FCGR3A-mediated phagocytosis (Homo sapiens)

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47, 623, 6010, 33, 574, 16, 23, 36, 48...1226, 42, 535542435932, 4534, 372, 9, 14, 49, 50, 6113, 21, 24, 35, 40...584, 5418, 4810, 27, 4452, 5856, 645, 72, 9, 14, 49, 50, 6131, 551, 8, 15, 17, 22...11, 17, 25, 29, 3019, 20, 39, 51436, 46LeishmaniaHostcytosolphagocytic cupcytosolIg heavy chain V-III region WEA IGKV1-12 IGLV7-43(1-?) IGLV4-60(1-?) RAC1:GTPIGKV3D-20 IGLV4-69(1-?) IGLV1-40(1-?) IGLV2-33(1-?) IGLV3-12(1-?) Ig lambda chain V-I region VOR Ig heavy chain V-III region KOL LYN IgH heavy chain V-III region VH26 precursor Ig heavy chain V-II region OU Ig kappa chain V-II region FR IGHV7-81(1-?) p-Y150,S343,T346-WASF2 Ig kappa chain V region EV15 Ig lambda chain V-II region MGC GRB2-1 Ig lambda chain V-IV region Kern IGLC6 IGKV2D-30 IGLV1-36(1-?) Ig kappa chain V-I region Daudi Ig heavy chain V-II region ARH-77 p-Y173-VAV3 Ig lambda chain V-II region TOG Ig heavy chain V-III region BUT IGHG2 IGLV7-43(1-?) Ig lambda chain V-IV region Kern Ig heavy chain V-II region NEWM IGKV2D-30 GRB2-1 IGLV(23-?) Ig lambda chain V-III region SH Ig kappa chain V-II region RPMI 6410 IGKV1-12 IGLC7 IGKV1-5(23-?) IGLV1-44(1-?) Ig heavy chain V-III region DOB ADPARPC1B Ig kappa chain V-I region BAN Ig kappa chain V-I region AU FCGR3A Ig heavy chain V-II region MCE Ig kappa chain V-III region VG Ig lambda chain V-I region NEW Ig lambda chain V-I region NEWM WRC:IRSp53/58:RAC1:GTP:PIP3NCKAP1L CDC42 Ig lambda chain V-III region LOI IGLV2-18(1-?) WASF3 IGHG2 Ig heavy chain V-II region NEWM IGLV7-46(1-?) NCKIPSD Ig heavy chain V-III region TRO Ig lambda chain V-I region VOR Ig heavy chain V-III region BRO IGLV3-16(1-?) Ig heavy chain V-II region OU IGKV2D-30 IGLV3-25(1-?) FGR IgG:Lmaantigens:FCGR3A:p-CD3 dimersIg kappa chain V-II region RPMI 6410 Ig lambda chain V-I region NEWM IGHV7-81(1-?) IGLV5-45(1-?) PI(4,5)P2 IGHV(1-?) ATPIGKV3D-20 IGLV11-55(1-?) IGLC1 IGLV3-12(1-?) Ig lambda chain V-IV region Bau IGLV8-61(1-?) NCK1 IGHG3 IGLC2 ADPIGLC2 IGKV1-12 IGKV4-1(21-?) IGLV2-18(1-?) IGHV1-2 IGLC1 Ig heavy chain V-III region DOB p-Y151,S,T-WASF1 IGHG2 p-Y151-WASF3 Ig kappa chain V-I region AG Ig lambda chain V-II region MGC Ig heavy chain V-II region NEWM Ig kappa chain V-I region HK101 Ig kappa chain V-II region FR Ig lambda chain V-IV region Bau IGHV(1-?) Ig kappa chain V-I region HK101 ADP Ig heavy chain V-III region TRO IgH heavy chain V-III region VH26 precursor Ig kappa chain V-I region BAN Ig heavy chain V-I region EU Ig heavy chain V-II region NEWM ARPC4 IGHG3 ACTG1 Ig heavy chain V-I region EU Ig kappa chain V-I region Gal IGLV10-54(1-?) Ig kappa chain V-I region AG ATP Ig kappa chain V-II region FR Motherfilament:branchingcomplex:daughterfilamentIg kappa chain V-III region B6 Ig kappa chain V-I region Daudi Ig lambda chain V-I region NEWM IGHG3 IgH heavy chain V-III region VH26 precursor Ig kappa chain V-I region AU IGLC6 IgG:Leishmaniasurface:FCGR3AIg lambda chain V-IV region Kern IGLV(23-?) Ig heavy chain V-III region CAM IGKV1-12 IGLV2-11(1-?) Ig lambda chain V-VI region AR Ig heavy chain V-II region NEWM BRK1 Ig lambda chain V-VI region AR Ig heavy chain V-II region OU Ig heavy chain V-I region HG3 IGKV4-1(21-?) Ig kappa chain V-III region POM Ig lambda chain V-IV region Bau IGLV3-16(1-?) Ig heavy chain V-III region JON IGLV3-22(1-?) Ig kappa chain V-I region BAN RAC1 IGKV2-28 IGKV4-1(21-?) IGLV11-55(1-?) Ig kappa chain V-I region AU IGLV1-40(1-?) Ig heavy chain V-II region WAH