FCGR3A-mediated phagocytosis (Homo sapiens)

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ArcPathVisio Brace Ellipse EndoplasmicReticulum GolgiApparatus HexagonPathVisio MimDegradation Mitochondria Octagon PentagonPathVisio Rectangle RoundedRectangle SarcoplasmicReticulum TriangleEquilateralEast TrianglePathVisio none cytosolphagocytic cupcytosolHostLeishmaniaCDC42:GTP:p-Y-WASP/p-Y-WASL:WIP:SH3 proteinsGDPFCGRIIIA:CD3G/CD3ZdimersPI(3,4,5)P3CDC42:GTP:WASP/N-WASPATPADPMyosin-X dimerBAIAP2ADPVAV1,2,3LPG1G2IgG:Lmaantigens:FCGR3A:p-CD3 dimers:p-6Y-SYKRAC1:GDPMyosinATPIgG:Lma amastigotesurfaceIgGADPIgG:Lma antigensIgG:Leishmaniasurface:p-FCGR3A:p-6Y-SYK:CRKII:DOCK180:ELMOPIP3:VAV1,2,3IgG:Lmaantigens:FCGR3A:p-CD3 dimersGTPG-actinIgG:Leishmaniasurface:FCGR3Ap-CD3dimers:p-6Y-SYK:VAV1,2,3:PI(3,4,5)P3ADPADPPI(4,5)P2:WASP/N-WASPIgG:Leishmaniasurface:FCGR3ACDC42:GTPPI(3,4)P2Myosin-Actinfilamentsp-Y,S,T-WRC:IRSp53/58:RAC1:GTP:PIP3p-T,Y MAPK dimersPiGDPATPMotherfilament:branchingcomplexWASP/N-WASPIgG:Leishmaniasurface:p-FCGR3A:p-6Y-SYK:p-VAV1,2,3:PI(3,4,5)P3GTPGDPp-Y-WRC:IRSp53/58:RAC1:GTP:PIP3ATPADPPI(4,5)P2ARP2/3 complex (ATPbound)WRC:IRSp53/58:RAC1:GTP:PIP3CDC42:GTP:WASP/N-WASP:WIP:SH3 proteinsSrc family kinases(SFKs)WAVE2, WASP,N-WASP:ARP2/3complex:G-actinSrc family kinases(SFKs)Motherfilament:branchingcomplex:daughterfilamentPiATPRAC1:GTPRAC1:GDPSH3 domain proteinsADPMotherfilament:ARP2/3:actin:ADPSYKUnknown GEFATPSrc-kinasesGTPIgG:Lmaantigens:FCGR3A:CD3dimersCRK:DOCK180:ELMO1,ELMO2ATPF-actinCDC42:GDPATPWAVE RegulatoryComplexABL1WAVE2, WASP, N-WASPIgG:LPG1G2Lma amastigotesurfaceWIP family proteinsIgG:Lmaantigens:FCGR3A:p-CD3 dimers:SYKG-actinActin filament boundMyosin-XMYO1CMYH9MYH2MYO5AMYO9BATPACTB(1-375)ACTG1Ig kappa chain V-II region CumIg heavy chain V-III region DOBIGLV11-55(1-?)Ig lambda chain V-IV region BauIGKV2D-30IGLV5-45(1-?)Ig lambda chain V-VI region ARIGKV1-12Ig heavy chain V-III region CAMIGHG1IGLV2-23(1-?)IGKV2-28Ig kappa chain V-I region HK101Ig lambda chain V region 4AIGKV3D-20IGKVA18(21-?)Ig kappa chain V-III region B6IgH heavy chain V-III region VH26 precursorIGLC7Ig heavy chain V-III region BROIGLV7-43(1-?)IGHG2Ig kappa chain V-I region DEEIg kappa chain V-I region DaudiIg heavy chain V-III region WEAIg heavy chain V-II region WAHIg heavy chain V-I region EUIGLV8-61(1-?)IGLV2-18(1-?)IGKV4-1(21-?)IGLC1IGLV2-11(1-?)Ig kappa chain V-I region BANIg lambda chain V-I region VORIGLV1-36(1-?)IGHG3Ig kappa chain V-I region GalIg lambda chain V-II region TOGIGKV1-5(23-?)IGLV10-54(1-?)Ig kappa chain V region EV15Lma amastigote surfaceIGLV3-27(1-?)IGLV7-46(1-?)IGLC3Ig lambda chain V-IV region KernIg lambda chain V-III region SHIGLV3-25(1-?)IGHV(1-?)Ig lambda chain V-I region NEWIGHG4Ig kappa chain V-II region FRIGHV7-81(1-?)LPG1G2Ig heavy chain V-I region HG3Ig heavy chain V-III region BUTIGLV1-40(1-?)Ig lambda chain V-III region LOIIg lambda chain V-I region NEWMIGLV3-22(1-?)IGLC6Ig lambda chain V-II region BOHIg heavy chain V-II region NEWMIg heavy chain V-II region MCEIg kappa chain V-I region WesIGLC2Ig lambda chain V-IV region HilIGLV3-12(1-?)IGLV(23-?)Ig heavy chain V-III region KOLIGLV4-69(1-?)Ig kappa chain V-II region RPMI 6410Ig heavy chain V-II region ARH-77Ig lambda chain V-II region MGCIGLV2-33(1-?)Ig lambda chain V-II region NEIIg heavy chain V-III region TROIGLV4-60(1-?)Ig kappa chain V-III region VGIg heavy chain V-III region JONIg kappa chain V-III