Fcgamma receptor (FCGR) dependent phagocytosis (Homo sapiens)

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ArcPathVisio Brace Ellipse EndoplasmicReticulum GolgiApparatus HexagonPathVisio MimDegradation Mitochondria Octagon PentagonPathVisio Rectangle RoundedRectangle SarcoplasmicReticulum TriangleEquilateralEast TrianglePathVisio none endoplasmic reticulum lumencytosolphagocytic cupAHCYL1:NAD+:ITPR1:I(1,4,5)P3 tetramerCDC42:GTP:p-Y-WASP/p-Y-WASL:WIP:SH3 proteinspLIMK dimer:HSP-90Phosphatidatephosphatasep-T,Y MAPK dimersDAGsMyosinATPH2OPLA2G6ARP2/3 complex (ATPbound)p-Y-WRC:IRSp53/58:RAC1:GTP:PIP3PLDPCVAV1,2,3RAC1:GTPPLC gamma1,2PI(3,4,5)P3LPCChoWAVE2, WASP, N-WASPp-4Y-PLCG1ADPCDC42:GTP:WASP/N-WASPMotherfilament:ARP2/3:actin:ADPActin filament boundMyosin-XADPclusteredIgG-Ag:FCGRsCDC42:GTP, RAC1:GTPWRC:IRSp53/58:RAC1:GTP:PIP3Motherfilament:branchingcomplex:daughterfilamentMyosin-X dimerPI3K:p-6Y-SYKADPCFL1ADPADPclusteredIgG-Ag:p-FCGRs:p-6Y-SYK:p-VAVPI(3,4,5)P3ADPGDPG-actinATPADPPI(3,4)P2ADPPAK1LIMK1Motherfilament:branchingcomplexFCGR2AATPPAPI(4,5)P2WAVE2, WASP,N-WASP:ARP2/3complex:G-actinUnknown GEFWAVE RegulatoryComplexPiPI(3,4,5)P3RAC1:GTP,CDC42:GTP:PAK1FCGRIA:CD3GhomodimerNF2Pip-Y,S,T-WRC:IRSp53/58:RAC1:GTP:PIP3p-T508-LIMK1ATPHSP90AA1,HSP90AB1Src family kinases(SFKs)DAGsclusteredIgG-Ag:p-FCGRsclusteredIgG-Ag:p-FCGRs:SYKPI(4,5)P2BAIAP2IP3 receptorhomotetramerIgG-Ag:FCGRIA:CD3GhomodimerATPSH3 domain proteinsclusteredIgG-Ag:p-FCGRsI(1,4,5)P3RAC1:GDPFCGRIIIA:CD3G/CD3ZdimersclusteredIgG-Ag:p-FCGRs:p-6Y-SYKCRKII:DOCK180:ELMOcomplex recruitedto phagocytic cupGTPSYKCDC42:GTPWASP/N-WASPSrc-kinasesAntigen:IgGIgG-Ag:FCGRIIAATPp-PLCGARAH2OpCofilin: ActiveLIMK-1CDC42:GDPATPITPR:I(1,4,5)P3tetramerPAK1 dimerIgG-Ag:FCGRIIIA:CD3G/CD3Z dimersclusteredIgG-Ag:p-FCGRsF-actinATPp-S144,T423-PAK1ATPPI3KPiATPADPWIP family proteinsCRK:DOCK180:ELMO1,ELMO2Ca2+ADPATPATPADPATPGDPABL1H2OPCclusteredIgG-Ag:p-FCGRs:p-6Y-SYK:VAVATPCa2+PI(4,5)P2clusteredIgG-Ag:p-FCGRs:p-6Y-SYK:p-3Y-PLCGATPH2OGTPG-actinMyosin-ActinfilamentsPhospho-PKC-delta/epsilonADPActive LIMK1PKC-delta/epsilonADPclusteredIgG-Ag:p-FCGRs:p-6Y-SYK:PLCGCDC42:GTP:WASP/N-WASP:WIP:SH3 proteinsABI2BRK1p-Y151-WASF1CYFIP1NCKAP1PI(3,4,5)P3RAC1NCKAP1LBAIAP2p-Y150-WASF2ABI1GTPCYFIP2p-Y151-WASF3ITPR3ITPR2ITPR1N-WASPWASGTPPI(4,5)P2CDC42PIK3R2PIK3CAPIK3R1PIK3CBp-S3-CFL1p-S,T508-LIMK1Ig heavy chain V-III region TROIg heavy chain V-II region MCEIGLV7-46(1-?)IGLV4-3(1-?)IGLC7IGHG2IGLC6IGKVA18(21-?)Ig lambda chain V-IV region BauIGHV(1-?)Ig heavy chain V-III region WEAIGLV10-54(1-?)IgH heavy chain V-III region VH26 precursorIGLV1-44(1-?)Ig lambda chain V-III region SHIg heavy chain V-III region KOLIGLV3-16(1-?)IGLC1Ig heavy chain V-III region BROIg lambda chain V-II region BOHIg kappa chain V-II region FRIg lambda chain V-I region VORIg kappa chain V-II region RPMI 6410Ig kappa chain V-I region AUFCGR3AIGHG4IGLV3-12(1-?)IGHV1-2IGLV3-25(1-?)IGKV1-5(23-?)Ig heavy chain V-II region ARH-77Ig kappa chain V-II region CumIGLV5-45(1-?)IGLV1-36(1-?)Ig heavy chain V-III region BUTIGLV2-23(1-?)IGLV4-69(1-?)Ig kappa chain V-I region GalIGHV7-81(1-?)IGLV2-18(1-?)Ig lambda chain V-II region TOGIGLC2IGLV3-27(1-?)Ig lambda chain V-I region NEWIGKV3D-20IGKV4-1(21-?)IGLV2-33(1-?)Ig kappa chain V-I region WesIGLV(23-?)IGKCCD3GIg lambda chain V-VI region ARIg lambda chain V-IV region KernIGLV2-11(1-?)IGKV2D-30Ig kappa chain V-I region HK101Ig lambda chain V-III region LOIIg heavy chain V-III region CAMCD247-1Ig lambda chain V-I region NEWMIg heavy chain V-II region WAHAntigenIg kappa chain V-III region VGIGLV11-55(1-?)IGKV2-28Ig heavy chain V-III region DOBIGHG3IGLV8-61(1-?)Ig kappa chain V region EV15Ig heavy chain V-I region HG3IGLV1-40(1-?)Ig heavy chain V-II region OUIg kappa chain V-I region AGIGKV1-12IGHG1FCGR1AIg lambda chain V-I region HAIg heavy chain V-I region EUFCGR2AIGLV5-37(1-?)Ig heavy chain V-III region JONIg heavy chain V-II region NEWMIGLV7-43(1-?)Ig lambda chain V region 4AIg lambda chain V-II region MGCIg lambda chain V-II region NEIIg kappa chain V-I region BANIg kappa chain V-I region DaudiIGLV4-60(1-?)Ig kappa chain V-I region DEEIg lambda chain V-IV region HilIg kappa chain V-III region B6Ig kappa chain V-III region POMIGLV3-22(1-?)IGLC3IGKVA18(21-?)IGHG4Ig lambda chain V-II region MGCp-6Y-CD247IGLV3-16(1-?)Ig kappa chain V region EV15IGLV2-23(1-?)IGKV3D-20IGLV4-60(1-?)IGLV7-43(1-?)Ig heavy chain V-I region HG3Ig heavy chain V-II region ARH-77IGLV4-3(1-?)Ig heavy chain V-III region DOBIg kappa chain V-III region B6IGKV2-28IGKV2D-30Ig kappa chain V-I region AUIg lambda