p-Y151,S,T-WASF1 IGLV3-25(1-?) Ig lambda chain V-IV region Kern IGLV3-12(1-?) ACTR3 Ig kappa chain V-III region B6 Ig lambda chain V-II region NEI p-T,Y MAPK dimersFCGR3A Ig lambda chain V region 4A WIPF2 Ig kappa chain V-I region HK101 Ig kappa chain V-II region RPMI 6410 Ig heavy chain V-II region WAH Ig lambda chain V-III region SH Ig kappa chain V-I region DEE Ig heavy chain V-III region JON IGLV7-46(1-?) IGHV1-2 Ig kappa chain V-II region RPMI 6410 IGLV8-61(1-?) IGLV3-25(1-?) IGHG3 IGKV4-1(21-?) Lma amastigote surface IGKV2-28 IGLV10-54(1-?) IGLV11-55(1-?) IGLV2-33(1-?) ABI2 IGKV4-1(21-?) GTP p-Y291-WAS Ig kappa chain V-I region Wes ATP IGLC6 IGKC ABI2 Ig kappa chain V-I region Daudi FCGR3A ADPATP IGLC3 Ig kappa chain V-III region POM VAV2 IGLV11-55(1-?) IGLV1-36(1-?) Ig heavy chain V-III region BRO Ig heavy chain V-III region KOL ACTB(1-375) Ig kappa chain V-I region AU BAIAP2 Ig heavy chain V-I region HG3 Ig lambda chain V-II region TOG NCKIPSD Ig heavy chain V-I region HG3 Ig heavy chain V-III region WEA IGHV7-81(1-?) IGKV2D-30 CDC42 ATP IGHV(1-?) ACTG1 GDP IGHV(1-?) p-Y151-WASF1 IGLV3-27(1-?) p-6Y-SYK IGHV(1-?) Ig kappa chain V-II region Cum IGKV2-28 Ig heavy chain V-II region NEWM IGLV2-33(1-?) Ig lambda chain V-IV region Kern RAC1:GDPIGKV1-5(23-?) IGLV1-36(1-?) IGLV11-55(1-?) IGLC1 IGKV1-12 VAV1 p-Y160,Y171-CD3G PI(4,5)P2IGLV7-43(1-?) p-Y151-WASF1 IGHG1 IGLV3-16(1-?) IGKV3D-20 Ig kappa chain V-I region Daudi IGKV4-1(21-?) IGKV4-1(21-?) Ig kappa chain V region EV15 Ig heavy chain V-III region CAM IGLV5-45(1-?) Ig kappa chain V-III region VG CDC42:GTP:WASP/N-WASPIGLC3 Ig heavy chain V-I region EU IGLV2-23(1-?) IGKV4-1(21-?) LPG1G2 IGLV10-54(1-?) Ig lambda chain V region 4A NCKAP1L IGKV1-5(23-?) Ig lambda chain V-I region NEW IGKV2-28 IGHG3 Ig lambda chain V-I region HA p-Y172-VAV2 IGLV10-54(1-?) Ig kappa chain V-I region Daudi ABI1 IGKV1-5(23-?) Ig heavy chain V-III region BUT Ig lambda chain V-I region NEW LPG1G2 IGLV4-69(1-?) ABL1IGKV3D-20 IGLC2 Ig kappa chain V-I region Daudi Ig kappa chain V-I region DEE IGHV7-81(1-?) IGLV8-61(1-?) Ig kappa chain V-II region Cum IGLV5-37(1-?) RAC1 Ig heavy chain V-III region BUT IGHV7-81(1-?) PI(3,4,5)P3 Ig heavy chain V-II region ARH-77 p-6Y-SYK ADPIg kappa chain V-III region B6 ELMO1 Ig lambda chain V-III region LOI IGLV2-11(1-?) IGHG3 GTP GTPIg heavy chain V-III region TRO Ig lambda chain V-II region TOG CDC42 IGHG4 IGKC ARPC3 Ig heavy chain V-II region ARH-77 p-Y256-WASL IGLV3-12(1-?) IGLV3-22(1-?) IGLV4-3(1-?) Ig lambda chain V-II region NEI HCK IGLV7-46(1-?) Ig lambda chain V-II region MGC Ig heavy chain V-II region ARH-77 Ig lambda chain V-I region NEWM IGLV4-69(1-?) Ig kappa chain V-I region AU IGLV1-36(1-?) IGHG1 IGLV4-3(1-?) IGKV1-12 IGKV3D-20 IgG:Lma amastigotesurfaceIg heavy chain V-II region WAH p-Y150,S343,T346-WASF2 IGLV7-46(1-?) SYK MYO1C Ig heavy chain V-III region DOB Ig lambda chain V-III region SH CYFIP2 Ig heavy chain V-III region TRO Ig lambda chain V-III region SH IGLV4-60(1-?) IGLC3 IGLV2-23(1-?) GTPIGLV3-22(1-?) Ig kappa chain V-I region Wes IGLV5-37(1-?) Ig kappa chain V region EV15 p-Y,S,T-WRC:IRSp53/58:RAC1:GTP:PIP3WIPF3 Ig kappa chain V-II region FR LPG1G2 Ig lambda chain V-IV region Bau Ig lambda chain V-I region VOR CYFIP2 ADPIg heavy chain V-II region WAH IGHV(1-?) IGHV7-81(1-?) IGLV8-61(1-?) Ig heavy chain V-II region MCE Ig heavy chain V-III region TRO Ig lambda chain V-I region NEW ACTR3 IGLV2-23(1-?) Ig lambda chain V-II region NEI IGKC IGLV4-60(1-?) p-Y256-WASL IGHV(1-?) Ig lambda