-III region VG IGKV3D-20 IGKVA18(21-?) Ig kappa chain V-II region FR Ig heavy chain V-III region BRO IGHV1-2 IGKV1-12 Ig lambda chain V-II region MGC Ig heavy chain V-III region WEA IGLV3-22(1-?) IGKV2-28 Ig lambda chain V-II region NEI Ig heavy chain V-III region BUT IgG:Leishmaniasurface:FCGR3AIGLV2-23(1-?) Ig heavy chain V-I region HG3 Ig heavy chain V-III region KOL IGLC6 IGLV8-61(1-?) Ig lambda chain V-IV region Bau Ig lambda chain V-IV region Kern Ig kappa chain V-I region DEE Ig kappa chain V-II region RPMI 6410 IGLV4-3(1-?) Lma amastigote surface IGLC7 IGHV(1-?) Ig lambda chain V-IV region Bau LPG1G2 BRK1 IGLV3-16(1-?) IgG:Leishmaniasurface:p-FCGR3A:p-6Y-SYK:p-VAV1,2,3:PI(3,4,5)P3IGLV10-54(1-?) IGHG4 ABI1 IGHG1 IGLV4-3(1-?) GTPIGLV7-43(1-?) IGKV2D-30 ACTR3 IGKVA18(21-?) Ig kappa chain V-I region DEE IGLV2-18(1-?) Ig kappa chain V-II region RPMI 6410 IGKC Ig kappa chain V-II region RPMI 6410 IGKV1-12 IGLV2-18(1-?) IGLV11-55(1-?) Ig kappa chain V region EV15 ARPC5 FCGRIIIA:CD3G/CD3ZdimersIGLV7-46(1-?) IGLV5-45(1-?) IGHG3 ARPC4 IGLV1-40(1-?) Ig kappa chain V-III region VG Ig kappa chain V-I region AU GDPIGLV1-36(1-?) NCKAP1L IGHV(1-?) Ig heavy chain V-III region KOL Ig lambda chain V-VI region AR N-WASP IGLV(23-?) RAC1 Ig heavy chain V-I region EU Ig heavy chain V-III region TRO IGLC7 IGLV3-12(1-?) ABI2 Pip-Y160,Y171-CD3G Ig heavy chain V-III region DOB NCKAP1L Motherfilament:branchingcomplex:daughterfilamentDOCK1 Ig lambda chain V-I region VOR Ig kappa chain V-II region Cum Ig kappa chain V-I region AU VAV1 IGKV1-5(23-?) IGLV(23-?) MYH9 Ig lambda chain V-II region NEI VAV3 Ig kappa chain V-III region VG Ig lambda chain V-III region LOI PI(3,4,5)P3 Ig lambda chain V-IV region Hil IGLV1-40(1-?) IGKV3D-20 IGHV(1-?) IGKV2-28 LPG1G2 Ig heavy chain V-III region BRO FCGR3A p-T202,Y204-MAPK3 ADPLma amastigote surface p-Y291-WAS LPG1G2 Ig heavy chain V-I region EU IGKV4-1(21-?) p-4S-ABI2 Ig heavy chain V-III region JON p-Y150,S343,T346-WASF2 Ig lambda chain V-I region VOR IGLV3-25(1-?) Ig lambda chain V-IV region Kern Ig kappa chain V-I region HK101 Ig kappa chain V-I region Wes IGLC3 IGLV2-33(1-?) Ig lambda chain V-III region SH Ig heavy chain V-I region EU Ig lambda chain V-II region MGC Ig heavy chain V-III region JON IGLV2-18(1-?) Ig kappa chain V-II region FR Ig lambda chain V-IV region Hil Ig heavy chain V-III region BRO IGLV8-61(1-?) ARPC1A ARPC2 IGHG4 Ig heavy chain V-III region BUT p-6Y-CD247 ADPIGLC2 Ig lambda chain V-III region LOI IGHG2 Ig lambda chain V-I region NEW Ig heavy chain V-III region TRO MYH2 IGHV7-81(1-?) WASF1 IGLV3-16(1-?) Ig heavy chain V-III region BUT WIPF2 IGKV4-1(21-?) IGLV5-45(1-?) IGLV(23-?) NCKIPSD Ig lambda chain V-III region LOI FCGR3A IGKV2D-30 IGLV1-44(1-?) Ig heavy chain V-II region NEWM IGLV7-46(1-?) Ig heavy chain V-III region DOB ARPC5 IGLV4-69(1-?) IgG:Lma antigensIGKV3D-20 IGLV7-46(1-?) IGLV2-33(1-?) Ig kappa chain V-I region DEE IGLC2 Ig kappa chain V-I region BAN ARPC1B Ig heavy chain V-III region BRO IGLV11-55(1-?) IGLV3-27(1-?) ARPC4 RAC1 ATPWIPF2 Ig lambda chain V-II region MGC Ig heavy chain V-III region BUT IGLV7-43(1-?) p-Y151-WASF1 Ig lambda chain V region 4A IGLV11-55(1-?) Ig heavy chain V-II region NEWM IGLV4-3(1-?) ADPIg heavy chain V-III region BUT GTPIgH heavy chain V-III region VH26 precursor Ig heavy chain V-II region ARH-77 IGLV3-16(1-?) Ig lambda chain V-IV region Bau ARPC1A IGKC Ig lambda