chain V-IV region KernIg heavy chain V-III region BUTIGLV7-46(1-?)IGLV4-69(1-?)Ig kappa chain V-I region DEEIGHG2Ig heavy chain V-II region NEWMIGLV3-12(1-?)Ig kappa chain V-I region DaudiIGLC2IGLV2-18(1-?)Ig kappa chain V-I region WesIg lambda chain V-III region LOIIGHV7-81(1-?)IGLV1-40(1-?)IGLV3-27(1-?)Ig kappa chain V-II region FRIg heavy chain V-I region EUp-Y288,Y304-FCGR2AIg heavy chain V-III region JONIg heavy chain V-III region TROIGHV(1-?)IgH heavy chain V-III region VH26 precursorIg kappa chain V-I region AGIg kappa chain V-I region HK101IGKV1-5(23-?)Ig heavy chain V-II region MCEAntigenIg kappa chain V-II region RPMI 6410Ig heavy chain V-III region BROIGLV11-55(1-?)Ig lambda chain V-III region SHp-Y160,Y171-CD3GIg kappa chain V-III region POMIg lambda chain V-I region NEWMFCGR3AIg lambda chain V-I region NEWIGHG1IGLV1-36(1-?)IGLV(23-?)IGLV2-11(1-?)Ig kappa chain V-I region GalIg lambda chain V-IV region BauIGLC3Ig heavy chain V-III region KOLIg heavy chain V-II region WAHIGLC1Ig heavy chain V-II region OUIg lambda chain V-I region VORIGLC7Ig lambda chain V region 4AIGLV10-54(1-?)IGKCFCGR1AIGHG3IGLV1-44(1-?)IGHV1-2Ig kappa chain V-III region VGIg lambda chain V-II region NEIIGLC6IGKV4-1(21-?)Ig lambda chain V-I region HAIGLV8-61(1-?)Ig lambda chain V-II region BOHSYKIGKV1-12IGLV5-37(1-?)Ig lambda chain V-VI region ARIg heavy chain V-III region WEAIg lambda chain V-II region TOGIg kappa chain V-II region CumIg lambda chain V-IV region HilIg kappa chain V-I region BANIGLV3-25(1-?)IGLV3-22(1-?)IGLV5-45(1-?)IGLV2-33(1-?)Ig heavy chain V-III region CAMWIPF2WIPF3PI(4,5)P2NCKIPSDN-WASPWIPF1GTPWASNCK1CDC42GRB2-1NCKIPSDNCK1GRB2-1PLD1PLD2PLD3PLD4Ig kappa chain V-III region VGIg lambda chain V-IV region HilIg heavy chain V-III region TROIg heavy chain V-III region BROIGLV3-16(1-?)Ig heavy chain V-III region WEAIgH heavy chain V-III region VH26 precursorIg heavy chain V-II region OUIGHG1IGLV1-44(1-?)IGKCIg lambda chain V-IV region BauIg kappa chain V-III region POMIg heavy chain V-I region HG3IGLV2-23(1-?)IGLV8-61(1-?)IGLC3Ig lambda chain V-I region VORIGHV1-2IGLV7-46(1-?)Ig kappa chain V-I region DaudiIGKVA18(21-?)IGLV2-18(1-?)FCGR2AIGLV1-36(1-?)Ig heavy chain V-III region JONIg kappa chain V-I region HK101IGLV3-25(1-?)Ig heavy chain V-III region CAMAntigenIGLV1-40(1-?)Ig lambda chain V-II region MGCIGLC2IGLV7-43(1-?)IGLV3-12(1-?)IGLV10-54(1-?)Ig kappa chain V-I region DEEIg kappa chain V-I region GalIg lambda chain V-IV region KernIGHG3IGLC6Ig kappa chain V-II region CumIGLV4-60(1-?)Ig heavy chain V-II region WAHIGLC7Ig lambda chain V-VI region ARIg heavy chain V-II region ARH-77IGLV5-37(1-?)Ig heavy chain V-II region MCEIg kappa chain V-I region WesIGLV2-11(1-?)Ig lambda chain V-II region TOGIg kappa chain V-III region B6IGLV5-45(1-?)IGKV3D-20IGHG4IGLV3-22(1-?)Ig kappa chain V region EV15IGKV2-28IGLV4-69(1-?)Ig kappa chain V-II region FRIGLV2-33(1-?)Ig lambda chain V-I region NEWMIGLV(23-?)IGKV4-1(21-?)Ig lambda chain V-II region BOHIg kappa chain V-II region RPMI 6410Ig heavy chain V-I region EUIg lambda chain V-II region NEIIg kappa chain V-I region AGIg kappa chain V-I region BANIGKV1-12IGLV4-3(1-?)IGLV3-27(1-?)IGLC1Ig lambda chain V-I region HAIg kappa chain V-I region AUIGHV(1-?)Ig heavy chain V-III region DOBIGKV2D-30IGLV11-55(1-?)Ig lambda chain V-I region NEWIg lambda chain V-III region LOIIGHV7-81(1-?)Ig heavy chain V-II region NEWMIGHG2Ig heavy chain V-III region BUTIGKV1-5(23-?)Ig lambda chain V-III region SHIg heavy chain V-III region KOLIg lambda chain V region 4Ap-Y151,S,T-WASF1NCKIPSDGTPNCKAP1LABI1WIPF3BAIAP2p-Y151-WASF1GRB2-1WIPF2WIPF1RAC1NCK1CYFIP2NCKAP1p-Y151,S,T-WASF3PI(4,5)P2CYFIP1ABI2BRK1p-Y150,S343,T346-WASF2p-5S-ABI1p-Y151-WASF3PI(3,4,5)P3p-Y256-WASLp-Y291-WASp-4S-ABI2p-Y150-WASF2CDC42BTKPTK2ITPR3ITPR1ITPR2NAD+AHCYL1I(1,4,5)P3ACTG1ACTB(1-375)ATPF-actinARPC2ARPC5ACTR3ACTR2ARPC1AARPC3ATPARPC4ARPC1Bp-Y291-WASNCK1WIPF2p-Y256-WASLNCKIPSDWIPF1CDC42GTPGRB2-1WIPF3PI(4,5)P2PAK1CD247-1CD3GFCGR3Ap-S,T508-LIMK1F-actinARPC5MYH9ARPC4ARPC2MYO5AACTR3ATPACTR2ARPC3ADPARPC1BARPC1AMYO1CMYH2MYO9BF-actinARPC1AACTR2MYO10ADPARPC1BATPARPC3ARPC2ACTR3ARPC4ARPC5PI(3,4)P2MYO10NCKAP1BAIAP2PI(3,4,5)P3GTPp-Y150,S343,T346-WASF2p-4S-ABI2p-Y151,S,T-WASF1CYFIP2p-Y151,S,T-WASF3NCKAP1Lp-5S-ABI1CYFIP1BRK1RAC1IGHG3IGKCIGLV4-69(1-?)Ig heavy chain V-I region HG3IGKV2D-30IGLV5-37(1-?)Ig kappa chain V-III region B6IGKVA18(21-?)Ig heavy chain V-III region BROIGLV2-18(1-?)IGLV10-54(1-?)IGLC2Ig heavy chain V-II region MCEIGHG1IGKV1-5(23-?)Ig lambda chain V-II region MGCIg kappa chain V region EV15AntigenIg lambda chain