Fcgamma receptor (FCGR) dependent phagocytosis (Homo sapiens)

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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

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Compare	Revision	Action	Time	User	Comment
	118475	view	20:32, 27 May 2021	Finterly	Removed incorrect and duplicated openControlledVocabulary PW:0000234
	114947	view	16:47, 25 January 2021	ReactomeTeam	Reactome version 75
	113391	view	11:46, 2 November 2020	ReactomeTeam	Reactome version 74
	112853	view	13:31, 12 October 2020	DeSl	Fixing ontology tag error
	112849	view	13:02, 12 October 2020	DeSl	Ontology Term : 'innate immune response pathway' added !
	112596	view	15:57, 9 October 2020	ReactomeTeam	Reactome version 73
	101512	view	11:37, 1 November 2018	ReactomeTeam	reactome version 66
	101048	view	21:19, 31 October 2018	ReactomeTeam	reactome version 65
	100579	view	19:52, 31 October 2018	ReactomeTeam	reactome version 64
	100128	view	16:38, 31 October 2018	ReactomeTeam	reactome version 63
	99678	view	15:07, 31 October 2018	ReactomeTeam	reactome version 62 (2nd attempt)
	99271	view	12:45, 31 October 2018	ReactomeTeam	reactome version 62
	94053	view	13:54, 16 August 2017	ReactomeTeam	reactome version 61
	93681	view	11:30, 9 August 2017	ReactomeTeam	reactome version 61
	89466	view	13:21, 15 September 2016	Mkutmon	fix ontology tag annotation
	87448	view	13:50, 22 July 2016	Mkutmon	Ontology Term : 'PW:0000234' added !
	86805	view	09:26, 11 July 2016	ReactomeTeam	reactome version 56
	83122	view	10:02, 18 November 2015	ReactomeTeam	Version54
	81461	view	12:59, 21 August 2015	ReactomeTeam	Version53
	76936	view	08:20, 17 July 2014	ReactomeTeam	Fixed remaining interactions
	76641	view	12:01, 16 July 2014	ReactomeTeam	Fixed remaining interactions
	75971	view	10:02, 11 June 2014	ReactomeTeam	Re-fixing comment source
	75674	view	10:59, 10 June 2014	ReactomeTeam	Reactome 48 Update
	75029	view	13:54, 8 May 2014	Anwesha	Fixing comment source for displaying WikiPathways description
	74673	view	08:44, 30 April 2014	ReactomeTeam	New pathway

External references

DataNodes

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Name	Type	Database reference	Comment
2-Lysophosphatidylcholine	Metabolite	CHEBI:17504 (ChEBI)
ABL1	Protein	P00519 (Uniprot-TrEMBL)
ACTB(1-375) [cytosol]	Protein	P60709 (Uniprot-TrEMBL)
ACTG1(1-375) [cytosol]	Protein	P63261 (Uniprot-TrEMBL)
ACTR2 [cytosol]	Protein	P61160 (Uniprot-TrEMBL)
ACTR3 [cytosol]	Protein	P61158 (Uniprot-TrEMBL)
ADP [cytosol]	Metabolite	CHEBI:16761 (ChEBI)
ADP	Metabolite	CHEBI:16761 (ChEBI)
ARP2/3 complex (ATP bound)	Complex	REACT_160979 (Reactome)
ARPC1A [cytosol]	Protein	Q92747 (Uniprot-TrEMBL)
ARPC2 [cytosol]	Protein	O15144 (Uniprot-TrEMBL)
ARPC3 [cytosol]	Protein	O15145 (Uniprot-TrEMBL)