region POMIg heavy chain V-II region OUIGLV1-44(1-?)IGKCIg kappa chain V-I region AUIg lambda chain V-I region HAIGHV1-2IGLV3-16(1-?)IGLV4-3(1-?)IGLV5-37(1-?)Ig kappa chain V-I region AGIg kappa chain V-III region B6IGLC3Ig heavy chain V-III region CAMIGHV1-2Ig heavy chain V-II region ARH-77Ig lambda chain V-III region SHIg kappa chain V-I region DaudiIGLV4-60(1-?)Ig lambda chain V region 4ALma amastigote surfaceIg heavy chain V-II region NEWMIGLV1-36(1-?)Ig kappa chain V-I region HK101Ig lambda chain V-I region HAIg heavy chain V-III region JONIGLV2-23(1-?)IGKV4-1(21-?)IGKV1-5(23-?)IGLV5-45(1-?)IGHV7-81(1-?)Ig lambda chain V-VI region ARIg lambda chain V-III region LOIIg heavy chain V-III region DOBp-6Y-CD247IGLC6IGLV5-37(1-?)Ig heavy chain V-II region WAHIGLV3-16(1-?)Ig heavy chain V-II region MCEIg kappa chain V-I region DEEIg heavy chain V-III region WEAIGLV8-61(1-?)Ig lambda chain V-I region NEWMIg lambda chain V-I region VORIg lambda chain V-IV region BauIGHV(1-?)Ig heavy chain V-III region BROIGKV2D-30Ig heavy chain V-III region KOLIg lambda chain V-II region NEIIg kappa chain V-I region WesIg lambda chain V-II region TOGIGHG2Ig lambda chain V-IV region KernIg heavy chain V-III region TROIGHG4IGKV1-12Ig kappa chain V-I region GalVAV1IGLV7-46(1-?)Ig kappa chain V region EV15IGHG1IGKVA18(21-?)Ig kappa chain V-II region CumIGLV7-43(1-?)IGLV3-12(1-?)Ig heavy chain V-I region HG3Ig heavy chain V-II region OUIGLC1Ig lambda chain V-I region NEWIGLV2-33(1-?)Ig kappa chain V-I region AUIgH heavy chain V-III region VH26 precursorIg kappa chain V-I region AGIg kappa chain V-III region VGIGKV3D-20IGLV(23-?)PI(3,4,5)P3p-6Y-SYKIGKCIGLV4-69(1-?)IGLV3-25(1-?)FCGR3ALPG1G2IGLV4-3(1-?)VAV2IGLV2-18(1-?)Ig kappa chain V-I region BANVAV3IGLV1-40(1-?)IGHG3Ig kappa chain V-II region RPMI 6410IGKV2-28Ig lambda chain V-II region BOHIg kappa chain V-II region FRIGLV1-44(1-?)IGLV3-22(1-?)IGLC2p-Y160,Y171-CD3GIGLV3-27(1-?)IGLV11-55(1-?)Ig heavy chain V-I region EUIGLV10-54(1-?)IGLV2-11(1-?)IGLC7Ig lambda chain V-II region MGCIg kappa chain V-III region POMIg lambda chain V-IV region HilIg heavy chain V-III region BUTGDPRAC1GTPRAC1F-actinARPC3ARPC5ACTR3ACTB(1-375)ARPC1AARPC4ADPACTG1ARPC2ACTR2ARPC1BATPABI1NCKAP1LABI2CYFIP2WASF3BRK1WASF2WASF1CYFIP1NCKAP1ARPC1AARPC2ACTR2ACTR3ARPC3ATPARPC5F-actinARPC1BARPC4VAV1VAV3VAV2Ig kappa chain V-I region BANIg kappa chain V-II region RPMI 6410IGLV5-45(1-?)IGLV5-37(1-?)Ig heavy chain V-I region HG3Ig lambda chain V-IV region Kernp-Y172-VAV2IGLV11-55(1-?)IGHV7-81(1-?)Ig kappa chain V-III region B6Ig kappa chain V-I region HK101Ig lambda chain V-VI region ARIGKV3D-20Ig heavy chain V-II region WAHIg lambda chain V-III region SHp-6Y-SYKIGKV2-28Ig heavy chain V-III region BUTIGLC3Ig kappa chain V-I region WesIg kappa chain V-I region DaudiIg lambda chain V-II region NEIIg lambda chain V-I region HAIg heavy chain V-III region WEALPG1G2IGHV1-2IGLC7Ig kappa chain V-I region DEEIGHV(1-?)IGKV2D-30Ig kappa chain V-III region POMIg kappa chain V-I region AUIGLV7-43(1-?)IGLV1-40(1-?)IGLV(23-?)PI(3,4,5)P3IGLV2-11(1-?)IGLC2p-Y173-VAV3IGLV8-61(1-?)p-6Y-CD247IGLV7-46(1-?)IgH heavy chain V-III region VH26 precursorIg lambda chain V-I region NEWMIg lambda chain V-IV region HilIGKV4-1(21-?)Ig lambda chain V-II region MGCIGHG2p-Y174-VAV1IGLV4-3(1-?)IGKCIGLV2-23(1-?)Ig lambda chain V-II region TOGIg kappa chain V-II region FRIg lambda chain V-I region VORIGLV3-25(1-?)IGLV1-36(1-?)Ig