V-I region VORIGLV7-43(1-?)Ig kappa chain V-II region FRIGLV2-33(1-?)Ig kappa chain V-III region POMIg kappa chain V-I region GalIgH heavy chain V-III region VH26 precursorIGHV7-81(1-?)IGLV3-12(1-?)IGLV3-22(1-?)Ig lambda chain V-IV region KernIGHG2Ig lambda chain V-I region HAIg lambda chain V-II region TOGIGLC7Ig heavy chain V-III region CAMIg heavy chain V-II region WAHIGLV3-16(1-?)IGLV3-27(1-?)Ig lambda chain V-II region BOHIg heavy chain V-III region DOBIg lambda chain V region 4AIGLC3Ig lambda chain V-I region NEWIg kappa chain V-I region AUIg lambda chain V-IV region HilIGLV3-25(1-?)Ig kappa chain V-II region RPMI 6410IGHV(1-?)IGLV2-23(1-?)IGLV4-60(1-?)IGKV4-1(21-?)IGLC6Ig heavy chain V-II region NEWMIGLV1-36(1-?)IGLV5-45(1-?)IGLV1-40(1-?)Ig kappa chain V-I region HK101IGKV2-28Ig heavy chain V-II region ARH-77Ig lambda chain V-IV region BauIg kappa chain V-I region WesIg kappa chain V-I region DEEIg lambda chain V-III region LOIIGLV7-46(1-?)Ig heavy chain V-II region OUIg heavy chain V-III region JONIGLC1Ig lambda chain V-I region NEWMIGLV(23-?)Ig kappa chain V-I region AGIGLV8-61(1-?)IGKV3D-20Ig lambda chain V-III region SHIg kappa chain V-III region VGIg kappa chain V-II region CumIg heavy chain V-III region WEAIg heavy chain V-I region EUIGKV1-12Ig lambda chain V-VI region ARIg heavy chain V-III region KOLIg lambda chain V-II region NEIIGHG4Ig kappa chain V-I region DaudiIGLV11-55(1-?)Ig heavy chain V-III region TROIGLV1-44(1-?)IGLV2-11(1-?)IGHV1-2Ig heavy chain V-III region BUTIGLV4-3(1-?)Ig kappa chain V-I region BANGTPCDC42FCGR1ACD3GITPR3ITPR1ITPR2I(1,4,5)P3N-WASPWASIGLV2-23(1-?)IGLV1-40(1-?)Ig heavy chain V-III region DOBIGLV1-36(1-?)PIK3R2Ig kappa chain V-I region AGIGHV7-81(1-?)Ig kappa chain V-III region POMIg lambda chain V-I region VORIg lambda chain V-II region BOHIGKV2D-30Ig heavy chain V-I region HG3p-Y160,Y171-CD3GIGLV3-16(1-?)Ig heavy chain V-I region EUIGLV4-69(1-?)IGHG2Ig kappa chain V-I region HK101IGLV3-12(1-?)Ig heavy chain V-III region CAMIGLV11-55(1-?)IGLV5-37(1-?)Ig lambda chain V-IV region BauIGLV2-11(1-?)IGLV2-18(1-?)IGLV3-27(1-?)IGHG4Ig kappa chain V-III region VGIGLV7-46(1-?)Ig lambda chain V-I region NEWMIGLV4-3(1-?)IGLV4-60(1-?)p-6Y-SYKIg kappa chain V-II region FRIg lambda chain V-III region LOIIGHV1-2Ig kappa chain V-I region AUIGLV8-61(1-?)AntigenPIK3R1IGLC3IGLC7IgH heavy chain V-III region VH26 precursorIGHG1IGLC6FCGR1AIGHV(1-?)Ig kappa chain V-II region CumIg heavy chain V-III region TROIg lambda chain V-II region TOGIGKV1-12Ig heavy chain V-II region ARH-77FCGR3AIg kappa chain V-I region DaudiIg kappa chain V-I region Wesp-Y288,Y304-FCGR2AIg heavy chain V-III region BROIg lambda chain V-IV region KernIg lambda chain V-VI region ARIg heavy chain V-II region WAHIg kappa chain V region EV15IGLC1Ig lambda chain V-III region SHIGKV4-1(21-?)IGKV3D-20IGHG3IGLV10-54(1-?)IGKV1-5(23-?)IGLV7-43(1-?)Ig heavy chain V-III region KOLIg kappa chain V-I region BANIg heavy chain V-II region NEWMIg heavy chain V-III region WEAIGLV2-33(1-?)Ig kappa chain V-III region B6Ig kappa chain V-II region RPMI 6410IGLV5-45(1-?)IGLV3-25(1-?)PIK3CAIg lambda chain V-IV region HilPIK3CBp-6Y-CD247Ig lambda chain V-I region NEWIGLV3-22(1-?)Ig lambda chain V region 4AIg heavy chain V-III region BUTIGKCIGLC2Ig heavy chain V-III region JONIGKVA18(21-?)IGKV2-28Ig heavy chain V-II region MCEIg kappa chain V-I region GalIGLV(23-?)IGLV1-44(1-?)Ig lambda chain V-I region HAIg lambda chain V-II region MGCIg kappa chain V-I region DEEIg heavy chain V-II region OUIg lambda chain V-II region NEIPPAPDC1BPPAPDC1AELMO1CRKDOCK1ELMO2IGLV(23-?)Ig kappa chain V-III region B6IGHG2Ig heavy chain V-III region JONIGKV1-12IGKV4-1(21-?)FCGR3AIg lambda chain V region 4AIg lambda chain V-I region HAIGLV1-44(1-?)IGLV5-37(1-?)Ig kappa chain V-I region GalIg lambda chain V-IV region BauIg kappa chain V-III region VGIg heavy chain V-I region EUIg heavy chain V-III region KOLIg kappa chain V-I region AUIg lambda chain V-IV region KernIg kappa chain V-II region CumIg kappa chain V-III region POMIg kappa chain V-I region HK101IGHV1-2Ig kappa chain V-I region AGIGHV(1-?)Ig lambda chain V-II region MGCIg kappa chain V-I region BANIg lambda chain V-II region NEIIGLV4-69(1-?)p-6Y-SYKIGLV3-16(1-?)IGKV1-5(23-?)Ig lambda chain V-III region SHp-Y160,Y171-CD3GIg heavy chain V-II region ARH-77IGLV3-25(1-?)IgH heavy chain V-III region VH26 precursorIGKV2D-30PI(3,4,5)P3IGKV2-28IGLV11-55(1-?)Ig kappa chain V-I region WesIGLC7Ig heavy chain V-III region CAMp-Y288,Y304-FCGR2AIg kappa chain V-I region DaudiIGLV1-36(1-?)IGLC1IGLV2-23(1-?)Ig