ARPC4 [cytosol]	Protein	P59998 (Uniprot-TrEMBL)
ARPC5 [cytosol]	Protein	O15511 (Uniprot-TrEMBL)
ATP [cytosol]	Metabolite	CHEBI:15422 (ChEBI)
ATP	Metabolite	CHEBI:15422 (ChEBI)
Actin filament bound Myosin-X	Complex	REACT_161386 (Reactome)
Actin:ADP	Complex	REACT_148188 (Reactome)
Activated WAVE2 and WASP/N-WASP:ARP2/3 complex:G-actin	Complex	REACT_160776 (Reactome)
Activated WAVE2 and WASP/N-WASP	Complex	REACT_160331 (Reactome)
Active LIMK1	Complex	REACT_19790 (Reactome)
Active RAC1/CDC42	Complex	REACT_20094 (Reactome)
Antigen-antibody complex	Complex	REACT_8124 (Reactome)
Arachidonic acid	Metabolite	CHEBI:15843 (ChEBI)
BAIAP2 [cytosol]	Protein	Q9UQB8 (Uniprot-TrEMBL)
BAIAP2	Protein	Q9UQB8 (Uniprot-TrEMBL)
BRK1(2-75) [cytosol]	Protein	Q8WUW1 (Uniprot-TrEMBL)
CD247-1 [plasma membrane]	Protein	P20963-1 (Uniprot-TrEMBL)
CD3G [plasma membrane]	Protein	P09693 (Uniprot-TrEMBL)
CDC42 [cytosol]	Protein	P60953 (Uniprot-TrEMBL)
CDC42-GDP	Complex	REACT_20401 (Reactome)
CDC42-GTP:WASP/N-WASP:WIP:SH3 proteins	Complex	REACT_160812 (Reactome)
CDC42-GTP:WASP/N-WASP	Complex	REACT_160830 (Reactome)
CDC42-GTP:p-WASP/p-N-WASP:WIP:SH3 proteins	Complex	REACT_161223 (Reactome)
CDC42:GTP	Complex	REACT_12889 (Reactome)
CFL1	Protein	P23528 (Uniprot-TrEMBL)
CRK(2-304) [cytosol]	Protein	P46108 (Uniprot-TrEMBL)
CRK:DOCK180:ELMO	Complex	REACT_160373 (Reactome)
CRKII:DOCK180:ELMO complex recruited to phagocytic cup	Complex	REACT_161310 (Reactome)
CYFIP2 [cytosol]	Protein	Q96F07 (Uniprot-TrEMBL)
Ca2+	Metabolite	CHEBI:29108 (ChEBI)
DAGs	Metabolite	CHEBI:18035 (ChEBI)
DOCK1 [cytosol]	Protein	Q14185 (Uniprot-TrEMBL)
ELMO1 [cytosol]	Protein	Q92556 (Uniprot-TrEMBL)
ELMO2 [cytosol]	Protein	Q96JJ3 (Uniprot-TrEMBL)
ERK	Protein	REACT_24485 (Reactome)
F-actin		REACT_20433 (Reactome)
FCGR1A [plasma membrane]	Protein	P12314 (Uniprot-TrEMBL)
FCGR2A [plasma membrane]	Protein	P12318 (Uniprot-TrEMBL)
FCGR2A	Protein	P12318 (Uniprot-TrEMBL)
FCGR3A [plasma membrane]	Protein	P08637 (Uniprot-TrEMBL)
FCGRIA:CD3G homodimer	Complex	REACT_161114 (Reactome)
FCGRIIIA:CD3G/CD3Z dimers	Complex	REACT_161118 (Reactome)
G-actin	Complex	REACT_19528 (Reactome)
GDP [cytosol]	Metabolite	CHEBI:17552 (ChEBI)
GDP	Metabolite	CHEBI:17552 (ChEBI)
GRB2-1 [cytosol]	Protein	P62993-1 (Uniprot-TrEMBL)
GTP [cytosol]	Metabolite	CHEBI:15996 (ChEBI)
GTP	Metabolite	CHEBI:15996 (ChEBI)
H2O	Metabolite	CHEBI:15377 (ChEBI)
HSP-90		REACT_19960 (Reactome)
HSP90AA1 [cytosol]	Protein	P07900 (Uniprot-TrEMBL)
HSP90AB1 [cytosol]	Protein	P08238 (Uniprot-TrEMBL)
I(1,4,5)P3 [cytosol]	Metabolite	CHEBI:16595 (ChEBI)
I(1,4,5)P3	Metabolite	CHEBI:16595 (ChEBI)
IGHG1(1-330) [extracellular region]	Protein	P01857 (Uniprot-TrEMBL)
IGHG2(1-326) [extracellular region]	Protein	P01859 (Uniprot-TrEMBL)
IGHG3 [extracellular region]	Protein	P01860 (Uniprot-TrEMBL)