chain V-III region LOI Ig heavy chain V-III region JON Ig kappa chain V-I region Gal Lma amastigote surface Ig lambda chain V region 4A PI(3,4,5)P3 IGKV4-1(21-?) CD247-1 F-actin IGLC6 Ig lambda chain V-II region BOH IgG:Lma amastigotesurfaceIg heavy chain V-II region ARH-77 Ig heavy chain V-III region KOL IGLV4-69(1-?) Ig heavy chain V-III region CAM Ig heavy chain V-II region WAH IGLV3-16(1-?) IGHV7-81(1-?) IGLV5-45(1-?) IGLC6 GTP CYFIP1 Ig lambda chain V-I region HA IGLV3-27(1-?) IGLV(23-?) Ig heavy chain V-III region TRO ARPC4 Ig heavy chain V-II region WAH CYFIP1 Ig kappa chain V-I region Daudi IgG:Leishmaniasurface:FCGR3Ap-CD3dimers:p-6Y-SYK:VAV1,2,3:PI(3,4,5)P3IgG:Lmaantigens:FCGR3A:CD3dimersWIPF3 Ig lambda chain V-VI region AR Ig kappa chain V-I region AG Ig lambda chain V-III region LOI IGLC3 Ig heavy chain V-III region DOB IgH heavy chain V-III region VH26 precursor WIPF3 Ig kappa chain V-II region Cum Ig heavy chain V-III region KOL IGLV(23-?) IGLV7-46(1-?) IGLV2-18(1-?) ELMO1 VAV1 IGHG1 GTP Ig kappa chain V-III region VG ACTB(1-375) IGLV2-23(1-?) IGLV2-23(1-?) Ig lambda chain V-II region NEI Ig kappa chain V-II region FR Ig lambda chain V-IV region Kern IGLV1-40(1-?) Ig kappa chain V-III region VG WASP/N-WASPIg kappa chain V region EV15 IGHV7-81(1-?) Ig kappa chain V-I region HK101 IGLC1 RAC1:GDPIGLV3-27(1-?) Ig heavy chain V-III region CAM IGLV1-36(1-?) Ig heavy chain V-II region ARH-77 ARPC3 SYK IGLV11-55(1-?) IGLV1-36(1-?) Ig kappa chain V-II region FR IGLV7-46(1-?) Ig lambda chain V-VI region AR IgH heavy chain V-III region VH26 precursor Ig kappa chain V-II region RPMI 6410 Ig kappa chain V-I region AU p-Y291-WAS ARPC2 IGLV5-45(1-?) Ig kappa chain V-I region AG PI(4,5)P2 IGLV4-60(1-?) Ig heavy chain V-I region HG3 Ig kappa chain V-II region Cum IGKV1-12 IGLV7-46(1-?) IGLV3-12(1-?) IGHG3 IGLV8-61(1-?) IGLV4-60(1-?) Ig kappa chain V-I region Gal Ig kappa chain V-III region B6 IGLC1 IGLV5-37(1-?) WAS IGLV3-27(1-?) Ig heavy chain V-I region HG3 Ig lambda chain V-I region NEWM IGLV4-60(1-?) IGLV2-33(1-?) IGLV10-54(1-?) IGKV4-1(21-?) ARPC4 Ig kappa chain V-I region Daudi Ig heavy chain V-II region OU Ig kappa chain V-I region Daudi IGKVA18(21-?) IGLC6 IGKV3D-20 Ig kappa chain V-I region HK101 IGKC IGLV2-33(1-?) IGLV3-22(1-?) Ig kappa chain V-I region Daudi FCGR3A MyosinIGKVA18(21-?) ADPp-Y172-VAV2 IGLC3 Ig kappa chain V-II region Cum Ig heavy chain V-II region MCE Ig heavy chain V-III region CAM p-6Y-SYK IGLV3-22(1-?) Ig kappa chain V-II region Cum WIP family proteinsIg lambda chain V-II region BOH Ig heavy chain V-II region WAH IGLV5-37(1-?) IGLV4-3(1-?) Ig lambda chain V region 4A Ig lambda chain V-IV region Kern IgG:LPG1G2Ig heavy chain V-II region WAH Ig heavy chain V-II region WAH Ig kappa chain V-III region VG Ig lambda chain V-IV region Kern Ig heavy chain V-III region BRO IGKV2-28 IGLV(23-?) p-Y256-WASL Ig heavy chain V-III region CAM IGLV4-60(1-?) IGLV2-23(1-?) Ig kappa chain V-I region BAN NCKAP1 BAIAP2Ig kappa chain V-III region POM IGHG3 IGLV2-18(1-?) p-Y151-WASF3 MYO5A IGLV1-44(1-?) Ig heavy chain V-II region OU CDC42:GTP:WASP/N-WASPIGKVA18(21-?) Ig lambda chain V-I region NEW Ig lambda chain V-I region NEWM IGKV4-1(21-?) Ig heavy chain V-II region NEWM IGLV5-45(1-?) ACTR3 CDC42 Ig kappa chain V-II region RPMI 6410 Ig lambda chain V-III region SH IgH heavy chain V-III region VH26 precursor Ig heavy chain V-III region TRO