heavy chain V-III region TROIGLV4-3(1-?)IGLC2Ig heavy chain V-II region NEWMVAV2IGHG4Ig heavy chain V-II region MCEIg lambda chain V-III region LOIAntigenVAV1IGKVA18(21-?)IGLV2-11(1-?)IGKV3D-20Ig kappa chain V-II region RPMI 6410Ig kappa chain V region EV15IGLV3-27(1-?)IGHG3IGLV2-33(1-?)IGLV2-18(1-?)IGLC3IGHV7-81(1-?)FCGR1AIg lambda chain V-I region NEWIGKCIg heavy chain V-I region HG3Ig heavy chain V-III region WEAIg lambda chain V-IV region HilIg lambda chain V-II region BOHIGLV8-61(1-?)IGLV10-54(1-?)Ig heavy chain V-III region BROIg heavy chain V-II region OUIGLV1-40(1-?)Ig lambda chain V-II region TOGIGLV5-45(1-?)Ig heavy chain V-III region DOBIGLV3-12(1-?)Ig heavy chain V-III region BUTIg heavy chain V-II region WAHIGLV7-43(1-?)IGLV7-46(1-?)Ig kappa chain V-II region FRIg lambda chain V-I region VORIGLV3-22(1-?)IGLC6IGHG1Ig lambda chain V-I region NEWMIg lambda chain V-VI region ARp-6Y-CD247Ig kappa chain V-I region DEEVAV3IGLV4-60(1-?)FCGR1AIg kappa chain V-I region DaudiIg heavy chain V-II region OUIGHG4Ig lambda chain V region 4AIg kappa chain V-II region FRIGLV1-36(1-?)IGLC7Ig lambda chain V-IV region KernIGLV8-61(1-?)Ig kappa chain V-III region POMIGLC3Ig lambda chain V-III region LOIIg lambda chain V-II region BOHIg kappa chain V-III region VGIGLV7-43(1-?)FCGR3Ap-6Y-CD247Ig lambda chain V-II region TOGIGHG2Ig kappa chain V-I region HK101IGKVA18(21-?)Ig lambda chain V-I region NEWIg kappa chain V-I region AUIg heavy chain V-III region TROIGLV3-27(1-?)Ig kappa chain V-I region GalIg kappa chain V-I region WesIGHG1IGLC1IGKV2D-30Ig kappa chain V-II region CumIGLV2-33(1-?)IGHV7-81(1-?)IGHG3IGLV5-37(1-?)IGKCIg lambda chain V-I region VORIGLV2-11(1-?)Ig heavy chain V-II region NEWMIGLC6Ig heavy chain V-II region ARH-77Ig heavy chain V-III region CAMIGKV4-1(21-?)Ig kappa chain V region EV15Ig kappa chain V-III region B6Ig kappa chain V-I region DEEIGLV3-25(1-?)IGLV7-46(1-?)Ig heavy chain V-III region JONIg lambda chain V-IV region BauIGLV2-23(1-?)Ig lambda chain V-II region NEIIg lambda chain V-IV region HilIg kappa chain V-I region AGIGLV3-16(1-?)IGLV11-55(1-?)IGHV(1-?)Ig heavy chain V-III region WEAIg heavy chain V-I region EUIGLV3-22(1-?)IGHV1-2IGKV3D-20Ig heavy chain V-III region DOBIGKV1-5(23-?)IGLV1-40(1-?)Ig heavy chain V-I region HG3IGLV4-69(1-?)IgH heavy chain V-III region VH26 precursorIGLV3-12(1-?)IGLV4-60(1-?)IGLV5-45(1-?)Ig heavy chain V-III region BUTIg heavy chain V-II region WAHIg heavy chain V-III region BROIg lambda chain V-II region MGCIGLV4-3(1-?)Ig lambda chain V-III region SHIGLV1-44(1-?)Ig kappa chain V-I region BANIg heavy chain V-II region MCEIg heavy chain V-III region KOLIg lambda chain V-I region HAAntigenIGLV(23-?)IGKV1-12p-Y160,Y171-CD3GIg lambda chain V-VI region ARIGKV2-28Ig lambda chain V-I region NEWMp-Y288,Y304-FCGR2AIGLV2-18(1-?)IGLC2IGLV10-54(1-?)Ig kappa chain V-II region RPMI 6410Ig heavy chain V-II region WAHIGLV4-69(1-?)IGLV5-45(1-?)IGHG4Ig lambda chain V-II region TOGIg heavy chain V-I region EUIg kappa chain V-I region DaudiIg lambda chain V-III region LOIIg heavy chain V-II region OUIg heavy chain V-I region HG3Ig lambda chain V-IV region KernELMO1Ig lambda chain V-II region MGCAntigenIGLV4-60(1-?)IGLV2-23(1-?)IGLC1IGLV(23-?)IGKV1-12IGKCIgH heavy chain V-III region VH26 precursorIg kappa chain V-I region AUIGHG2p-Y288,Y304-FCGR2AIg heavy chain V-III region BROIg heavy chain V-III region DOBIGLV4-3(1-?)Ig kappa chain V-III region POMCRKIGLV1-44(1-?)Ig heavy chain V-III region JONIg kappa chain V region EV15Ig lambda chain V-VI region ARIGLV5-37(1-?)IGKV2D-30IGLV10-54(1-?)IGLV3-16(1-?)IGLV8-61(1-?)Ig kappa chain V-III region VGIg kappa chain V-I region BANIg kappa chain V-I region AGIGLV2-11(1-?)Ig heavy chain V-II region MCEIGKVA18(21-?)Ig heavy chain V-III region TROIGHV(1-?)Ig lambda chain V-II region NEIIg heavy chain V-III region KOLIGKV1-5(23-?)Ig heavy chain V-II region NEWMIg lambda chain V-I region NEWDOCK1Ig heavy chain V-II region ARH-77Ig lambda chain V-IV region Hilp-6Y-SYKIg lambda chain V-IV region BauIGHV1-2p-6Y-CD247IGLV7-43(1-?)Ig kappa chain V-III region B6Ig heavy chain V-III region CAMIg kappa chain V-II region FRIGLV1-36(1-?)Ig lambda chain V-I region VORIGKV3D-20ELMO2Ig kappa chain V-I region HK101IGLV11-55(1-?)Ig kappa chain V-II region RPMI 6410IGKV2-28Ig lambda chain V region 4AIGLV2-33(1-?)IGLV7-46(1-?)Ig lambda chain V-I region NEWMIGLV2-18(1-?)IGLC2p-Y160,Y171-CD3GIGLC6Ig heavy chain V-III region WEAIg kappa chain V-II region CumIGLV3-12(1-?)IGLC7Ig lambda chain V-I region HAIGLV1-40(1-?)IGHG1Ig lambda chain V-III region