IGHG4(1-327) [extracellular region]	Protein	P01861 (Uniprot-TrEMBL)
IGHV(1-?) [extracellular region]	Protein	A2KUC3 (Uniprot-TrEMBL)
IGHV7-81(1-?) [extracellular region]	Protein	Q6PIL0 (Uniprot-TrEMBL)
IGKC(1-106) [extracellular region]	Protein	P01834 (Uniprot-TrEMBL)
IGKV1-5(23-?) [extracellular region]	Protein	P01602 (Uniprot-TrEMBL)
IGKV4-1(21-?) [extracellular region]	Protein	P06312 (Uniprot-TrEMBL)
IGKVA18(21-?) [extracellular region]	Protein	A2NJV5 (Uniprot-TrEMBL)
IGLC1(1-105) [extracellular region]	Protein	P0CG04 (Uniprot-TrEMBL)
IGLC2(?-106) [extracellular region]	Protein	P0CG05 (Uniprot-TrEMBL)
IGLC3(?-106) [extracellular region]	Protein	P0CG06 (Uniprot-TrEMBL)
IGLC6(?-106) [extracellular region]	Protein	P0CF74 (Uniprot-TrEMBL)
IGLC7(?-106) [extracellular region]	Protein	A0M8Q6 (Uniprot-TrEMBL)
IGLV(23-?) [extracellular region]	Protein	A2NXD2 (Uniprot-TrEMBL)
IGLV1-36(1-?) [extracellular region]	Protein	Q5NV67 (Uniprot-TrEMBL)
IGLV1-40(1-?) [extracellular region]	Protein	Q5NV69 (Uniprot-TrEMBL)
IGLV1-44(1-?) [extracellular region]	Protein	Q5NV81 (Uniprot-TrEMBL)
IGLV10-54(1-?) [extracellular region]	Protein	Q5NV86 (Uniprot-TrEMBL)
IGLV11-55(1-?) [extracellular region]	Protein	Q5NV87 (Uniprot-TrEMBL)
IGLV2-11(1-?) [extracellular region]	Protein	Q5NV84 (Uniprot-TrEMBL)
IGLV2-18(1-?) [extracellular region]	Protein	Q5NV65 (Uniprot-TrEMBL)
IGLV2-23(1-?) [extracellular region]	Protein	Q5NV89 (Uniprot-TrEMBL)
IGLV2-33(1-?) [extracellular region]	Protein	Q5NV66 (Uniprot-TrEMBL)
IGLV3-12(1-?) [extracellular region]	Protein	Q5NV85 (Uniprot-TrEMBL)
IGLV3-16(1-?) [extracellular region]	Protein	Q5NV64 (Uniprot-TrEMBL)
IGLV3-22(1-?) [extracellular region]	Protein	Q5NV75 (Uniprot-TrEMBL)
IGLV3-25(1-?) [extracellular region]	Protein	Q5NV90 (Uniprot-TrEMBL)
IGLV3-27(1-?) [extracellular region]	Protein	Q5NV91 (Uniprot-TrEMBL)
IGLV4-3(1-?) [extracellular region]	Protein	Q5NV61 (Uniprot-TrEMBL)
IGLV4-60(1-?) [extracellular region]	Protein	Q5NV79 (Uniprot-TrEMBL)
IGLV4-69(1-?) [extracellular region]	Protein	Q5NV92 (Uniprot-TrEMBL)
IGLV5-37(1-?) [extracellular region]	Protein	Q5NV68 (Uniprot-TrEMBL)
IGLV5-45(1-?) [extracellular region]	Protein	Q5NV82 (Uniprot-TrEMBL)
IGLV7-43(1-?) [extracellular region]	Protein	Q5NV80 (Uniprot-TrEMBL)
IGLV7-46(1-?) [extracellular region]	Protein	Q5NV83 (Uniprot-TrEMBL)
IGLV8-61(1-?) [extracellular region]	Protein	Q5NV62 (Uniprot-TrEMBL)
IP3 receptor homotetramer	Complex	REACT_12247 (Reactome)
IP3 receptor:IP3 complex	Complex	REACT_12249 (Reactome)
ITPR1 [endoplasmic reticulum membrane]	Protein	Q14643 (Uniprot-TrEMBL)
ITPR2 [endoplasmic reticulum membrane]	Protein	Q14571 (Uniprot-TrEMBL)
ITPR3 [endoplasmic reticulum membrane]	Protein	Q14573 (Uniprot-TrEMBL)
Ig heavy chain V-I region EU [extracellular region]	Protein	P01742 (Uniprot-TrEMBL)