Description

The Fc gamma receptors (FCGRs) have been reported to facilitate Leishmania internalization, especially when in its amastigote form (Ueno et al. 2012). Following cell-to-cell propagation within an established infection or reinfection of a previously infected host, the IgG produced by the host covers the surface of Leishmania amastigote parasites, making them more susceptible to phagocytosis through FCGRs (Polando et al. 2013).

Classically, phagocytosis via FCGRs has been associated with the subsequent activation of Rac GTPases and Cdc42 which in turn activate the phagocyte's NADPH oxidase, contributing to the activation of killing mechanisms (Ueno et al. 2012). View original pathway at Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 9664422
Reactome-version 
Reactome version: 73
Reactome Author 
Reactome Author: Jassal, Bijay

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Bibliography

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  57. 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
  58. 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
  59. Thomas BN, Buxbaum LU.; ''FcgammaRIII mediates immunoglobulin G-induced interleukin-10 and is required for chronic Leishmania mexicana lesions.''; PubMed Europe PMC Scholia
  60. Polando R, Dixit UG, Carter CR, Jones B, Whitcomb JP, Ballhorn W, Harintho M, Jerde CL, Wilson ME, McDowell MA.; ''The roles of complement receptor 3 and Fcγ receptors during Leishmania phagosome maturation.''; PubMed Europe PMC Scholia
  61. Bompard G, Caron E.; ''Regulation of WASP/WAVE proteins: making a long story short.''; PubMed Europe PMC Scholia
  62. 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
  63. Miki H, Suetsugu S, Takenawa T.; ''WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac.''; PubMed Europe PMC Scholia
  64. 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