SHIGLV3-27(1-?)Ig lambda chain V-II region BOHIg heavy chain V-III region BUTIg kappa chain V-I region GalIGHV7-81(1-?)IGLV3-25(1-?)IGLV3-22(1-?)FCGR3AIGLC3Ig kappa chain V-I region DEEFCGR1AIGHG3IGKV4-1(21-?)Ig kappa chain V-I region WesPLCG1PLCG2ACTB(1-375)ACTG1ATPCYFIP2ARPC5GTPNCK1ACTB(1-375)p-Y291-WASNCKIPSDARPC3ACTR2ABI1WIPF1RAC1NCKAP1p-Y256-WASLp-5S-ABI1WIPF3BAIAP2PI(4,5)P2ARPC1ABRK1p-Y151,S,T-WASF3NCKAP1LPI(3,4,5)P3GRB2-1ATPp-Y150,S343,T346-WASF2WIPF2CDC42p-Y151-WASF3ACTG1ACTR3p-Y151,S,T-WASF1CYFIP1ARPC4ABI2p-Y151-WASF1ARPC1BARPC2p-4S-ABI2F-actinp-Y150-WASF2Ig kappa chain V-I region GalIGLC1Ig heavy chain V-II region MCEIGHV(1-?)IGKV2D-30IGKV2-28IGLV1-44(1-?)Ig kappa chain V-II region RPMI 6410Ig lambda chain V-I region NEWIGLV3-12(1-?)Ig lambda chain V-IV region Baup-6Y-CD247Ig kappa chain V-I region BANIg lambda chain V-IV region HilIGHG4IGHG3IgH heavy chain V-III region VH26 precursorp-Y174-VAV1IGLV2-11(1-?)Ig heavy chain V-I region EUIGKCIg kappa chain V-II region CumIg kappa chain V-III region VGIg kappa chain V-I region DEEIg lambda chain V-III region LOIIg heavy chain V-III region JONIGLV2-18(1-?)Ig kappa chain V-I region WesIGKV1-12AntigenIGLV10-54(1-?)Ig kappa chain V-II region FRFCGR3AIGLC3Ig kappa chain V-I region HK101IGLV5-45(1-?)Ig heavy chain V-II region WAHIg heavy chain V-III region WEAIGLV4-3(1-?)IGLC2IGKV3D-20IGLV3-27(1-?)Ig lambda chain V-II region MGCIg lambda chain V-I region NEWMIg kappa chain V region EV15p-Y173-VAV3Ig kappa chain V-I region DaudiIg heavy chain V-III region BROIGLV5-37(1-?)IGLV3-25(1-?)IGLV7-43(1-?)IGLC7Ig kappa chain V-I region AGIGHV7-81(1-?)Ig lambda chain V-II region TOGIGLV8-61(1-?)IGLV7-46(1-?)IGLV3-22(1-?)Ig lambda chain V-I region HAIGLV2-23(1-?)IGHG1FCGR1AIg lambda chain V-II region NEIIg kappa chain V-III region B6Ig kappa chain V-I region AUIGLV(23-?)IGLV1-40(1-?)IGLV3-16(1-?)Ig heavy chain V-II region OUIGHV1-2Ig heavy chain V-I region HG3Ig heavy chain V-III region DOBp-Y160,Y171-CD3GIg lambda chain V-III region SHp-6Y-SYKIGLV4-60(1-?)IGLV1-36(1-?)Ig heavy chain V-II region NEWMIg lambda chain V-IV region KernIg kappa chain V-III region POMIg heavy chain V-II region ARH-77Ig lambda chain V-VI region ARIGLV4-69(1-?)Ig heavy chain V-III region TROIGLC6IGLV11-55(1-?)Ig heavy chain V-III region BUTIg lambda chain V-II region BOHIg lambda chain V-I region VORIGKVA18(21-?)IGLV2-33(1-?)IGKV4-1(21-?)Ig heavy chain V-III region KOLIg heavy chain V-III region CAMp-Y288,Y304-FCGR2AIg lambda chain V region 4Ap-Y172-VAV2IGKV1-5(23-?)IGHG2p-T202,Y204-MAPK3p-T185,Y187-MAPK1p-T508-LIMK1HSP90AB1HSP90AA1FYNLYNHCKSRC-1YES1FGRRAC1GTPp-Y753,Y759,Y1217-PLCG2p-4Y-PLCG1Ig lambda chain V-I region NEWIg heavy chain V-III region DOBIg kappa chain V-I region HK101Ig heavy chain V-II region NEWMIGHV7-81(1-?)IGLV2-33(1-?)Ig heavy chain V-II region WAHAntigenIg heavy chain V-III region KOLIGLC1IGKVA18(21-?)IGLV2-11(1-?)IGHG2Ig kappa chain V-III region POMIg lambda chain V-IV region BauIg heavy chain V-III region CAMIGLV3-16(1-?)Ig kappa chain V-I region AUIGLV5-37(1-?)Ig heavy chain V-III region JONIg lambda chain V-III region SHIg kappa chain V-I region WesIGLV5-45(1-?)Ig lambda chain V-IV region HilIGLV7-43(1-?)Ig heavy chain V-III region BUTIGHV1-2IGLV8-61(1-?)Ig kappa chain V-I region DEEIGHG1IGLV7-46(1-?)IGLV3-27(1-?)Ig heavy chain V-II region ARH-77Ig heavy chain V-II region MCEIGLV3-22(1-?)IGKV1-5(23-?)IGHG4Ig lambda chain V-I region NEWMIg lambda chain V-IV region KernIGLC3IGLV3-25(1-?)FCGR1AIg kappa chain V-I region AGIGLC7Ig kappa chain V-II region FRIGKV2-28IGLV2-18(1-?)IGLV1-44(1-?)IGLV11-55(1-?)IGKV4-1(21-?)Ig heavy chain V-III region WEAIGLV4-69(1-?)IGLC6Ig kappa chain V-III region B6Ig kappa chain V-II region CumIGKCIGLV4-3(1-?)Ig lambda chain V-II region MGCIg kappa chain V-III region VGIg lambda chain V-VI region ARIGLV4-60(1-?)IGLV(23-?)IGLV1-36(1-?)IgH heavy chain V-III region VH26 precursorIg kappa chain V-I region GalIGKV2D-30Ig heavy chain V-I region HG3Ig lambda chain V-III region LOIIg kappa chain V-II region RPMI 6410Ig lambda chain V region 4AIGLC2Ig heavy chain V-II region OUIg lambda chain V-I region VORIGHV(1-?)Ig lambda chain V-II region NEIIg lambda chain V-II region TOGIGLV3-12(1-?)CD3GIGLV2-23(1-?)Ig kappa chain V-I region BANIGLV1-40(1-?)Ig heavy chain V-I region EUIg lambda chain V-II region BOHIg lambda chain V-I region HAIg kappa chain V-I region DaudiIg kappa chain V region EV15Ig heavy chain V-III region BROIGKV1-12IGLV10-54(1-?)IGKV3D-20IGHG3Ig heavy chain V-III region TROIg heavy chain V-I region HG3Ig heavy chain V-III region