Ig heavy chain V-I region HG3 [extracellular region]	Protein	P01743 (Uniprot-TrEMBL)
Ig heavy chain V-I region Mot [extracellular region]	Protein	P06326 (Uniprot-TrEMBL)
Ig heavy chain V-I region ND [extracellular region]	Protein	P01744 (Uniprot-TrEMBL)
Ig heavy chain V-I region SIE [extracellular region]	Protein	P01761 (Uniprot-TrEMBL)
Ig heavy chain V-I region WOL [extracellular region]	Protein	P01760 (Uniprot-TrEMBL)
Ig heavy chain V-II region ARH-77 [extracellular region]	Protein	P06331 (Uniprot-TrEMBL)
Ig heavy chain V-II region COR [extracellular region]	Protein	P01815 (Uniprot-TrEMBL)
Ig heavy chain V-II region DAW [extracellular region]	Protein	P01816 (Uniprot-TrEMBL)
Ig heavy chain V-II region HE [extracellular region]	Protein	P01818 (Uniprot-TrEMBL)
Ig heavy chain V-II region MCE [extracellular region]	Protein	P01817 (Uniprot-TrEMBL)
Ig heavy chain V-II region NEWM [extracellular region]	Protein	P01825 (Uniprot-TrEMBL)
Ig heavy chain V-II region OU [extracellular region]	Protein	P01814 (Uniprot-TrEMBL)
Ig heavy chain V-II region SESS [extracellular region]	Protein	P04438 (Uniprot-TrEMBL)
Ig heavy chain V-II region WAH [extracellular region]	Protein	P01824 (Uniprot-TrEMBL)
Ig heavy chain V-III region BRO [extracellular region]	Protein	P01766 (Uniprot-TrEMBL)
Ig heavy chain V-III region BUR [extracellular region]	Protein	P01773 (Uniprot-TrEMBL)
Ig heavy chain V-III region BUT [extracellular region]	Protein	P01767 (Uniprot-TrEMBL)
Ig heavy chain V-III region CAM [extracellular region]	Protein	P01768 (Uniprot-TrEMBL)
Ig heavy chain V-III region DOB [extracellular region]	Protein	P01782 (Uniprot-TrEMBL)
Ig heavy chain V-III region GA [extracellular region]	Protein	P01769 (Uniprot-TrEMBL)
Ig heavy chain V-III region GAL [extracellular region]	Protein	P01781 (Uniprot-TrEMBL)
Ig heavy chain V-III region HIL [extracellular region]	Protein	P01771 (Uniprot-TrEMBL)
Ig heavy chain V-III region JON [extracellular region]	Protein	P01780 (Uniprot-TrEMBL)
Ig heavy chain V-III region KOL [extracellular region]	Protein	P01772 (Uniprot-TrEMBL)
Ig heavy chain V-III region LAY [extracellular region]	Protein	P01775 (Uniprot-TrEMBL)
Ig heavy chain V-III region NIE [extracellular region]	Protein	P01770 (Uniprot-TrEMBL)
Ig heavy chain V-III region POM [extracellular region]	Protein	P01774 (Uniprot-TrEMBL)
Ig heavy chain V-III region TEI [extracellular region]	Protein	P01777 (Uniprot-TrEMBL)
Ig heavy chain V-III region TIL [extracellular region]	Protein	P01765 (Uniprot-TrEMBL)
Ig heavy chain V-III region TRO [extracellular region]	Protein	P01762 (Uniprot-TrEMBL)
Ig heavy chain V-III region TUR [extracellular region]	Protein	P01779 (Uniprot-TrEMBL)
Ig heavy chain V-III region WAS [extracellular region]	Protein	P01776 (Uniprot-TrEMBL)
Ig heavy chain V-III region WEA [extracellular region]	Protein	P01763 (Uniprot-TrEMBL)