chain V-II region BOH IgH heavy chain V-III region VH26 precursor IGLV5-45(1-?) ATPIGLV3-27(1-?) IGLV5-45(1-?) PI(3,4,5)P3 IGHG2 ACTB(1-375) Ig lambda chain V-II region TOG Ig lambda chain V-III region LOI Ig lambda chain V-IV region Hil GTPLPG1G2 IgG:LPG1G2Ig heavy chain V-III region WEA IGLC7 Ig kappa chain V-I region AU Ig lambda chain V-VI region AR Ig lambda chain V region 4A Ig lambda chain V-I region NEWM Ig lambda chain V-I region NEWM IGLC6 IgG:Lma antigensIGLV11-55(1-?) Ig kappa chain V-I region AG p-Y291-WAS Ig lambda chain V-III region LOI WIPF3 IGKV1-5(23-?) IGHV7-81(1-?) Ig kappa chain V-III region B6 Ig lambda chain V-IV region Hil LPG1G2 Ig heavy chain V-I region HG3 IGLV1-36(1-?) FCGR3A Ig kappa chain V-III region POM Ig heavy chain V-III region BRO Ig lambda chain V-I region NEWM Ig lambda chain V-IV region Hil IGLC6 WAS IGLV2-18(1-?) Ig kappa chain V-III region B6 MYO1C IGKVA18(21-?) Ig kappa chain V-III region POM ACTB(1-375) Ig lambda chain V-II region TOG IGHG4 FCGR3A Ig heavy chain V-II region MCE Ig heavy chain V-III region KOL p-Y151,S,T-WASF1 IGLV3-25(1-?) Ig lambda chain V-I region HA WIPF2 IGHG1 ACTR3 Ig lambda chain V region 4A IGLV8-61(1-?) F-actin Ig heavy chain V-III region CAM IGKV2D-30 Ig heavy chain V-II region ARH-77 Ig lambda chain V-II region BOH Ig lambda chain V region 4A Ig lambda chain V region 4A IgH heavy chain V-III region VH26 precursor Ig heavy chain V-II region ARH-77 ATPIg kappa chain V-II region FR IGLV3-16(1-?) IGLC2 Ig kappa chain V-I region BAN Ig lambda chain V-III region LOI Ig kappa chain V-I region Daudi Ig lambda chain V-IV region Hil Ig lambda chain V-II region BOH Ig lambda chain V-IV region Hil IGKVA18(21-?) IGLV3-12(1-?) CYFIP2 IGHV7-81(1-?) IGLC7 ACTR2 IGHG4 IgG:Leishmaniasurface:FCGR3Ap-CD3dimers:p-6Y-SYK:VAV1,2,3:PI(3,4,5)P3Ig lambda chain V-II region BOH IGLV7-43(1-?) Ig heavy chain V-II region OU Ig kappa chain V-I region AG Ig lambda chain V-III region LOI PI(3,4,5)P3 Ig lambda chain V-VI region AR Ig kappa chain V-I region Gal p-4S-ABI2 VAV3 IGLV2-33(1-?) Ig lambda chain V-II region MGC CD3G PI(3,4,5)P3Ig heavy chain V-II region OU IGHV1-2 IGLV2-11(1-?) Ig lambda chain V-II region NEI Ig lambda chain V region 4A IGKC YES1 Ig lambda chain V-II region NEI IGKVA18(21-?) IGHV1-2 Ig kappa chain V-I region AG IGKV2D-30 IGKV2D-30 IGLV3-16(1-?) Ig kappa chain V region EV15 CDC42 IGLV3-27(1-?) PI(3,4,5)P3 Ig kappa chain V-I region HK101 CYFIP2 IGHG3 Ig lambda chain V-I region HA Ig heavy chain V-III region JON Ig kappa chain V-III region VG Ig kappa chain V-III region B6 GTP IGHG2 NCKAP1 PI(3,4,5)P3 p-4S-ABI2 WAS Ig heavy chain V-III region DOB Ig kappa chain V-I region HK101 Ig heavy chain V-II region ARH-77 Ig lambda chain V region 4A Ig heavy chain V-III region JON Ig heavy chain V-I region EU IGLV3-12(1-?) Ig kappa chain V-I region BAN IGLC2 IGHV1-2 IGLV2-33(1-?) Ig kappa chain V-I region Daudi Ig lambda chain V-IV region Kern Ig kappa chain V-I region Gal Ig heavy chain V-II region OU Ig heavy chain V-II region OU ARPC5 IGLV4-69(1-?) Ig kappa chain V-II region FR ARPC5 GTP IGKV3D-20 F-actinIg kappa chain V-I region AG Ig heavy chain V-I region HG3 CYFIP2 Ig kappa chain V-I region Wes IGHG4 p-6Y-CD247 IGHG4 Ig heavy chain V-II region ARH-77 IGLV10-54(1-?) IGHV1-2 WIPF1 Ig kappa chain V-I region BAN CYFIP1 Ig lambda chain V-II region MGC IGKV2D-30 IGLV3-27(1-?) Ig heavy chain V-III region WEA Lma amastigote surface IGLV4-69(1-?) ARPC5 Ig heavy chain V-III region CAM ATP Ig heavy chain V-III region