heavy chain V-III region TROIGHG4IGKV1-12Ig heavy chain V-I region EUIg lambda chain V-I region NEWIGKV1-5(23-?)IGLV4-60(1-?)Ig heavy chain V-III region BROIGLV3-12(1-?)Ig heavy chain V-III region JONIg heavy chain V-III region CAMIGKVA18(21-?)Ig heavy chain V-II region OUIg heavy chain V-II region NEWMIGLC6IGHG1Ig lambda chain V region 4AFCGR3AIg kappa chain V region EV15Ig heavy chain V-II region MCEIg kappa chain V-III region VGIGLV3-22(1-?)p-Y160,Y171-CD3GLma amastigote surfaceIGLV3-16(1-?)Ig kappa chain V-I region AGIGHG3Ig lambda chain V-III region LOIIGLV2-18(1-?)Ig heavy chain V-II region ARH-77Ig heavy chain V-III region KOLIGLV3-27(1-?)IGLV4-69(1-?)Ig lambda chain V-II region BOHIGLV2-33(1-?)IGLC1IGLV1-44(1-?)Ig kappa chain V-II region CumIg kappa chain V-I region GalIGLV10-54(1-?)Ig lambda chain V-IV region BauIg heavy chain V-III region DOBGDPRAC1p-T202,Y204-MAPK3p-T185,Y187-MAPK1GTPNCKAP1LABI2p-Y151-WASF3CYFIP1BAIAP2p-Y151-WASF1BRK1p-Y150-WASF2NCKAP1RAC1ABI1PI(3,4,5)P3CYFIP2ARPC4ARPC3ARPC1AACTR3ARPC1BACTR2ATPARPC5ARPC2WASPI(4,5)P2CDC42N-WASPGTPIg lambda chain V-I region NEWMIGKV1-5(23-?)Ig heavy chain V-I region HG3Ig lambda chain V-II region BOHIg kappa chain V-I region DEEIGLV2-33(1-?)IGLV4-69(1-?)IGHG1Ig kappa chain V-III region B6Ig lambda chain V-I region VORIg kappa chain V-III region POMIGLV3-22(1-?)IGLV10-54(1-?)IGLV3-12(1-?)Ig kappa chain V region EV15IGHG2Ig heavy chain V-II region NEWMIg lambda chain V-II region NEIIGLV7-43(1-?)Ig lambda chain V-II region TOGIg heavy chain V-III region TROIg kappa chain V-II region RPMI 6410Ig kappa chain V-I region AUIGLV2-11(1-?)IGLC2Ig lambda chain V-VI region ARIg lambda chain V-IV region HilIGLV2-18(1-?)IGLV2-23(1-?)IGLV3-25(1-?)IGLV3-16(1-?)Ig heavy chain V-II region WAHIGKVA18(21-?)Ig lambda chain V-IV region KernIg kappa chain V-I region AGIg heavy chain V-III region BROIg lambda chain V-I region HAIGLC3IGHG4IGLC1IGKCIgH heavy chain V-III region VH26 precursorIGLV1-36(1-?)IGLC6IGLV11-55(1-?)IGKV2D-30IGKV4-1(21-?)Ig lambda chain V region 4AIg heavy chain V-III region KOLIg heavy chain V-III region CAMIg heavy chain V-II region OUIg lambda chain V-III region LOIIg kappa chain V-I region DaudiIg lambda chain V-II region MGCIg heavy chain V-III region WEAIGLV8-61(1-?)IGHV1-2Ig heavy chain V-I region EUIGKV2-28IGLV5-45(1-?)Ig heavy chain V-III region DOBIGLV1-44(1-?)IGHG3Ig heavy chain V-III region JONIg heavy chain V-II region ARH-77IGLV7-46(1-?)Ig lambda chain V-I region NEWIg kappa chain V-I region WesIg kappa chain V-II region CumIGLV5-37(1-?)IGLV(23-?)Ig lambda chain V-III region SHIGLV1-40(1-?)Ig kappa chain V-III region VGIg kappa chain V-I region HK101IGHV(1-?)Ig kappa chain V-I region GalIGLV4-60(1-?)IGHV7-81(1-?)Ig kappa chain V-II region FRIGLV3-27(1-?)Ig lambda chain V-IV region BauIGKV3D-20Ig heavy chain V-II region MCEIg heavy chain V-III region BUTIGLC7IGLV4-3(1-?)Ig kappa chain V-I region BANIGKV1-12ABI2GTPNCKAP1WASF3PI(3,4,5)P3NCKAP1LBRK1BAIAP2WASF2ABI1CYFIP2RAC1WASF1CYFIP1PI(4,5)P2N-WASPWASCDC42NCKIPSDGRB2-1GTPWIPF2WIPF1PI(4,5)P2WIPF3p-Y256-WASLNCK1p-Y291-WASCDC42GDPHCKLYNYES1FYNSRC-1FGRABI2WIPF1p-Y151-WASF3CYFIP2p-Y150,S343,T346-WASF2p-Y150-WASF2GTPp-Y151-WASF1NCKAP1PI(4,5)P2p-Y151,S,T-WASF1p-5S-ABI1CDC42ABI1PI(3,4,5)P3CYFIP1NCKIPSDBRK1BAIAP2NCKAP1LWIPF2p-Y256-WASLp-4S-ABI2p-Y151,S,T-WASF3RAC1p-Y291-WASWIPF3NCK1GRB2-1ARPC1AACTR3ATPARPC4ARPC3MYO9BMYO5AMYH2ARPC1BADPACTR2F-actinMYH9ARPC2MYO1CARPC5FYNFGRLYNHCKYES1SRC-1Ig