JONIg kappa chain V-III region POMIg lambda chain V-I region VORIg lambda chain V-III region LOIIGLV2-33(1-?)Ig heavy chain V-II region NEWMIGLV1-40(1-?)IGKV1-5(23-?)Ig lambda chain V-IV region BauIGLC3IGHG2IGLC6Ig lambda chain V-II region TOGIg heavy chain V-II region WAHIg lambda chain V-III region SHIg kappa chain V-I region DaudiIg heavy chain V-III region BROIg heavy chain V-III region DOBIg heavy chain V-III region WEAIGKCIg heavy chain V-III region KOLFCGR1AIg lambda chain V-VI region ARIg lambda chain V-II region NEIIg lambda chain V-I region NEWIg lambda chain V-I region NEWMIGLV3-27(1-?)IGHV7-81(1-?)Ig heavy chain V-II region ARH-77IGLV5-37(1-?)IGLV2-11(1-?)IGLC7IGLV11-55(1-?)Ig kappa chain V-I region AGIGLV8-61(1-?)IGLV3-22(1-?)IGLV4-69(1-?)IGLV2-18(1-?)IGLV5-45(1-?)Ig lambda chain V-II region MGCIg lambda chain V-IV region HilIg kappa chain V-I region DEEIg kappa chain V-II region RPMI 6410IGKV4-1(21-?)p-6Y-CD247IGLV7-43(1-?)IGLV7-46(1-?)IGHG4IGKVA18(21-?)IGHV(1-?)IGKV2D-30IGLV4-3(1-?)IGLV3-12(1-?)IGLV3-16(1-?)Ig lambda chain V-II region BOHIg kappa chain V-III region VGIg lambda chain V region 4AIg kappa chain V region EV15IGHG3IGLV2-23(1-?)AntigenIGLV3-25(1-?)Ig kappa chain V-III region B6Ig heavy chain V-III region BUTIGLC2Ig lambda chain V-I region HAp-6Y-SYKIg kappa chain V-I region HK101IGLV10-54(1-?)Ig kappa chain V-I region GalIg lambda chain V-IV region KernIGLC1IgH heavy chain V-III region VH26 precursorIGLV(23-?)IGKV3D-20IGLV4-60(1-?)Ig heavy chain V-II region OUp-Y288,Y304-FCGR2AIGHG1Ig heavy chain V-II region MCEIg kappa chain V-I region WesIg heavy chain V-III region TROIg kappa chain V-II region CumIg kappa chain V-I region AUIg kappa chain V-I region BANIGHV1-2FCGR3Ap-Y160,Y171-CD3GIGLV1-44(1-?)Ig heavy chain V-III region CAMIg heavy chain V-I region EUIGLV1-36(1-?)IGKV2-28Ig kappa chain V-II region FRIGKV1-12CYFIP1CYFIP2BRK1ABI2NCKAP1ABI1WASF1NCKAP1LWASF3WASF2MYO9BMYO5AMYH9MYO1CMYH2PRKCDPRKCEIGLV2-18(1-?)Ig lambda chain V-I region HAIg kappa chain V-I region GalIg lambda chain V-III region LOIIg kappa chain V-I region DaudiIGLV11-55(1-?)IGKV2-28Ig lambda chain V-IV region BauFCGR1AIg lambda chain V-II region BOHIGLV5-45(1-?)Ig lambda chain V-II region NEIIg heavy chain V-II region MCEIGKV1-12Ig lambda chain V-III region SHIGLV1-44(1-?)Ig lambda chain V-IV region KernIGKV3D-20IGLC3Ig kappa chain V-II region CumIGLC2Ig kappa chain V-II region FRIg kappa chain V-I region HK101IgH heavy chain V-III region VH26 precursorIg heavy chain V-III region CAMIg heavy chain V-III region DOBIGHG4Ig heavy chain V-III region WEAIg kappa chain V region EV15p-Y160,Y171-CD3GIGHV7-81(1-?)PLCG1IGLV4-60(1-?)Ig kappa chain V-I region BANIGLV2-11(1-?)IGHG1IGLV5-37(1-?)IGLV3-12(1-?)Ig kappa chain V-II region RPMI 6410Ig heavy chain V-III region JONIGKV1-5(23-?)IGLC1IGHV1-2IGKVA18(21-?)Ig heavy chain V-III region KOLIGLV2-33(1-?)Ig lambda chain V-II region TOGPLCG2IGHV(1-?)Ig heavy chain V-III region BROIGLV3-25(1-?)Ig kappa chain V-III region B6Ig lambda chain V-I region VORIg lambda chain V region 4AIg kappa chain V-I region DEEIg heavy chain V-I region EUIGLV1-36(1-?)Ig kappa chain V-I region AUIg kappa chain V-III region POMIGLV1-40(1-?)IGKV4-1(21-?)IGLV3-16(1-?)Ig heavy chain V-II region NEWMIg kappa chain V-I region AGp-6Y-SYKIGKCIGKV2D-30IGLV10-54(1-?)Ig heavy chain V-III region BUTIg heavy chain V-I region HG3IGLV7-43(1-?)p-Y288,Y304-FCGR2AIg lambda chain V-II region MGCIGLV3-22(1-?)IGLV2-23(1-?)IGLV3-27(1-?)FCGR3AIGHG2IGHG3Ig heavy chain V-II region OUIGLV(23-?)Ig kappa chain V-I region WesIGLC6p-6Y-CD247Ig kappa chain V-III region VGIg heavy chain V-III region TROIGLV7-46(1-?)Ig lambda chain V-VI region ARIg lambda chain V-I region NEWIg heavy chain V-II region ARH-77Ig lambda chain V-IV region HilIGLV8-61(1-?)Ig heavy chain V-II region WAHIGLV4-3(1-?)IGLV4-69(1-?)Ig lambda chain V-I region NEWMAntigenIGLC7GTPCDC42PAK1RAC1HSP90AB1HSP90AA1p-T566,T710,S729-PRKCEp-T507,S645,S664-PRKCD(1-676)ACTR3ARPC3ATPARPC4ARPC5ACTR2ARPC2ARPC1BARPC1ARAC1CYFIP1CYFIP2WASF2BRK1BAIAP2NCKAP1LABI1PI(3,4,5)P3GTPABI2WASF3WASF1NCKAP1VAV1VAV2VAV3GRB2-1NCK1WIPF3p-Y151,S,T-WASF1p-Y291-WASACTR2p-Y151-WASF1PI(4,5)P2p-Y256-WASLARPC1BBRK1CYFIP2p-4S-ABI2WIPF2ARPC3p-Y150,S343,T346-WASF2ATPABI2ARPC1ARAC1ARPC5PI(3,4,5)P3p-Y151,S,T-WASF3ARPC2ACTR3BAIAP2ACTG1ACTB(1-375)p-Y150-WASF2WIPF1p-Y151-WASF3NCKAP1LNCKIPSDp-5S-ABI1CYFIP1ABI1ARPC4NCKAP1CDC42GTPIg heavy chain V-III region BUTIg heavy chain V-II region MCEIg lambda chain V-II region MGCIGLV2-18(1-?)Ig heavy chain V-II region WAHIg lambda chain V region 