BRO Ig lambda chain V-III region LOI Ig heavy chain V-III region TRO Ig kappa chain V-III region B6 Ig kappa chain V-I region HK101 Ig lambda chain V region 4A Ig kappa chain V-III region B6 IGLV1-36(1-?) ARPC5 IGHV1-2 IGLV7-43(1-?) Ig heavy chain V-II region NEWM IGLV8-61(1-?) ARPC2 NCK1 Ig lambda chain V-IV region Kern IGKV4-1(21-?) ACTR2 Ig kappa chain V-I region BAN WIPF2 Ig heavy chain V-III region DOB IGLV3-25(1-?) ELMO2 Ig kappa chain V-I region Wes Ig kappa chain V-I region AU IGKVA18(21-?) Ig lambda chain V-IV region Hil Ig heavy chain V-III region KOL p-Y174-VAV1 IGKV2D-30 IGHG2 Ig kappa chain V-II region FR Ig kappa chain V-II region FR IGLV2-23(1-?) IGKV2-28 WIPF2 IGHV(1-?) Ig kappa chain V-III region VG Ig lambda chain V-VI region AR Ig lambda chain V-II region NEI Ig kappa chain V-I region HK101 Ig kappa chain V-I region Wes IGLV7-43(1-?) PI(4,5)P2 Actin filament boundMyosin-XADPIGLV2-23(1-?) Ig heavy chain V-III region TRO WIPF1 IGLV1-40(1-?) LPG1G2Ig lambda chain V-IV region Bau Motherfilament:ARP2/3:actin:ADPIg lambda chain V-I region HA PI(4,5)P2 MyosinIGLV7-46(1-?) ARPC4 WIP family proteinsIGHG1 WIPF3 Ig kappa chain V-I region AG Ig lambda chain V-IV region Kern IGLV11-55(1-?) MYH2 Unknown GEFIGLV10-54(1-?) GDPIg lambda chain V-II region MGC IGLV5-37(1-?) Ig lambda chain V-VI region AR IGLV(23-?) Ig heavy chain V-II region NEWM Ig heavy chain V-I region EU DOCK1 IGKVA18(21-?) Ig lambda chain V-I region HA IGKVA18(21-?) IGLV8-61(1-?) ARPC1A IGLV3-25(1-?) Ig kappa chain V-III region VG Ig heavy chain V-I region EU IGLV3-25(1-?) RAC1 Ig lambda chain V-II region TOG Ig heavy chain V-III region WEA IGLV(23-?) BAIAP2 GTP Ig kappa chain V-I region AU IGLV3-22(1-?) IGLC2 IGLC1 Ig lambda chain V-I region HA IGLC7 Ig heavy chain V-II region MCE IGHG4 Lma amastigote surface Ig kappa chain V-I region AU IGKV4-1(21-?) p-Y150-WASF2 GTP Ig lambda chain V-III region SH IGLC7 ARP2/3 complex (ATPbound)CYFIP2 F-actin Ig heavy chain V-III region CAM Ig kappa chain V region EV15 Ig kappa chain V-I region Daudi Ig heavy chain V-II region ARH-77 IGKV1-12 Ig kappa chain V-II region Cum Ig lambda chain V-IV region Hil p-Y160,Y171-CD3G RAC1:GDPIg heavy chain V-II region OU ADPIGLC3 Ig heavy chain V-III region TRO CDC42:GTPARPC1A Lma amastigote surface WAS LPG1G2 Ig heavy chain V-III region KOL IgG:Lmaantigens:FCGR3A:p-CD3 dimers:p-6Y-SYKIg heavy chain V-III region BUT IGKVA18(21-?) Ig heavy chain V-III region KOL ABI2 IGLV3-16(1-?) Ig heavy chain V-III region JON Ig heavy chain V-II region WAH IGKV1-5(23-?) IGLV5-37(1-?) Myosin-ActinfilamentsIGKV3D-20 IgH heavy chain V-III region VH26 precursor ABI1 IGLC3 IGLC6 p-Y151-WASF3 IGLV2-11(1-?) IGLV1-40(1-?) NCKAP1 p-Y160,Y171-CD3G ACTG1 IGLV1-36(1-?) PI(3,4,5)P3 IGLV4-60(1-?) ARPC4 Ig heavy chain V-III region JON Ig kappa chain V-I region Wes IGLV3-27(1-?) Ig kappa chain V-II region FR IGLC7 Ig kappa chain V-I region DEE IGLV1-44(1-?) IGLV3-27(1-?) IGLV5-45(1-?) SRC-1 ACTR2 F-actin Ig lambda chain V-I region HA ACTR2 p-5S-ABI1 Ig lambda chain V region 4A Ig heavy chain V-III region TRO IGLV11-55(1-?) WAVE2, WASP,N-WASP:ARP2/3complex:G-actinIg lambda chain V-IV region Bau Ig kappa chain V-II region Cum ARPC5 p-Y151,S,T-WASF3 WIPF3 BRK1 Ig kappa chain V-I region AG Ig lambda chain V-I region VOR IGLV3-16(1-?) PiIg kappa chain V-III region B6 Ig heavy chain V-II region MCE Lma amastigote surface IgG:Lmaantigens:FCGR3A:p-CD3 dimers:SYKp-Y160,Y171-CD3G Ig kappa chain V-III region POM IGLV4-69(1-?) IGLV2-33(1-?) IGLV(23-?) FYN Ig