History

CompareRevisionActionTimeUserComment
114922view16:44, 25 January 2021ReactomeTeamReactome version 75
113367view11:44, 2 November 2020ReactomeTeamReactome version 74
112818view18:23, 9 October 2020DeSlOntology Term : 'phagocytosis pathway' added !
112766view16:16, 9 October 2020ReactomeTeamNew 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)
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)
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: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)
CRK ProteinP46108 (Uniprot-TrEMBL)
CRK:DOCK180:ELMO1,ELMO2ComplexR-HSA-2029141 (Reactome)
CYFIP1 ProteinQ7L576 (Uniprot-TrEMBL)
CYFIP2 ProteinQ96F07 (Uniprot-TrEMBL)
DOCK1 ProteinQ14185 (Uniprot-TrEMBL)
ELMO1 ProteinQ92556 (Uniprot-TrEMBL)
ELMO2 ProteinQ96JJ3 (Uniprot-TrEMBL)
F-actin R-HSA-201877 (Reactome)
F-actinR-HSA-201877 (Reactome)
FCGR3A ProteinP08637 (Uniprot-TrEMBL)
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)
HCK ProteinP08631 (Uniprot-TrEMBL)
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)
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:LPG1G2ComplexR-HSA-9675736 (Reactome)
IgG:Leishmania surface:FCGR3AComplexR-HSA-9666434 (Reactome)
IgG:Leishmania

surface:FCGR3Ap-CD3

dimers:p-6Y-SYK:VAV1,2,3:PI(3,4,5)P3		ComplexR-HSA-9666421 (Reactome)
IgG:Leishmania surface:p-FCGR3A:p-6Y-SYK:CRKII:DOCK180:ELMOComplexR-HSA-9666431 (Reactome)
IgG:Leishmania surface:p-FCGR3A:p-6Y-SYK:p-VAV1,2,3:PI(3,4,5)P3ComplexR-HSA-9666423 (Reactome)
IgG:Lma

antigens:FCGR3A:CD3

dimers		ComplexR-HSA-9664263 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:SYKComplexR-HSA-9664272 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:p-6Y-SYKComplexR-HSA-9664265 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimersComplexR-HSA-9664282 (Reactome)
IgG:Lma amastigote surfaceComplexR-HSA-9664283 (Reactome)
IgG:Lma antigensComplexR-HSA-9666422 (Reactome)
IgGComplexR-HSA-182629 (Reactome) In view of the highly variable nature of antibody proteins, this biological object is an approximate and fragmented representation of an IgM/IgD antibody, given the limitations of Ig chain enumeration in UniProt. A single mRNA transcript is alternatively spliced to give either IgM or IgD. Thus unactivated B cells contain both classes of antibody.
IgH heavy chain V-III region VH26 precursor ProteinP01764 (Uniprot-TrEMBL)
LPG1G2 ProteinQ4QD44 (Uniprot-TrEMBL)
LPG1G2ProteinQ4QD44 (Uniprot-TrEMBL)
LYN ProteinP07948 (Uniprot-TrEMBL)
Lma amastigote surfaceR-LMA-9664274 (Reactome) This entity is intended to represent any molecule that might be at the outer cell surface of a Leishmania amastigote parasite.
Lma amastigote surface R-LMA-9664274 (Reactome) This entity is intended to represent any molecule that might be at the outer cell surface of a Leishmania amastigote parasite.
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)
NCK1 ProteinP16333 (Uniprot-TrEMBL)
NCKAP1 ProteinQ9Y2A7 (Uniprot-TrEMBL)
NCKAP1L ProteinP55160 (Uniprot-TrEMBL)
NCKIPSD ProteinQ9NZQ3 (Uniprot-TrEMBL)
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)P2:WASP/N-WASPComplexR-HSA-9667225 (Reactome)
PI(4,5)P2MetaboliteCHEBI:18348 (ChEBI)
PIP3:VAV1,2,3ComplexR-HSA-5340329 (Reactome)
PTK2 ProteinQ05397 (Uniprot-TrEMBL)
PiMetaboliteCHEBI:18367 (ChEBI)
RAC1 ProteinP63000 (Uniprot-TrEMBL)
RAC1:GDPComplexR-HSA-5674631 (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)
p-4S-ABI2 ProteinQ9NYB9 (Uniprot-TrEMBL)
p-5S-ABI1 ProteinQ8IZP0 (Uniprot-TrEMBL)
p-6Y-CD247 ProteinP20963-1 (Uniprot-TrEMBL)
p-6Y-SYK ProteinP43405 (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-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-Y291-WAS ProteinP42768 (Uniprot-TrEMBL)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
ABL1mim-catalysisR-HSA-2130194 (Reactome)
ADPArrowR-HSA-2029469 (Reactome)
ADPArrowR-HSA-2130194 (Reactome)
ADPArrowR-HSA-2197698 (Reactome)
ADPArrowR-HSA-9664261 (Reactome)
ADPArrowR-HSA-9664275 (Reactome)
ADPArrowR-HSA-9666425 (Reactome)
ADPArrowR-HSA-9666458 (Reactome)
ARP2/3 complex (ATP bound)R-HSA-442592 (Reactome)
ATPR-HSA-1861595 (Reactome)
ATPR-HSA-2029469 (Reactome)
ATPR-HSA-2130194 (Reactome)
ATPR-HSA-2197698 (Reactome)
ATPR-HSA-9664261 (Reactome)
ATPR-HSA-9664275 (Reactome)
ATPR-HSA-9666425 (Reactome)
ATPR-HSA-9666458 (Reactome)
Actin filament bound Myosin-XArrowR-HSA-1861595 (Reactome)
BAIAP2R-HSA-2029465 (Reactome)
CDC42:GDPR-HSA-2029445 (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-WASPArrowR-HSA-9670155 (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)
CDC42:GTPR-HSA-9670155 (Reactome)
CRK:DOCK180:ELMO1,ELMO2R-HSA-9666426 (Reactome)
F-actinR-HSA-2029466 (Reactome)
FCGRIIIA:CD3G/CD3Z dimersR-HSA-9664406 (Reactome)
G-actinR-HSA-2029473 (Reactome)
G-actinR-HSA-442592 (Reactome)
GDPArrowR-HSA-2029445 (Reactome)
GDPArrowR-HSA-9666428 (Reactome)
GDPArrowR-HSA-9666430 (Reactome)
GTPR-HSA-2029445 (Reactome)
GTPR-HSA-9666428 (Reactome)
GTPR-HSA-9666430 (Reactome)
IgG:LPG1G2ArrowR-HSA-9664397 (Reactome)
IgG:Leishmania surface:FCGR3AArrowR-HSA-9666458 (Reactome)
IgG:Leishmania