Ig heavy chain V-III region ZAP [extracellular region]	Protein	P01778 (Uniprot-TrEMBL)
Ig kappa chain V region EV15 [extracellular region]	Protein	P06315 (Uniprot-TrEMBL)
Ig kappa chain V-I region AG [extracellular region]	Protein	P01593 (Uniprot-TrEMBL)
Ig kappa chain V-I region AU [extracellular region]	Protein	P01594 (Uniprot-TrEMBL)
Ig kappa chain V-I region BAN [extracellular region]	Protein	P04430 (Uniprot-TrEMBL)
Ig kappa chain V-I region Bi [extracellular region]	Protein	P01595 (Uniprot-TrEMBL)
Ig kappa chain V-I region CAR [extracellular region]	Protein	P01596 (Uniprot-TrEMBL)
Ig kappa chain V-I region DEE [extracellular region]	Protein	P01597 (Uniprot-TrEMBL)
Ig kappa chain V-I region Daudi [extracellular region]	Protein	P04432 (Uniprot-TrEMBL)
Ig kappa chain V-I region EU [extracellular region]	Protein	P01598 (Uniprot-TrEMBL)
Ig kappa chain V-I region Gal [extracellular region]	Protein	P01599 (Uniprot-TrEMBL)
Ig kappa chain V-I region HK101 [extracellular region]	Protein	P01601 (Uniprot-TrEMBL)
Ig kappa chain V-I region Hau [extracellular region]	Protein	P01600 (Uniprot-TrEMBL)
Ig kappa chain V-I region Ka [extracellular region]	Protein	P01603 (Uniprot-TrEMBL)
Ig kappa chain V-I region Kue [extracellular region]	Protein	P01604 (Uniprot-TrEMBL)
Ig kappa chain V-I region Lay [extracellular region]	Protein	P01605 (Uniprot-TrEMBL)
Ig kappa chain V-I region Mev [extracellular region]	Protein	P01612 (Uniprot-TrEMBL)
Ig kappa chain V-I region Ni [extracellular region]	Protein	P01613 (Uniprot-TrEMBL)
Ig kappa chain V-I region OU [extracellular region]	Protein	P01606 (Uniprot-TrEMBL)
Ig kappa chain V-I region Rei [extracellular region]	Protein	P01607 (Uniprot-TrEMBL)
Ig kappa chain V-I region Roy [extracellular region]	Protein	P01608 (Uniprot-TrEMBL)
Ig kappa chain V-I region Scw [extracellular region]	Protein	P01609 (Uniprot-TrEMBL)
Ig kappa chain V-I region WAT [extracellular region]	Protein	P80362 (Uniprot-TrEMBL)
Ig kappa chain V-I region WEA [extracellular region]	Protein	P01610 (Uniprot-TrEMBL)
Ig kappa chain V-I region Walker [extracellular region]	Protein	P04431 (Uniprot-TrEMBL)
Ig kappa chain V-I region Wes [extracellular region]	Protein	P01611 (Uniprot-TrEMBL)
Ig kappa chain V-II region Cum [extracellular region]	Protein	P01614 (Uniprot-TrEMBL)
Ig kappa chain V-II region FR [extracellular region]	Protein	P01615 (Uniprot-TrEMBL)
Ig kappa chain V-II region GM607 [extracellular region]	Protein	P06309 (Uniprot-TrEMBL)
Ig kappa chain V-II region MIL [extracellular region]	Protein	P01616 (Uniprot-TrEMBL)
Ig kappa chain V-II region RPMI 6410 [extracellular region]	Protein	P06310 (Uniprot-TrEMBL)
Ig kappa chain V-II region TEW [extracellular region]	Protein	P01617 (Uniprot-TrEMBL)