heavy chain V-III region JON ATPIg lambda chain V-III region LOI p-4S-ABI2 Ig heavy chain V-II region ARH-77 Ig heavy chain V-III region BRO Ig kappa chain V-I region Wes IGLV10-54(1-?) WASF1 Ig lambda chain V-II region TOG NCKAP1L Ig lambda chain V-III region SH IGLV4-60(1-?) IGLV7-46(1-?) IGLV2-33(1-?) Ig kappa chain V-I region AG IGLV2-33(1-?) PI(3,4,5)P3 Ig kappa chain V-I region BAN IGLV4-69(1-?) IGLV3-12(1-?) ACTR3 IGHG2 p-Y151,S,T-WASF3 IGLV1-40(1-?) IGLV7-46(1-?) IGHG2 ACTR2 IGLV2-18(1-?) BAIAP2 CRK:DOCK180:ELMO1,ELMO2Ig heavy chain V-III region BRO Ig lambda chain V-VI region AR Ig kappa chain V-II region RPMI 6410 Ig kappa chain V-I region Gal IGHV(1-?) NCK1 ARPC3 IGKV2-28 IGLV3-12(1-?) IGKVA18(21-?) IGLV7-43(1-?) Ig lambda chain V-IV region Kern IGHG3 Ig lambda chain V region 4A IGLV5-45(1-?) IgG:Leishmaniasurface:p-FCGR3A:p-6Y-SYK:p-VAV1,2,3:PI(3,4,5)P3IGKV2-28 Ig heavy chain V-III region CAM IGHV7-81(1-?) IGLC7 Ig kappa chain V-I region AG ATP Ig lambda chain V-I region VOR Ig lambda chain V-II region MGC IGLC1 Ig kappa chain V-I region DEE Ig lambda chain V-II region TOG Ig lambda chain V-I region HA Ig kappa chain V-I region BAN IGLC3 Ig lambda chain V-II region TOG Ig heavy chain V-III region BRO IGHG3 Ig kappa chain V-I region Gal Ig kappa chain V-I region HK101 Ig lambda chain V-I region VOR Ig lambda chain V-II region BOH Ig heavy chain V-III region BUT IGLV2-18(1-?) Ig lambda chain V-IV region Bau LPG1G2 Ig kappa chain V-II region RPMI 6410 IGLV4-69(1-?) Ig kappa chain V-II region Cum ABI1 IGLV3-25(1-?) IGLV5-45(1-?) IGLV1-44(1-?) Ig lambda chain V-IV region Hil Ig lambda chain V-I region NEW NCKAP1L ARPC3 NCK1 CYFIP1 Ig kappa chain V-I region Gal Ig kappa chain V-II region FR Ig kappa chain V-III region POM Ig lambda chain V-I region NEWM p-Y160,Y171-CD3G IGLV8-61(1-?) IGLV4-3(1-?) FYN NCK1 Ig lambda chain V-III region SH IGLC6 IGHG4 WAVE RegulatoryComplexACTR2 IGLV11-55(1-?) IGLV5-37(1-?) BRK1 Ig kappa chain V-I region Gal GTP IGKV1-5(23-?) ARPC2 ARPC3 Ig heavy chain V-II region OU Ig kappa chain V region EV15 Ig lambda chain V-II region NEI IGLV1-44(1-?) VAV1 IGLV7-46(1-?) GTP IGLV4-60(1-?) Ig lambda chain V-I region VOR Ig kappa chain V-I region HK101 IGHG3 Ig lambda chain V-I region HA IGKV3D-20 NCKAP1 Ig lambda chain V-I region NEWM p-6Y-SYK Ig lambda chain V-II region NEI Ig kappa chain V-II region Cum ARPC3 IGLV1-36(1-?) IGLV2-23(1-?) CRK IGKV1-12 IGLV3-22(1-?) IGLC2 Ig heavy chain V-III region TRO CYFIP1 Ig heavy chain V-III region JON p-T185,Y187-MAPK1 CYFIP1 IGLV5-45(1-?) Ig kappa chain V region EV15 Ig lambda chain V-II region MGC IGHV7-81(1-?) ARPC2 MYH9 Ig kappa chain V-III region POM IGLV2-23(1-?) IGLV1-40(1-?) Ig kappa chain V-I region AU IGLC3 IGLV1-36(1-?) IGLC6 Ig heavy chain V-II region WAH Ig heavy chain V-II region OU p-Y160,Y171-CD3G IGLV1-36(1-?) Ig heavy chain V-III region BUT Ig heavy chain V-II region WAH Ig lambda chain V-I region NEW Ig kappa chain V-III region VG Ig heavy chain V-III region BRO Ig kappa chain V-I region AU IGLV3-27(1-?) IGLV2-18(1-?) MYH2 IGLV3-22(1-?) IGLV3-16(1-?) Ig heavy chain V-II region ARH-77 NCKIPSD IGLV3-16(1-?) ARPC1B IGLV1-40(1-?) IgH heavy chain V-III region VH26 precursor Ig kappa chain V-I region Wes Ig kappa chain V-II region RPMI 6410 ATPIGLV2-11(1-?) IGLC3 IGLC1 Ig lambda chain V-II region TOG NCKAP1 p-5S-ABI1 IgH heavy chain V-III region VH26 precursor Ig lambda chain V-IV region Kern ARPC4 IGKV1-5(23-?) Ig heavy chain V-I region HG3 Ig heavy chain V-III region KOL