heavy chain V-III region BROIGKV1-12Ig heavy chain V-I region HG3Ig lambda chain V-IV region KernIGLV1-36(1-?)Ig kappa chain V-III region VGIg lambda chain V-I region NEWIGLV2-11(1-?)Ig kappa chain V-II region FRIg lambda chain V-VI region ARIg lambda chain V-II region NEIIg lambda chain V-I region VORIGLC6IGLV3-12(1-?)Lma amastigote surfaceIGLV10-54(1-?)IGHG1IGLC1Ig kappa chain V-I region AGIGLV(23-?)Ig heavy chain V-I region EUIGLV11-55(1-?)IGKCIGLV3-27(1-?)Ig heavy chain V-III region CAMIGKV1-5(23-?)IGHG2IGLV8-61(1-?)Ig kappa chain V-II region CumIg lambda chain V-I region HAIGKVA18(21-?)Ig heavy chain V-II region MCEIg heavy chain V-III region KOLIGHV7-81(1-?)IGHV1-2IGKV2D-30Ig kappa chain V-I region DEEIg lambda chain V-II region TOGIGLV1-44(1-?)IGLV7-46(1-?)IGKV2-28IGLV2-33(1-?)IGLV2-18(1-?)Ig lambda chain V-I region NEWMIg heavy chain V-III region JONIGLC3Ig heavy chain V-III region TROIg kappa chain V-II region RPMI 6410Ig lambda chain V-III region LOIIGHG4Ig heavy chain V-III region DOBIGLC7Ig heavy chain V-II region NEWMIGLV5-37(1-?)Ig heavy chain V-II region ARH-77IGLV2-23(1-?)Ig kappa chain V-III region POMIg heavy chain V-III region BUTIGLV4-3(1-?)Ig kappa chain V-I region DaudiIGLV5-45(1-?)IGLV4-69(1-?)Ig lambda chain V-II region BOHIg heavy chain V-II region OUIGLV3-22(1-?)IGLV1-40(1-?)Ig heavy chain V-II region WAHIGLC2Ig lambda chain V-IV region BauIg lambda chain V-IV region HilIGHV(1-?)IGLV4-60(1-?)Ig lambda chain V-II region MGCIg kappa chain V-I region WesIGHG3Ig lambda chain V region 4AIGKV3D-20IGLV7-43(1-?)Ig kappa chain V region EV15Ig lambda chain V-III region SHIg heavy chain V-III region WEAIg kappa chain V-I region GalIg kappa chain V-I region BANIg kappa chain V-I region HK101Ig kappa chain V-III region B6IGLV3-25(1-?)IgH heavy chain V-III region VH26 precursorIGLV3-16(1-?)IGKV4-1(21-?)Ig kappa chain V-I region AURAC1PI(3,4,5)P3p-Y151,S,T-WASF1p-4S-ABI2p-5S-ABI1NCKAP1CYFIP2BRK1NCKAP1Lp-Y150,S343,T346-WASF2CYFIP1BAIAP2p-Y151,S,T-WASF3GTPWASN-WASPN-WASPWIPF1NCKIPSDWIPF3GRB2-1CDC42GTPWASWIPF2PI(4,5)P2NCK1ARPC2ARPC5NCKAP1ACTR2p-Y150-WASF2ACTB(1-375)ABI1p-Y256-WASLARPC1Bp-Y151,S,T-WASF1WIPF2BAIAP2GRB2-1NCK1ARPC1API(3,4,5)P3WIPF3ATPARPC4p-Y291-WASCYFIP2PI(4,5)P2p-Y150,S343,T346-WASF2F-actinp-Y151-WASF1RAC1BRK1ARPC3NCKIPSDp-Y151-WASF3CYFIP1p-4S-ABI2p-5S-ABI1WIPF1NCKAP1Lp-Y151,S,T-WASF3CDC42GTPACTG1ABI2ACTR3Ig lambda chain V-I region HAIGLC2Ig lambda chain V-III region LOIIGKVA18(21-?)FCGR3ACD3GIGLV8-61(1-?)Ig heavy chain V-III region DOBIg kappa chain V-I region DaudiIGLV7-46(1-?)IGLV3-27(1-?)Ig lambda chain V-IV region BauIGKCIg kappa chain V-III region POMIg kappa chain V-II region FRIGLV11-55(1-?)Ig kappa chain V region EV15IGLV5-45(1-?)IGLV10-54(1-?)IGLV3-22(1-?)IGHV(1-?)IGLV7-43(1-?)Ig lambda chain V-II region MGCIGLV4-3(1-?)Ig lambda chain V-IV region KernIGLC7IGLC1IGKV4-1(21-?)Lma amastigote surfaceIGKV2D-30IGLV3-25(1-?)Ig heavy chain V-II region NEWMIg heavy chain V-II region OUIg heavy chain V-II region ARH-77IGLV4-60(1-?)Ig kappa chain V-II region RPMI 6410IGLC3Ig heavy chain V-I region HG3Ig kappa chain V-I region DEEIg lambda chain V-II region BOHIGLV2-18(1-?)IGLV5-37(1-?)IGKV3D-20Ig kappa chain V-II region CumIGHG2Ig heavy chain V-III region KOLIg lambda chain V-II region TOGIg lambda chain V-IV region HilIg heavy chain V-III region TROIg kappa chain V-I region WesIGLV1-36(1-?)Ig heavy chain V-III region