4AIGLV3-22(1-?)IGLV3-27(1-?)AntigenIGLV2-33(1-?)Ig kappa chain V-I region GalIg heavy chain V-III region KOLIGKV1-5(23-?)Ig kappa chain V-III region B6FCGR1AIg heavy chain V-II region NEWMIGLV2-11(1-?)Ig lambda chain V-IV region KernIGLC1IGLV10-54(1-?)Ig lambda chain V-III region SHIg lambda chain V-IV region HilIGHV7-81(1-?)Ig kappa chain V-I region WesIGKVA18(21-?)p-6Y-CD247Ig lambda chain V-III region LOIIGLV1-40(1-?)Ig heavy chain V-III region WEAIGLV5-45(1-?)IGLV7-46(1-?)Ig lambda chain V-IV region BauIg kappa chain V-II region RPMI 6410Ig kappa chain V-III region VGIGLC7Ig lambda chain V-II region TOGIg heavy chain V-III region DOBIGLV4-69(1-?)IGLV11-55(1-?)IGLV1-36(1-?)Ig heavy chain V-I region EUIGKV2-28IGLV3-16(1-?)Ig heavy chain V-III region CAMIGLV1-44(1-?)Ig heavy chain V-II region OUIGHG1IGHG4p-Y288,Y304-FCGR2AIg heavy chain V-I region HG3Ig lambda chain V-I region NEWIGLC3Ig kappa chain V-I region HK101Ig kappa chain V-III region POMIGHV(1-?)IgH heavy chain V-III region VH26 precursorIGLV3-25(1-?)IGHG3IGLV3-12(1-?)Ig kappa chain V-II region CumIGLC6Ig kappa chain V-I region BANIg heavy chain V-III region BROIGLV7-43(1-?)IGLV5-37(1-?)IGHV1-2Ig kappa chain V region EV15Ig kappa chain V-I region AGIg kappa chain V-II region FRIg kappa chain V-I region DEEIGKCIg kappa chain V-I region DaudiIGLV4-3(1-?)FCGR3AIg lambda chain V-I region HAIg lambda chain V-II region NEIIg kappa chain V-I region AUIGKV1-12IGLV2-23(1-?)Ig heavy chain V-III region JONIGKV3D-20Ig lambda chain V-II region BOHIGKV4-1(21-?)IGLV4-60(1-?)Ig lambda chain V-I region NEWMIGLV(23-?)Ig heavy chain V-II region ARH-77IGLV8-61(1-?)Ig lambda chain V-VI region ARIg heavy chain V-III region TROIGHG2Ig lambda chain V-I region VORp-Y160,Y171-CD3GIGKV2D-30IGLC2IGLV1-44(1-?)Ig lambda chain V region 4AIg lambda chain V-II region NEIIg lambda chain V-I region NEWMIg heavy chain V-II region MCEIg kappa chain V-I region AUIGHV1-2Ig heavy chain V-II region ARH-77Ig lambda chain V-IV region BauIGLC7Ig heavy chain V-III region BROIGHV(1-?)Ig heavy chain V-III region DOBIGKV2D-30IGLV10-54(1-?)IGKV4-1(21-?)IGLV2-23(1-?)CD3GIGLV5-37(1-?)IGLV3-16(1-?)Ig heavy chain V-III region JONIg heavy chain V-II region WAHIGLV3-27(1-?)Ig kappa chain V-I region WesIGLV4-60(1-?)CD247-1IGLV5-45(1-?)IGKVA18(21-?)IGLV2-33(1-?)IGLV3-25(1-?)IGLC1Ig heavy chain V-III region TROIGLC6Ig lambda chain V-IV region KernIg lambda chain V-II region MGCIg kappa chain V-III region B6IGLV2-11(1-?)IGLV2-18(1-?)IGLV3-12(1-?)Ig lambda chain V-I region NEWFCGR3AIg heavy chain V-III region KOLIGHG3IGKCIGKV1-5(23-?)Ig heavy chain V-II region NEWMIg heavy chain V-II region OUIg kappa chain V-III region POMIg lambda chain V-VI region ARIg kappa chain V-III region VGIGLV1-40(1-?)Ig heavy chain V-III region WEAIGHV7-81(1-?)Ig lambda chain V-II region BOHIg kappa chain V-I region GalIGLV4-3(1-?)Ig kappa chain V region EV15Ig lambda chain V-II region TOGIGHG4Ig kappa chain V-I region AGIGLV7-46(1-?)Ig kappa chain V-I region HK101Ig kappa chain V-II region FRIGLV11-55(1-?)Ig kappa chain V-I region DEEIg kappa chain V-I region DaudiIg lambda chain V-III region LOIIGLV7-43(1-?)AntigenIg lambda chain V-I region HAIGKV2-28IGHG1IGLV(23-?)IGKV3D-20IGLC3Ig heavy chain V-I region EUIg lambda chain V-I region VORIg lambda chain V-IV region HilIGLV4-69(1-?)Ig heavy chain V-III region CAMIGLV8-61(1-?)IGKV1-12Ig kappa chain V-II region CumIg heavy chain V-I region HG3IgH heavy chain V-III region VH26 precursorIg heavy chain V-III region BUTIg kappa chain V-II region RPMI 6410IGHG2IGLV1-36(1-?)Ig kappa chain V-I region BANIGLV3-22(1-?)IGLC2Ig lambda chain V-III region SHGTPCDC42RAC1WIPF3WIPF2WIPF1CDC42GDPIGHG3IGKV2-28Ig kappa chain V-I region GalIGLV8-61(1-?)Ig heavy chain V-I region EUIg heavy chain V-II region WAHIGKV1-5(23-?)Ig heavy chain V-III region JONIGLC2Ig kappa chain V-I region HK101IGLV2-18(1-?)IGLC1IGLV1-44(1-?)Ig lambda chain V-II region BOHIGHG2Ig lambda chain V-II region TOGp-Y288,Y304-FCGR2API(3,4,5)P3Ig heavy chain V-III region KOLIGLC7IGLC6IGLV7-46(1-?)IGLV10-54(1-?)IGHV1-2Ig lambda chain V-IV region BauIg lambda chain V-II region MGCIg lambda chain V-VI region ARIGLV3-22(1-?)Ig lambda chain V region 4Ap-6Y-SYKIGKVA18(21-?)IGLV2-33(1-?)Ig heavy chain V-II region MCEIg kappa chain V-I region AGIg heavy chain V-III region BROIGHV7-81(1-?)Ig heavy chain V-III region TROIGLV3-27(1-?)IGLV5-37(1-?)Ig kappa chain V-I region DaudiIg heavy chain V-III region BUTIg lambda chain V-I region VORIg lambda chain V-IV region KernIGLV4-69(1-?)IGKV1-12Ig heavy chain V-III region WEAIg kappa chain V-II region