BAIAP2IGLV3-27(1-?) IGLV3-27(1-?) MYH9 VAV1,2,3IgGIg heavy chain V-II region WAH GRB2-1 IGLV1-40(1-?) Ig heavy chain V-III region BRO GDP FCGR3A PI(4,5)P2 Src family kinases(SFKs)RAC1 Ig heavy chain V-III region DOB IGKV2D-30 Ig lambda chain V-III region SH Ig kappa chain V-III region VG IGLC3 Ig kappa chain V-I region HK101 IGLV(23-?) LPG1G2 p-Y291-WAS ABI2 ADP Ig kappa chain V-II region Cum IGHV(1-?) IGLV4-60(1-?) IGLV3-22(1-?) IGLV2-23(1-?) Ig kappa chain V-I region Daudi RAC1 ATP Ig lambda chain V-II region NEI NCKAP1L PI(4,5)P2:WASP/N-WASPIg heavy chain V-III region KOL RAC1 IGKV1-5(23-?) Ig lambda chain V-I region NEW WASF2 CYFIP1 Ig heavy chain V-III region KOL Ig heavy chain V-II region MCE Ig heavy chain V-II region MCE IGLC6 Ig lambda chain V-IV region Hil Ig lambda chain V-I region NEWM Ig kappa chain V-III region B6 G-actinIGLV4-69(1-?) Ig lambda chain V-I region VOR p-Y151,S,T-WASF3 IGLV5-37(1-?) IGHG2 ACTB(1-375) IGLC6 MYO10 IGLV(23-?) Ig heavy chain V-III region DOB Ig kappa chain V-I region HK101 IGHV1-2 IGLV3-22(1-?) Ig kappa chain V-III region VG VAV1 IGKC IGKV2-28 F-actin IGLV3-25(1-?) IGLV3-16(1-?) Ig heavy chain V-III region BUT CDC42 IGLV1-40(1-?) IGKV4-1(21-?) IGLV1-44(1-?) Ig kappa chain V-I region Gal ARPC1A IGLV3-27(1-?) ARPC1B NCK1 Ig heavy chain V-I region HG3 HCK Lma amastigote surface IGLV10-54(1-?) ARPC3 BAIAP2 IGKV2D-30 IGLV3-12(1-?) Ig kappa chain V-I region Wes Ig lambda chain V-II region BOH Ig heavy chain V-II region NEWM WIPF2 Ig lambda chain V-I region NEWM Ig heavy chain V-I region EU Ig heavy chain V-II region WAH p-Y150-WASF2 IGLV2-18(1-?) MYO5A WIPF3 IGLV5-37(1-?) IGLV4-60(1-?) MYO5A Ig heavy chain V-I region HG3 p-Y151,S,T-WASF1 Ig lambda chain V-I region VOR IGHG1 ATPIg lambda chain V-II region MGC IGHV7-81(1-?) Ig heavy chain V-III region BUT PI(3,4,5)P3 p-6Y-CD247 ARPC4 Ig kappa chain V-II region Cum Ig lambda chain V-VI region AR ARPC5 IGLV3-22(1-?) WASP/N-WASPIGLV2-11(1-?) ARPC1B IGHV1-2 Ig lambda chain V-IV region Kern IGLC2 Ig heavy chain V-III region BUT FCGR3A Lma amastigote surface PTK2 Ig heavy chain V-I region EU p-Y151-WASF1 IGHG1 Ig lambda chain V-I region NEW Ig heavy chain V-I region HG3 ELMO2 p-Y256-WASL WAS ARPC2 Ig lambda chain V-IV region Bau Ig heavy chain V-II region NEWM IGLV10-54(1-?) Ig lambda chain V region 4A Ig lambda chain V-VI region AR IGKV1-12 p-6Y-CD247 IGLV2-11(1-?) IGLV11-55(1-?) IGLV1-44(1-?) Ig heavy chain V-II region WAH BRK1 IGHG1 IGKV4-1(21-?) IGLV3-27(1-?) IGHG1 Ig lambda chain V-II region BOH Lma amastigote surface RAC1 GRB2-1 ACTR3 CDC42 IGLV7-46(1-?) Ig lambda chain V-IV region Bau IGKV1-5(23-?) Lma amastigotesurfaceLPG1G2 IGKV2-28 Ig kappa chain V-I region AG IGLV2-11(1-?) IGHG4 IgH heavy chain V-III region VH26 precursor Ig kappa chain V-III region VG ATP Ig heavy chain V-III region WEA IGHG3 IGLV2-33(1-?) IGLV2-18(1-?) Ig heavy chain V-II region ARH-77 Ig kappa chain V-III region B6 Ig lambda chain V-II region BOH Ig lambda chain V-I region VOR IGLV7-46(1-?) IGLC7 Ig lambda chain V-III region LOI Ig kappa chain V-II region RPMI 6410 Ig heavy chain V-II region NEWM PI(4,5)P2 ARPC3 Ig kappa chain V-II region FR IGKC WASF3 IGKV2-28 ARPC5 SH3 domain proteinsIg lambda chain V-II region MGC IGKV2-28 Ig lambda chain V-I region HA IGLV3-12(1-?) IGKV2D-30 IGLV8-61(1-?) IGKV3D-20 IGLV1-44(1-?) Ig lambda chain V-IV region Bau Ig heavy chain V-I region EU IGHV1-2 ACTG1 IGHV1-2 Ig heavy chain V-III region CAM Ig heavy chain V-III region BRO IGLV5-37(1-?) Ig kappa chain V-I region BAN Ig lambda chain