Ig kappa chain V-III region B6 [extracellular region]	Protein	P01619 (Uniprot-TrEMBL)
Ig kappa chain V-III region CLL [extracellular region]	Protein	P04207 (Uniprot-TrEMBL)
Ig kappa chain V-III region GOL [extracellular region]	Protein	P04206 (Uniprot-TrEMBL)
Ig kappa chain V-III region HAH [extracellular region]	Protein	P18135 (Uniprot-TrEMBL)
Ig kappa chain V-III region HIC [extracellular region]	Protein	P18136 (Uniprot-TrEMBL)
Ig kappa chain V-III region IARC/BL41 [extracellular region]	Protein	P06311 (Uniprot-TrEMBL)
Ig kappa chain V-III region NG9 [extracellular region]	Protein	P01621 (Uniprot-TrEMBL)
Ig kappa chain V-III region POM [extracellular region]	Protein	P01624 (Uniprot-TrEMBL)
Ig kappa chain V-III region SIE [extracellular region]	Protein	P01620 (Uniprot-TrEMBL)
Ig kappa chain V-III region Ti [extracellular region]	Protein	P01622 (Uniprot-TrEMBL)
Ig kappa chain V-III region VG [extracellular region]	Protein	P04433 (Uniprot-TrEMBL)
Ig kappa chain V-III region VH [extracellular region]	Protein	P04434 (Uniprot-TrEMBL)
Ig kappa chain V-III region WOL [extracellular region]	Protein	P01623 (Uniprot-TrEMBL)
Ig kappa chain V-IV region B17 [extracellular region]	Protein	P06314 (Uniprot-TrEMBL)
Ig kappa chain V-IV region JI [extracellular region]	Protein	P06313 (Uniprot-TrEMBL)
Ig kappa chain V-IV region Len [extracellular region]	Protein	P01625 (Uniprot-TrEMBL)
Ig kappa chain V-IV region STH [extracellular region]	Protein	P83593 (Uniprot-TrEMBL)
Ig lambda chain V-III region LOI [extracellular region]	Protein	P80748 (Uniprot-TrEMBL)
Ig lambda chain V-III region SH [extracellular region]	Protein	P01714 (Uniprot-TrEMBL)
Ig lambda chain V-VII region MOT [extracellular region]	Protein	P01720 (Uniprot-TrEMBL)
Ig lambda chain V region 4A [extracellular region]	Protein	P04211 (Uniprot-TrEMBL)
Ig lambda chain V-I region BL2 [extracellular region]	Protein	P06316 (Uniprot-TrEMBL)
Ig lambda chain V-I region EPS [extracellular region]	Protein	P06888 (Uniprot-TrEMBL)
Ig lambda chain V-I region HA [extracellular region]	Protein	P01700 (Uniprot-TrEMBL)
Ig lambda chain V-I region MEM [extracellular region]	Protein	P06887 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEW [extracellular region]	Protein	P01701 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEWM [extracellular region]	Protein	P01703 (Uniprot-TrEMBL)
Ig lambda chain V-I region NIG-64 [extracellular region]	Protein	P01702 (Uniprot-TrEMBL)
Ig lambda chain V-I region VOR [extracellular region]	Protein	P01699 (Uniprot-TrEMBL)
Ig lambda chain V-I region WAH [extracellular region]	Protein	P04208 (Uniprot-TrEMBL)
Ig lambda chain V-II region BO [extracellular region]	Protein	P01710 (Uniprot-TrEMBL)
Ig lambda chain V-II region BOH [extracellular region]	Protein	P01706 (Uniprot-TrEMBL)