CumIGKCIg heavy chain V-III region CAMIGHG1IGHV(1-?)IGLV1-40(1-?)IGLV3-12(1-?)Ig lambda chain V-III region LOIIg kappa chain V-I region DEEIg lambda chain V-I region HAIg kappa chain V-III region B6p-Y160,Y171-CD3GIg kappa chain V-III region VGIg lambda chain V-II region NEIIg lambda chain V-I region NEWMIg kappa chain V region EV15Ig kappa chain V-III region POMIGLV11-55(1-?)IGLV4-60(1-?)FCGR3AIGLV2-23(1-?)IGLV3-16(1-?)Ig heavy chain V-II region ARH-77Ig lambda chain V-I region NEWp-4Y-PLCG1Ig heavy chain V-II region OUIg heavy chain V-II region NEWMIg kappa chain V-II region FRIGKV4-1(21-?)Ig lambda chain V-III region SHIg kappa chain V-II region RPMI 6410IGLC3Ig kappa chain V-I region WesIGLV(23-?)IGKV2D-30IGLV5-45(1-?)AntigenIg heavy chain V-III region DOBp-6Y-CD247IGLV2-11(1-?)IGLV7-43(1-?)IGLV3-25(1-?)Ig kappa chain V-I region BANIGHG4IGLV1-36(1-?)Ig lambda chain V-IV region HilIGKV3D-20FCGR1AIGLV4-3(1-?)Ig heavy chain V-I region HG3p-Y753,Y759,Y1217-PLCG2IgH heavy chain V-III region VH26 precursorIg kappa chain V-I region AURAC1GDPIGLV3-27(1-?)IGLC7IGLC1Ig heavy chain V-III region KOLIGLV3-12(1-?)IGLV2-23(1-?)IGLV4-69(1-?)FCGR1AIg kappa chain V-III region VGIg lambda chain V region 4AIGLV5-37(1-?)IGLV3-25(1-?)Ig kappa chain V-I region GalIg heavy chain V-III region CAMIg kappa chain V-III region B6Ig lambda chain V-II region NEIAntigenIg lambda chain V-I region NEWIg lambda chain V-VI region ARIg heavy chain V-II region NEWMIGLC6Ig kappa chain V-I region DEEIg lambda chain V-I region NEWMIGLV10-54(1-?)Ig heavy chain V-I region HG3IGHG2Ig heavy chain V-III region WEAIg heavy chain V-III region BUTIg lambda chain V-III region SHIg heavy chain V-II region WAHIg lambda chain V-IV region HilIGLV4-3(1-?)Ig lambda chain V-I region VORIg lambda chain V-II region MGCIGKV3D-20IGHG4IGLV3-16(1-?)Ig kappa chain V-I region Daudip-6Y-CD247Ig kappa chain V-I region HK101Ig kappa chain V-I region AGIGLV7-43(1-?)IGKV1-12IGKV2-28IGKV2D-30IGLV2-33(1-?)IGKCIg heavy chain V-III region BROIg heavy chain V-II region ARH-77Ig kappa chain V region EV15IGHV7-81(1-?)p-Y160,Y171-CD3GIg kappa chain V-I region AUIGLV2-18(1-?)Ig lambda chain V-II region TOGIGKV4-1(21-?)IGLV1-44(1-?)Ig lambda chain V-IV region BauIg lambda chain V-IV region KernIg lambda chain V-I region HAIGKV1-5(23-?)IGHG1Ig heavy chain V-II region MCEIg kappa chain V-II region RPMI 6410FCGR3AIg kappa chain V-III region POMIg kappa chain V-II region CumIGHG3IGLV(23-?)Ig heavy chain V-III region TROIGLV4-60(1-?)IGHV(1-?)IGLC2IGLV5-45(1-?)IGHV1-2Ig kappa chain V-II region FRIGLV2-11(1-?)IGLV3-22(1-?)IGLV1-40(1-?)Ig kappa chain V-I region WesIg heavy chain V-I region EUIg lambda chain V-II region BOHIg kappa chain V-I region BANp-Y288,Y304-FCGR2AIGLV1-36(1-?)Ig heavy chain V-III region JONIGLV7-46(1-?)Ig lambda chain V-III region LOIIGKVA18(21-?)IGLC3IGLV8-61(1-?)IGLV11-55(1-?)Ig heavy chain V-III region DOBIgH heavy chain V-III region VH26 precursorIg heavy chain V-II region OUARPC1AARPC4ACTR2ARPC2ARPC1BACTG1ARPC3ACTB(1-375)ACTR3ARPC5ADPATPF-actinName: Fcgamma receptor (FCGR) dependent phagocytosisOrganism: Homo sapiens


Description

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

Comments

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

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Bibliography

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

History

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

External references

DataNodes

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

complex recruited

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

filament:branching complex:daughter

filament		ComplexR-HSA-1861699 (Reactome)
Mother

filament:branching

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

N-WASP:ARP2/3

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

Annotated Interactions

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

complex recruited

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

complex recruited

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

filament:branching complex:daughter

filament		ArrowR-HSA-2029473 (Reactome)
Mother

filament:branching complex:daughter

filament		R-HSA-1861595 (Reactome)
Mother

filament:branching complex:daughter

filament		R-HSA-2029476 (Reactome)
Mother

filament:branching

complex		ArrowR-HSA-2029466 (Reactome)
Mother

filament:branching

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

N-WASP:ARP2/3

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

N-WASP:ARP2/3

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