V-VI region AR ADP Ig heavy chain V-II region OU Ig heavy chain V-III region KOL IGHG4 MYO10 IGLC6 Ig heavy chain V-III region CAM IGKC Ig kappa chain V-II region Cum Ig kappa chain V-II region RPMI 6410 PI(3,4)P2IGKVA18(21-?) Ig heavy chain V-I region EU LPG1G2 IGLV1-40(1-?) NCKAP1L IGHG2 Ig heavy chain V-III region CAM Ig lambda chain V-IV region Hil Ig heavy chain V-III region BRO p-Y151,S,T-WASF3 p-Y150,S343,T346-WASF2 Ig heavy chain V-III region DOB Ig heavy chain V-III region JON IGLV4-60(1-?) IGLV(23-?) p-5S-ABI1 Ig lambda chain V-I region NEW VAV2 IGHV(1-?) Ig heavy chain V-II region WAH Ig kappa chain V region EV15 GRB2-1 Ig kappa chain V-I region DEE Ig kappa chain V-I region AU GRB2-1 IGHV7-81(1-?) Ig heavy chain V-III region DOB CD247-1 RAC1 IGLC7 IGLV5-37(1-?) Lma amastigote surface IGHG4 IGLC7 IGLV2-18(1-?) IGLC2 MYO9B IGLV1-44(1-?) p-5S-ABI1 p-6Y-SYK Ig heavy chain V-III region TRO IGLC2 CDC42:GDPp-6Y-CD247 IGLV4-60(1-?) NCKIPSD Ig heavy chain V-II region WAH Ig kappa chain V-III region POM IGLV1-44(1-?) IGLV2-33(1-?) ARPC1A Ig lambda chain V-I region NEWM IGLV7-43(1-?) Ig lambda chain V-III region SH GDPIGLV5-45(1-?) NCKIPSD VAV2 ARPC2 IGLV11-55(1-?) IGLV1-36(1-?) IGLV4-3(1-?) FGR IGLV2-11(1-?) CDC42 IGKV2-28 IGLV4-3(1-?) IGLV4-3(1-?) Motherfilament:branchingcomplexIg heavy chain V-I region EU Lma amastigote surface IGLV2-23(1-?) IGLV3-12(1-?) VAV3 IGLV3-16(1-?) Ig lambda chain V-I region NEW IGLV(23-?) Ig lambda chain V-IV region Hil Ig lambda chain V-I region HA Ig kappa chain V-I region DEE Ig kappa chain V-III region POM IGLV4-3(1-?) IGKV3D-20 IGHG4 CYFIP1 IGLV4-3(1-?) Ig lambda chain V-II region MGC DOCK1 PI(3,4)P2 IGLV4-3(1-?) Ig heavy chain V-III region BUT IGLV7-43(1-?) CDC42:GTP:p-Y-WASP/p-Y-WASL:WIP:SH3 proteinsN-WASP ARPC1A WIPF2 Ig heavy chain V-I region HG3 WIPF3 Ig lambda chain V-I region HA PiIg lambda chain V-II region BOH IGLV2-11(1-?) Ig kappa chain V-II region RPMI 6410 YES1 p-Y150-WASF2 FCGRIIIA:CD3G/CD3ZdimersIg lambda chain V-II region NEI IGLV1-40(1-?) Ig kappa chain V-III region POM Ig lambda chain V-II region TOG IGKV3D-20 IGKV1-12 BTK RAC1 Ig lambda chain V-III region SH IGLV2-33(1-?) IGLC3 GDPIGLC1 WAVE2, WASP, N-WASPIg lambda chain V-II region TOG NCKAP1 ARPC1B IGLV1-40(1-?) Ig kappa chain V-I region BAN Src family kinases(SFKs)IGLV3-22(1-?) Ig heavy chain V-I region HG3 IGLV7-43(1-?) BAIAP2 BRK1 CD3G IGLV11-55(1-?) IGLV3-22(1-?) Ig kappa chain V-I region Wes ARPC1A ABI2 Ig kappa chain V-II region RPMI 6410 Ig lambda chain V-III region LOI IgH heavy chain V-III region VH26 precursor Ig heavy chain V-III region BUT IGLC1 Ig kappa chain V-I region Gal p-Y256-WASL ARPC2 Ig heavy chain V-III region BRO IGLV10-54(1-?) p-Y150-WASF2 ACTR3 Ig heavy chain V-III region KOL IGHG2 IGLV5-37(1-?) CD247-1 p-Y150,S343,T346-WASF2 Ig heavy chain V-III region WEA IGLV1-44(1-?) Ig lambda chain V-II region NEI IGLV8-61(1-?) Ig kappa chain V-I region Wes MYO9B IGLC2 IGLC1 IGKV1-5(23-?) IGLC1 Ig kappa chain V-II region FR ELMO1 Ig kappa chain V-I region DEE ACTB(1-375) p-Y151-WASF1 IGHG1 ATP Ig heavy chain V-III region JON Ig kappa chain V-I region DEE Ig kappa chain V region EV15 BRK1 Ig lambda chain V-III region LOI Ig heavy chain V-III region BUT Ig lambda chain V-II region NEI IGLV2-23(1-?) IGLV10-54(1-?) IGLV5-37(1-?) Src-kinasesIGHG1 Ig kappa chain V-I region DEE Ig kappa chain V region EV15 IGLV2-18(1-?) IGLV10-54(1-?) BAIAP2 IGLV2-18(1-?) Ig lambda chain V-III region SH WIPF1 Ig heavy chain V-II region MCE IGLV4-69(1-?) WIPF1 