surface:FCGR3Ap-CD3

dimers:p-6Y-SYK:VAV1,2,3:PI(3,4,5)P3		ArrowR-HSA-9666435 (Reactome)
IgG:Leishmania

surface:FCGR3Ap-CD3

dimers:p-6Y-SYK:VAV1,2,3:PI(3,4,5)P3		R-HSA-9666425 (Reactome)
IgG:Leishmania surface:p-FCGR3A:p-6Y-SYK:CRKII:DOCK180:ELMOArrowR-HSA-9666426 (Reactome)
IgG:Leishmania surface:p-FCGR3A:p-6Y-SYK:CRKII:DOCK180:ELMOmim-catalysisR-HSA-9666428 (Reactome)
IgG:Leishmania surface:p-FCGR3A:p-6Y-SYK:p-VAV1,2,3:PI(3,4,5)P3ArrowR-HSA-9666425 (Reactome)
IgG:Leishmania surface:p-FCGR3A:p-6Y-SYK:p-VAV1,2,3:PI(3,4,5)P3mim-catalysisR-HSA-9666430 (Reactome)
IgG:Lma

antigens:FCGR3A:CD3

dimers		ArrowR-HSA-9664406 (Reactome)
IgG:Lma

antigens:FCGR3A:CD3

dimers		R-HSA-9664275 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:SYKArrowR-HSA-9664273 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:SYKR-HSA-9664261 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:p-6Y-SYKArrowR-HSA-9664261 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:p-6Y-SYKR-HSA-9666426 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:p-6Y-SYKR-HSA-9666435 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimers:p-6Y-SYKmim-catalysisR-HSA-9666425 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimersArrowR-HSA-9664275 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimersR-HSA-9664273 (Reactome)
IgG:Lma antigens:FCGR3A:p-CD3 dimersR-HSA-9666458 (Reactome)
IgG:Lma amastigote surfaceArrowR-HSA-9666433 (Reactome)
IgG:Lma antigensR-HSA-9664406 (Reactome)
IgGR-HSA-9664397 (Reactome)
IgGR-HSA-9666433 (Reactome)
LPG1G2R-HSA-9664397 (Reactome)
Lma amastigote surfaceR-HSA-9666433 (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-9666458 (Reactome)
Mother