WEAIg kappa chain V-I region AGIg lambda chain V region 4AIg lambda chain V-VI region ARIGLV3-16(1-?)Ig heavy chain V-II region WAHIg heavy chain V-III region JONIGHV7-81(1-?)Ig kappa chain V-I region HK101IGKV1-12Ig kappa chain V-III region B6IGKV2-28IGHG1IGLV3-12(1-?)IGHV1-2IGLV2-33(1-?)IGLC6IGKV1-5(23-?)Ig lambda chain V-I region NEWIg heavy chain V-III region BUTIg heavy chain V-III region BROIg heavy chain V-III region CAMIgH heavy chain V-III region VH26 precursorIg kappa chain V-I region GalIg lambda chain V-I region NEWMIg kappa chain V-III region VGIg kappa chain V-I region AUIGHG3IGLV1-40(1-?)LPG1G2IGLV4-69(1-?)Ig heavy chain V-II region MCEIg lambda chain V-III region SHCD247-1IGHG4Ig lambda chain V-I region VORIGLV2-23(1-?)Ig lambda chain V-II region NEIIGLV1-44(1-?)IGLV(23-?)Ig heavy chain V-I region EUIg kappa chain V-I region BANIGLV2-11(1-?)IGLC3IGLV2-11(1-?)Ig kappa chain V region EV15IGLV8-61(1-?)Ig heavy chain V-III region JONIg heavy chain V-III region TROSYKLma amastigote surfaceIg kappa chain V-I region AUIGHG4IGHV7-81(1-?)IGLV11-55(1-?)Ig kappa chain V-I region HK101Ig kappa chain V-III region VGIg kappa chain V-III region POMIg lambda chain V-II region MGCFCGR3AIGLC7Ig lambda chain V-II region NEIIg heavy chain V-I region HG3IGLC6Ig heavy chain V-II region ARH-77Ig lambda chain V-I region VORIg kappa chain V-II region CumIGLV3-22(1-?)Ig heavy chain V-III region WEAp-Y160,Y171-CD3GIg lambda chain V-I region NEWMIg heavy chain V-III region DOBIg kappa chain V-III region B6IGLV2-23(1-?)Ig heavy chain V-II region WAHIGKV2-28Ig kappa chain V-II region RPMI 6410IGLV2-18(1-?)IGLV7-46(1-?)Ig lambda chain V-VI region ARIGLV1-44(1-?)IGLV1-36(1-?)IGLV3-12(1-?)Ig heavy chain V-III region KOLIGHG2Ig lambda chain V region 4AIGKV3D-20IGKCIg lambda chain V-I region NEWIGKV2D-30IGLC2IGKV1-12Ig lambda chain V-IV region KernIGHG3Ig kappa chain V-II region FRIg kappa chain V-I region BANIg heavy chain V-III region BUTIGLV5-37(1-?)Ig lambda chain V-II region TOGIGLV3-16(1-?)IGLV4-60(1-?)Ig kappa chain V-I region DaudiIg lambda chain V-III region SHIGHV(1-?)IGLV10-54(1-?)Ig kappa chain V-I region DEEIGLV7-43(1-?)IGHV1-2Ig kappa chain V-I region WesIGLV3-27(1-?)IGLV(23-?)IGLV3-25(1-?)Ig heavy chain V-II region NEWMIGLV5-45(1-?)Ig kappa chain V-I region AGIg heavy chain V-II region OUIGLC1Ig heavy chain V-II region MCEIgH heavy chain V-III region VH26 precursorIGKV1-5(23-?)Ig heavy chain V-III region CAMIGLV2-33(1-?)Ig lambda chain V-IV region HilIg lambda chain V-II region BOHIGKV4-1(21-?)Ig lambda chain V-III region LOIIg lambda chain V-I region HAIGLV4-3(1-?)IGLV1-40(1-?)IGKVA18(21-?)IGLV4-69(1-?)p-6Y-CD247LPG1G2Ig heavy chain V-I region EUIg lambda chain V-IV region BauIg heavy chain V-III region BROIGHG1Ig kappa chain V-I region GalWIPF2WIPF1WIPF3NCKIPSDNCK1GRB2-1CD3GFCGR3ACD247-1IGLV3-16(1-?)Ig kappa chain V-II region RPMI 6410Ig lambda chain V region 4AIGLV1-44(1-?)Ig lambda chain V-IV region HilIGHV7-81(1-?)IgH heavy chain V-III region VH26 precursorIGLV7-46(1-?)Ig lambda chain V-II region BOHIGLV1-36(1-?)Ig kappa chain V region EV15Ig lambda chain V-I region NEWIg lambda chain V-I region NEWMIGLV2-18(1-?)IGLV2-11(1-?)Ig lambda chain V-III region SHIGKV3D-20IGLV2-23(1-?)IGHG4Ig kappa chain V-I region BANLma amastigote surfaceIg kappa chain V-III region B6Ig heavy chain V-III region JONIg lambda chain V-VI region ARIGKV2D-30IGLV4-3(1-?)Ig heavy chain V-III region