Ig lambda chain V-II region BUR [extracellular region]	Protein	P01708 (Uniprot-TrEMBL)
Ig lambda chain V-II region MGC [extracellular region]	Protein	P01709 (Uniprot-TrEMBL)
Ig lambda chain V-II region NEI [extracellular region]	Protein	P01705 (Uniprot-TrEMBL)
Ig lambda chain V-II region NIG-58 [extracellular region]	Protein	P01713 (Uniprot-TrEMBL)
Ig lambda chain V-II region NIG-84 [extracellular region]	Protein	P04209 (Uniprot-TrEMBL)
Ig lambda chain V-II region TOG [extracellular region]	Protein	P01704 (Uniprot-TrEMBL)
Ig lambda chain V-II region TRO [extracellular region]	Protein	P01707 (Uniprot-TrEMBL)
Ig lambda chain V-II region VIL [extracellular region]	Protein	P01711 (Uniprot-TrEMBL)
Ig lambda chain V-II region WIN [extracellular region]	Protein	P01712 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Bau [extracellular region]	Protein	P01715 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Hil [extracellular region]	Protein	P01717 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Kern [extracellular region]	Protein	P01718 (Uniprot-TrEMBL)
Ig lambda chain V-IV region MOL [extracellular region]	Protein	P06889 (Uniprot-TrEMBL)
Ig lambda chain V-IV region X [extracellular region]	Protein	P01716 (Uniprot-TrEMBL)
Ig lambda chain V-V region DEL [extracellular region]	Protein	P01719 (Uniprot-TrEMBL)
Ig lambda chain V-VI region AR [extracellular region]	Protein	P01721 (Uniprot-TrEMBL)
Ig lambda chain V-VI region EB4 [extracellular region]	Protein	P06319 (Uniprot-TrEMBL)
Ig lambda chain V-VI region NIG-48 [extracellular region]	Protein	P01722 (Uniprot-TrEMBL)
Ig lambda chain V-VI region SUT [extracellular region]	Protein	P06317 (Uniprot-TrEMBL)
Ig lambda chain V-VI region WLT [extracellular region]	Protein	P06318 (Uniprot-TrEMBL)
IgG-Ag:FCGRIA:CD3G homodimer	Complex	REACT_161410 (Reactome)
IgG-Ag:FCGRIIA	Complex	REACT_161266 (Reactome)
IgG-Ag:FCGRIIIA:CD3G/CD3Z dimers	Complex	REACT_161242 (Reactome)
IgH heavy chain V-III region VH26 precursor [extracellular region]	Protein	P01764 (Uniprot-TrEMBL)
LIMK1	Protein	P53667 (Uniprot-TrEMBL)
MYO10 [cytosol]	Protein	Q9HD67 (Uniprot-TrEMBL)
Mother filament:ARP2/3:actin:GDP	Complex	REACT_161497 (Reactome)
Mother filament:branching complex:daughter filament	Complex	REACT_161289 (Reactome)
Mother filament:branching complex	Complex	REACT_161230 (Reactome)
Myosin-Actin filaments	Complex	REACT_160496 (Reactome)
Myosin-X dimer	Complex	REACT_160739 (Reactome)
Myosin	Protein	REACT_160342 (Reactome)
NCK1 [cytosol]	Protein	P16333 (Uniprot-TrEMBL)
NCKAP1 [cytosol]	Protein	Q9Y2A7 (Uniprot-TrEMBL)
NCKIPSD [cytosol]	Protein	Q9NZQ3 (Uniprot-TrEMBL)
PA	Metabolite	CHEBI:16337 (ChEBI)
PAK1 [cytosol]	Protein	Q13153 (Uniprot-TrEMBL)
PAK1 dimer	Complex	REACT_23136 (Reactome)
PAK1	Protein	Q13153 (Uniprot-TrEMBL)
PC	Metabolite	CHEBI:16110 (ChEBI)