Myosin-X dimerARPC4 WASF1 ACTR3 p-Y291-WAS Ig lambda chain V-IV region Hil IGHG2 GTP IGLV8-61(1-?) IGLV1-44(1-?) Ig heavy chain V-III region WEA IGLV(23-?) LYN GTP CYFIP1 Ig lambda chain V-III region LOI ABI1 IgH heavy chain V-III region VH26 precursor NCKIPSD Ig heavy chain V-III region CAM PI(4,5)P2 IGLC1 Ig heavy chain V-III region JON Ig lambda chain V-VI region AR GTP IGLC3 Ig kappa chain V-III region POM IGKV1-5(23-?) IGLV5-45(1-?) PI(4,5)P2 FCGR3A Ig heavy chain V-I region EU IGLV2-18(1-?) IGLV8-61(1-?) IGKC IGLV(23-?) Ig kappa chain V-I region BAN Ig lambda chain V-IV region Kern Ig kappa chain V-I region Gal p-Y-WRC:IRSp53/58:RAC1:GTP:PIP3Ig kappa chain V-I region HK101 IGLV4-60(1-?) Ig kappa chain V-III region VG IGLC6 Ig lambda chain V-I region NEW IgH heavy chain V-III region VH26 precursor Ig heavy chain V-III region DOB IGKV1-12 IGLV2-33(1-?) IGLV2-23(1-?) ARPC1A Ig kappa chain V-I region Wes SRC-1 BRK1 IGKVA18(21-?) ARPC2 Ig kappa chain V-I region Daudi IGLV4-3(1-?) Ig heavy chain V-I region HG3 IGLV2-11(1-?) Ig heavy chain V-III region CAM IGKC Ig lambda chain V-I region VOR IGLV7-46(1-?) CDC42 Ig lambda chain V-IV region Bau IGLV4-69(1-?) Ig heavy chain V-III region JON IGHG3 IGLC3 Ig lambda chain V-IV region Bau Ig lambda chain V-I region NEW IGKV3D-20 ABI2 Ig kappa chain V-II region Cum Ig kappa chain V-III region VG IGLV(23-?) IGKC Ig heavy chain V-III region WEA Ig kappa chain V-III region B6 IGLV4-3(1-?) Ig kappa chain V-I region AG NCKAP1 IGLV3-25(1-?) Ig lambda chain V-I region VOR Ig lambda chain V-II region BOH IgG:Lmaantigens:FCGR3A:CD3dimersGDP Ig heavy chain V-II region MCE CYFIP2 G-actinIg lambda chain V-II region MGC IGLV7-43(1-?) N-WASP PIP3:VAV1,2,3Ig heavy chain V-II region MCE Ig kappa chain V-I region Daudi FCGR3A Ig kappa chain V-II region Cum IGLV1-44(1-?) ATPIg lambda chain V-III region SH Ig kappa chain V-I region Gal WIPF1 Ig kappa chain V-III region POM IGLV5-45(1-?) IGKC Ig kappa chain V-I region Gal IGLV7-46(1-?) Ig lambda chain V-VI region AR Ig heavy chain V-III region CAM IGLV1-36(1-?) Ig heavy chain V-III region WEA Ig kappa chain V-I region DEE Ig kappa chain V-II region RPMI 6410 p-6Y-CD247 VAV3 N-WASP IGLV7-43(1-?) N-WASP Ig heavy chain V-III region WEA ARPC1B p-Y151-WASF3 ACTR2 Ig heavy chain V-III region KOL Ig heavy chain V-II region MCE IGLV4-60(1-?) NCKAP1L p-4S-ABI2 Ig heavy chain V-III region TRO Ig kappa chain V region EV15 ATPIGLC7 IGLV4-69(1-?) IGLV4-3(1-?) IGLC1 p-6Y-CD247 WIPF1 CDC42:GTP:WASP/N-WASP:WIP:SH3 proteinsIg lambda chain V-II region BOH IGLV3-16(1-?) IGLV2-11(1-?) IGHV(1-?) SYKIg kappa chain V-I region DEE IGLV2-23(1-?) IGLV3-27(1-?) IGLV5-45(1-?) IGHG4 IGHV1-2 Ig heavy chain V-III region WEA p-T202,Y204-MAPK3 PI(3,4,5)P3 Ig kappa chain V region EV15 IGLV3-25(1-?) IGKC IgG:Leishmaniasurface:p-FCGR3A:p-6Y-SYK:CRKII:DOCK180:ELMOIGLV3-22(1-?) IGLC2 ACTG1 IGLV3-12(1-?) p-Y151-WASF3 CRK IGHG1 IGLC7 Ig heavy chain V-III region DOB Ig heavy chain V-II region OU F-actin Ig kappa chain V-I region DEE IGKVA18(21-?) ARPC1B Ig kappa chain V-III region VG ARPC4 Ig heavy chain V-II region NEWM Ig heavy chain V-II region MCE ABI1 Ig kappa chain V-II region Cum IGKV1-12 ABI1 NCKAP1 IGHG1 Ig lambda chain V-II region BOH IGLV3-25(1-?) Ig heavy chain V-III region DOB IGLV5-37(1-?) WASF2 IGKVA18(21-?)


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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  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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