BUTIg kappa chain V-I region DaudiIg heavy chain V-I region EUIGLV5-45(1-?)IGKCIg kappa chain V-II region FRIg heavy chain V-III region CAMIg lambda chain V-II region NEIIGLV3-22(1-?)IGLV(23-?)Ig heavy chain V-II region ARH-77Ig kappa chain V-II region CumLPG1G2IGLC7Ig lambda chain V-IV region BauIg kappa chain V-I region DEEIGKV1-12IGHV1-2Ig lambda chain V-III region LOIIGLV2-33(1-?)Ig kappa chain V-I region HK101Ig kappa chain V-I region AGIg lambda chain V-II region MGCIg kappa chain V-I region GalIGLV8-61(1-?)IGHG1FCGR3AIGLV10-54(1-?)IGLV11-55(1-?)IGKVA18(21-?)IGLV3-12(1-?)Ig lambda chain V-IV region KernIGLC1Ig heavy chain V-II region NEWMIGLV4-69(1-?)IGHG2IGLV3-25(1-?)IGHG3Ig heavy chain V-II region WAHIGLV4-60(1-?)Ig heavy chain V-III region WEAIg kappa chain V-I region WesIg heavy chain V-III region TROIGLV5-37(1-?)Ig lambda chain V-I region HAIg heavy chain V-III region DOBIg kappa chain V-III region VGIGKV2-28Ig kappa chain V-III region POMIg kappa chain V-I region AUIGLV3-27(1-?)Ig heavy chain V-II region MCEIg lambda chain V-I region VORIGHV(1-?)Ig heavy chain V-III region KOLIg lambda chain V-II region TOGIGKV1-5(23-?)IGLV7-43(1-?)IGLV1-40(1-?)IGLC3Ig heavy chain V-I region HG3Ig heavy chain V-III region BROIg heavy chain V-II region OUIGLC2IGLC6IGKV4-1(21-?)MYO10ATPPI(3,4)P2ARPC1BARPC3F-actinARPC5ARPC2ACTR3ARPC4ADPACTR2ARPC1ABAIAP2p-Y151-WASF3CYFIP1ATPCYFIP2NCKAP1p-Y291-WASBRK1NCK1p-Y151,S,T-WASF1GRB2-1WIPF1NCKIPSDWIPF3ARPC4NCKAP1LPI(3,4,5)P3p-4S-ABI2p-Y151-WASF1ACTB(1-375)PI(4,5)P2ARPC1BABI2GTPARPC3RAC1ACTR3p-Y151,S,T-WASF3p-Y150-WASF2ARPC1AARPC2p-5S-ABI1ARPC5p-Y150,S343,T346-WASF2ACTG1ABI1WIPF2ACTR2p-Y256-WASLCDC42BTKPTK2ACTG1ACTB(1-375)ATPIGLV2-23(1-?)Ig lambda chain V-I region VORIg lambda chain V-II region TOGIGLV11-55(1-?)Ig kappa chain V-II region RPMI 6410Ig kappa chain V-II region FRIg heavy chain V-III region BUTIg lambda chain V-II region MGCp-6Y-CD247IGKCIg kappa chain V-II region CumIGLV3-22(1-?)IGLV1-36(1-?)Ig heavy chain V-II region WAHIg kappa chain V-III region POMIGHG2Ig heavy chain V-I region HG3Ig lambda chain V-I region NEWMIg lambda chain V-IV region BauIg heavy chain V-III region JONIg heavy chain V-III region KOLIGLV3-12(1-?)Ig lambda chain V-I region HAIGKVA18(21-?)IGLV2-18(1-?)Ig kappa chain V-I region DaudiIGLV3-25(1-?)IGKV2D-30Ig heavy chain V-II region ARH-77IGLV7-43(1-?)IGLV3-27(1-?)IGHG4IGHV1-2Ig heavy chain V-III region WEAIGHV7-81(1-?)Ig heavy chain V-III region BROIGLV(23-?)IGLV5-45(1-?)IGHV(1-?)IGLC3IGLV4-60(1-?)IGKV1-5(23-?)FCGR3AIg lambda chain V-I region NEWIGLV2-11(1-?)IGLV1-44(1-?)Ig lambda chain V region 4AIGKV2-28Ig heavy chain V-II region OUp-Y160,Y171-CD3GIg kappa chain V-I region DEEIg lambda chain V-II region NEIIg heavy chain V-II region NEWMIg lambda chain V-IV region HilIg lambda chain V-III region LOIIGLC6Ig kappa chain V-III region VGIGKV1-12IGKV4-1(21-?)Ig kappa chain V-III region B6Ig kappa chain V-I region GalIGLV4-69(1-?)Ig heavy chain V-II region MCEIg lambda chain V-VI region ARIGKV3D-20IGLV2-33(1-?)Ig kappa chain V-I region WesIg kappa chain V region EV15IGLV3-16(1-?)Ig kappa chain V-I region AGIg kappa chain V-I region BANIg heavy chain V-III region CAMIGHG1Ig heavy chain V-III region TROIGLC1LPG1G2IGLV8-61(1-?)IGLV4-3(1-?)Ig kappa chain V-I region HK101Ig lambda chain V-IV region KernIgH heavy chain V-III region VH26 precursorIGLV1-40(1-?)IGLC2Ig lambda chain V-II region BOHIg lambda chain V-III