filament:branching

complex		ArrowR-HSA-2029466 (Reactome)
Mother

filament:branching

complex		R-HSA-2197690 (Reactome)
Myosin-Actin filamentsArrowR-HSA-9666458 (Reactome)
Myosin-X dimerR-HSA-1861595 (Reactome)
Myosin-X dimermim-catalysisR-HSA-1861595 (Reactome)
MyosinR-HSA-9666458 (Reactome)
PI(3,4)P2R-HSA-1861595 (Reactome)
PI(3,4,5)P3R-HSA-2029465 (Reactome)
PI(3,4,5)P3R-HSA-434637 (Reactome)
PI(4,5)P2:WASP/N-WASPArrowR-HSA-9670156 (Reactome)
PI(4,5)P2:WASP/N-WASPR-HSA-9670155 (Reactome)
PI(4,5)P2R-HSA-442586 (Reactome)
PI(4,5)P2R-HSA-9670156 (Reactome)
PIP3:VAV1,2,3ArrowR-HSA-434637 (Reactome)
PIP3:VAV1,2,3R-HSA-9666435 (Reactome)
PiArrowR-HSA-1861595 (Reactome)
PiArrowR-HSA-9666458 (Reactome)
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-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-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-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-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-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-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-434637 (Reactome) Vav interacts directly with PIP2 and PIP3, with a fivefold selectivity for PIP3 over PIP2. PIP3 gives a twofold stimulation of Vav1 GEF activity while PIP2 leads to 90% inhibition. Binding probably occurs through the PH domain, known to bind phosphoinositides.
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).
R-HSA-9664261 (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-9664273 (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-9664275 (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-9664397 (Reactome) The internalization of Leishmania amastigotes by macrophages is thought to be mediated mainly through opsonization with immunoglobulins (Igs) which bind FcγRs, stimulating the uptake (Morehead et al 2002 & Padigel et al. 2005). Glycoinositol phospholipids (GIPLs) are the most abundant glycolipids on the surface of the amastigote form of Leishmania parasites and Buxbaum and colleagues showed that IgG1 in mice, binds the GIPL molecules on the amastigote stage of L. mexicana to subsequently induced the phagocytosis through FcγRs (Buxbaum 2013).
R-HSA-9664406 (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-9666425 (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-9666426 (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-9666428 (Reactome) RAC1 is activated from inactive GDP-bound state to active GTP-bound form by the GEF activity of DOCK180:ELMO complex.
R-HSA-9666430 (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-9666433 (Reactome) The internalization of Leishmania amastigotes by macrophages is thought to be mediated mainly through opsonization with immunoglobulins (Igs) which bind Fc gamma receptors (FCGRs), stimulating their uptake (Morehead et al 2002 & Padigel et al. 2005). Glycoinositol phospholipids (GIPLs) are the most abundant glycolipids on the surface of the amastigote form of Leishmania parasites and Buxbaum and colleagues showed that IgG1 in mice binds GIPL molecules on the amastigote stage of L. mexicana to subsequently induce phagocytosis through FCGRs (Buxbaum 2013).
R-HSA-9666435 (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-9666458 (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-9670155 (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-9670156 (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).
RAC1:GDPR-HSA-9666428 (Reactome)
RAC1:GDPR-HSA-9666430 (Reactome)
RAC1:GTPArrowR-HSA-9666428 (Reactome)
RAC1:GTPArrowR-HSA-9666430 (Reactome)
RAC1:GTPR-HSA-2029465 (Reactome)
SH3 domain proteinsR-HSA-2197691 (Reactome)
SYKR-HSA-9664273 (Reactome)
Src family kinases (SFKs)mim-catalysisR-HSA-9664261 (Reactome)
Src family kinases (SFKs)mim-catalysisR-HSA-9664275 (Reactome)
Src-kinasesmim-catalysisR-HSA-2197698 (Reactome)
Unknown GEFmim-catalysisR-HSA-2029445 (Reactome)
VAV1,2,3R-HSA-434637 (Reactome)
WASP/N-WASPR-HSA-442586 (Reactome)
WASP/N-WASPR-HSA-9670156 (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)
p-T,Y MAPK dimersmim-catalysisR-HSA-2029469 (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)
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