region SHLma amastigote surfaceIg heavy chain V-III region DOBIGHG3Ig heavy chain V-I region EUIGLV10-54(1-?)IGLC7Ig kappa chain V-I region AUIGLV5-37(1-?)IGLV7-46(1-?)ELMO1ELMO2CRKDOCK1MYO10IGLV3-22(1-?)IGLC2IGLC6IGLV4-69(1-?)IGHV1-2IGLV4-3(1-?)Ig kappa chain V region EV15Ig heavy chain V-I region HG3Ig kappa chain V-II region CumIGLV7-46(1-?)IGLV7-43(1-?)FCGR3AIGLV3-25(1-?)IGHG4Ig lambda chain V-I region HAIg lambda chain V-III region LOIIGKV1-5(23-?)IGLV3-16(1-?)IGHV(1-?)IGLV4-60(1-?)IGHG2IGLC1Ig heavy chain V-III region TROIgH heavy chain V-III region VH26 precursorIg heavy chain V-III region BROIg heavy chain V-II region ARH-77IGHG3IGLV1-36(1-?)IGLV3-12(1-?)Ig lambda chain V-IV region KernIg kappa chain V-III region VGIg kappa chain V-I region AUIGKV2D-30Ig kappa chain V-II region FRIGKV4-1(21-?)Ig kappa chain V-I region GalIGLV(23-?)Ig kappa chain V-I region DaudiDOCK1Ig lambda chain V-II region NEIIg heavy chain V-III region BUTp-6Y-CD247IGKV1-12Ig heavy chain V-III region CAMELMO2Ig kappa chain V-II region RPMI 6410IGLV1-44(1-?)IGLV8-61(1-?)Ig lambda chain V-II region BOHLma amastigote surfaceIGKV3D-20Ig heavy chain V-II region WAHIGLV1-40(1-?)Ig kappa chain V-I region WesIg kappa chain V-I region DEEIGLV3-27(1-?)IGLV5-45(1-?)Ig heavy chain V-III region JONIg lambda chain V-I region NEWIg lambda chain V-I region VORIGLV11-55(1-?)IGLC7IGHG1Ig kappa chain V-III region B6IGLC3IGLV2-11(1-?)Ig heavy chain V-II region MCEIg lambda chain V-IV region HilIg heavy chain V-III region WEAIg kappa chain V-I region BANIg lambda chain V region 4AIg kappa chain V-III region POMIGKV2-28IGLV2-33(1-?)Ig kappa chain V-I region AGIg heavy chain V-III region KOLp-6Y-SYKIGKCIGLV10-54(1-?)LPG1G2Ig heavy chain V-III region DOBIg heavy chain V-I region EUCRKp-Y160,Y171-CD3GIg heavy chain V-II region OUIGLV2-18(1-?)Ig lambda chain V-II region TOGIGLV5-37(1-?)IGHV7-81(1-?)IGKVA18(21-?)Ig lambda chain V-IV region BauELMO1Ig heavy chain V-II region NEWMIGLV2-23(1-?)Ig lambda chain V-I region NEWMIg kappa chain V-I region HK101Ig lambda chain V-VI region ARIg lambda chain V-II region MGCIg lambda chain V-III region SHCDC42GTPIg kappa chain V-I region AUIg heavy chain V-III region WEAIGLV3-12(1-?)Ig heavy chain V-II region NEWMIg heavy chain V-II region WAHIGKV1-5(23-?)Ig kappa chain V-III region VGIg kappa chain V-III region B6IGKV2-28IgH heavy chain V-III region VH26 precursorIg kappa chain V-II region CumIg kappa chain V-I region GalIGLV7-43(1-?)Ig heavy chain V-II region OUIg heavy chain V-III region BROIGKV2D-30Ig lambda chain V-III region SHIGLV(23-?)IGLV3-16(1-?)IGLV1-44(1-?)Ig lambda chain V-I region NEWIg kappa chain V-II region RPMI 6410IGLV11-55(1-?)IGLC2Ig lambda chain V region 4AIGLC6IGHG2IGHV1-2Ig kappa chain V-I region DaudiIGLV1-36(1-?)Lma amastigote surfaceIg heavy chain V-II region MCEIGHG4IGLC7p-Y160,Y171-CD3GIg heavy chain V-II region ARH-77Ig heavy chain V-I region EUIGLV10-54(1-?)Ig lambda chain V-IV region BauIGHV7-81(1-?)p-6Y-SYKIg kappa chain V-II region FRIGLC1IGLV2-33(1-?)IGHG3Ig lambda chain V-IV region HilIg heavy chain V-III region KOLIGLV8-61(1-?)Ig heavy chain V-III region DOBIg lambda chain V-II region TOGIg kappa chain V-I region BANIg heavy chain V-III region JONIGLV5-45(1-?)Ig lambda chain V-VI region ARIGLV3-22(1-?)Ig kappa chain V region EV15IGLV4-69(1-?)IGLV7-46(1-?)FCGR3AIGLV2-11(1-?)IGLV5-37(1-?)Ig lambda chain V-III region LOIIGHG1Ig lambda chain V-I region NEWMIg kappa chain V-III region POMIg lambda chain V-II region BOHIGKV1-12IGLC3IGLV3-25(1-?)IGLV2-23(1-?)IGLV4-3(1-?)Ig lambda chain V-II region NEIIGLV4-60(1-?)IGLV2-18(1-?)Ig heavy chain V-III region TROIg lambda chain V-IV region KernIGLV3-27(1-?)Ig lambda chain V-I region VORIGLV1-40(1-?)Ig heavy chain V-I region HG3Ig lambda chain V-I region HAIGKCIGHV(1-?)Ig heavy chain V-III region BUTIg kappa chain V-I region HK101LPG1G2p-6Y-CD247Ig heavy chain V-III region CAMIGKVA18(21-?)Ig kappa chain V-I region AGIGKV3D-20Ig kappa chain V-I region WesIg kappa chain V-I region DEEIg lambda chain V-II region MGCIGKV4-1(21-?)VAV3VAV1PI(3,4,5)P3VAV2IGLV7-46(1-?)Ig heavy chain V-III region KOLIGLC2Ig heavy chain V-III region TROIGLV(23-?)IGHV(1-?)Ig heavy chain V-I region EUIg kappa chain V-I region BANIg lambda chain V-III region SHIg lambda chain V-VI region ARIg lambda chain V-II region TOGIg lambda chain V region 4AIGHV7-81(1-?)IGKV3D-20IGLV1-40(1-?)IgH heavy chain V-III region VH26 precursorIGLC7Ig heavy chain V-II region OUIGLV8-61(1-?)Ig lambda chain V-IV region BauIg kappa chain V region EV15IGLV3-22(1-?)IGLV4-3(1-?)Ig lambda chain V-I region VORIg kappa chain V-III region VGIg kappa chain V-I region DEEIg lambda chain V-I region NEWMIGHG4Ig kappa chain V-I region WesIg lambda chain V-IV region KernIg heavy chain V-III region WEALPG1G2IGKVA18(21-?)IGKCIg heavy chain V-III region DOBIg lambda chain V-II region MGCIg kappa chain V-II region RPMI 6410IGHG2Ig heavy chain V-III region BROIGLV3-27(1-?)IGKV1-5(23-?)IGLC6Ig heavy chain V-III region JONIg kappa chain V-I region DaudiIGLV5-45(1-?)IGLV2-33(1-?)Ig lambda chain V-I region HAIg lambda chain V-II region BOHIg heavy chain V-III region BUTIGLV4-69(1-?)IGLV1-36(1-?)Ig heavy chain V-II region ARH-77IGKV2-28Ig heavy chain V-II region NEWMIGLV11-55(1-?)Ig heavy chain V-II region MCEIGKV1-12Ig lambda chain V-II region NEIIGLV3-16(1-?)IGLV3-12(1-?)Ig heavy chain V-II region WAHIg kappa chain V-I region GalIGLV2-18(1-?)IGLV1-44(1-?)IGHG3IGHG1Ig kappa chain V-II region FRIGLV7-43(1-?)Ig heavy chain V-III region CAMIg kappa chain V-I region HK101IGKV4-1(21-?)Ig lambda chain V-III region LOIIg kappa chain V-III region POMIGLV10-54(1-?)IGLV4-60(1-?)Ig kappa chain V-I region AGIGLV2-23(1-?)IGLV2-11(1-?)Ig heavy chain V-I region HG3Ig kappa chain V-I region AUIg kappa chain V-III region B6Ig lambda chain V-I region NEWIGLC3Ig lambda chain V-IV region HilIg kappa chain V-II region CumIGLC1IGLV5-37(1-?)IGHV1-2IGLV3-25(1-?)IGKV2D-30Name: FCGR3A-mediated phagocytosisOrganism: Homo sapiens


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: 75
Reactome Author 
Reactome Author: Jassal, Bijay

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Quality Tags

Image:Reactome.pngCommunity: Reactome
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Ontology Terms

Pathway Ontology : signaling pathway
 

Bibliography

View all...
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History

CompareRevisionActionTimeUserComment
114922
Reactome
view16:44, 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...
Name  ↓Type  ↓Database reference  ↓Comment  ↓
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:43474 (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...
Source  ↓Target  ↓Type  ↓Database reference  ↓Comment  ↓
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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