PI(3,4)P2 [plasma membrane]	Metabolite	CHEBI:16152 (ChEBI)
PI(3,4)P2	Metabolite	CHEBI:16152 (ChEBI)
PI(3,4,5)P3 [plasma membrane]	Metabolite	CHEBI:16618 (ChEBI)
PI(3,4,5)P3	Metabolite	CHEBI:16618 (ChEBI)
PI(4,5)P2 [plasma membrane]	Metabolite	CHEBI:18348 (ChEBI)
PI(4,5)P2	Metabolite	CHEBI:18348 (ChEBI)
PI3K:p-6Y-SYK	Complex	REACT_160388 (Reactome)
PI3K	Complex	REACT_4240 (Reactome)
PIK3CA [cytosol]	Protein	P42336 (Uniprot-TrEMBL)
PIK3CB [cytosol]	Protein	P42338 (Uniprot-TrEMBL)
PIK3R1 [cytosol]	Protein	P27986 (Uniprot-TrEMBL)
PIK3R2 [cytosol]	Protein	O00459 (Uniprot-TrEMBL)
PKC-delta/epsilon		REACT_12301 (Reactome)
PLA2G6	Protein	O60733 (Uniprot-TrEMBL)
PLC gamma1/2	Protein	REACT_120292 (Reactome)
PLCG1(2-1290) [cytosol]	Protein	P19174 (Uniprot-TrEMBL)
PLCG2 [cytosol]	Protein	P16885 (Uniprot-TrEMBL)
PLD	Protein	REACT_161489 (Reactome)
Phosphatidate phosphatase	Protein	REACT_160956 (Reactome)
Phosphatidylcholine	Metabolite	CHEBI:16110 (ChEBI)
Phospho-PKC-delta/epsilon	Protein	REACT_12203 (Reactome)
Pi	Metabolite	CHEBI:18367 (ChEBI)
RAC1 [cytosol]	Protein	P63000 (Uniprot-TrEMBL)
RAC1-GDP	Complex	REACT_22018 (Reactome)
RAC1-GTP	Complex	REACT_21594 (Reactome)
RAC1/CDC42:PAK dimer	Complex	REACT_160723 (Reactome)
RAC1/CDC42:p-S144,T423-PAK	Complex	REACT_160965 (Reactome)
SH3 domain proteins	Protein	REACT_160607 (Reactome)
SYK [cytosol]	Protein	P43405 (Uniprot-TrEMBL)
SYK	Protein	P43405 (Uniprot-TrEMBL)
Src family kinases (SFKs)	Protein	REACT_161384 (Reactome)
Src-kinases	Protein	REACT_161502 (Reactome)
VAV1 [cytosol]	Protein	P15498 (Uniprot-TrEMBL)
VAV2 [cytosol]	Protein	P52735 (Uniprot-TrEMBL)
VAV3 [cytosol]	Protein	Q9UKW4 (Uniprot-TrEMBL)
VAV	Protein	REACT_21165 (Reactome)
WAS [cytosol]	Protein	P42768 (Uniprot-TrEMBL)
WASL [cytosol]	Protein	O00401 (Uniprot-TrEMBL)
WASP/N-WASP	Protein	REACT_161400 (Reactome)
WAVE Regulatory Complex	Complex	REACT_161217 (Reactome)
WIP family proteins	Protein	REACT_161452 (Reactome)
WIPF1 [cytosol]	Protein	O43516 (Uniprot-TrEMBL)
WIPF2 [cytosol]	Protein	Q8TF74 (Uniprot-TrEMBL)
WIPF3 [cytosol]	Protein	A6NGB9 (Uniprot-TrEMBL)
WRC:IRSp53/58:RAC1-GTP:PIP3	Complex	REACT_160732 (Reactome)
choline	Metabolite	CHEBI:15354 (ChEBI)
clustered IgG-Ag:FCGRs	Complex	REACT_160485 (Reactome)
clustered IgG-Ag:p-FCGRs:SYK	Complex	REACT_161298 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:PLCG	Complex	REACT_161309 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:VAV	Complex	REACT_160419 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:p-3Y-PLCG	Complex	REACT_160360 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:p-VAV	Complex	REACT_161035 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK	Complex	REACT_161038 (Reactome)
clustered IgG-Ag:p-FCGRs	Complex	REACT_160515 (Reactome)
clustered IgG-Ag:p-FCGRs	Complex	REACT_160696 (Reactome)
p-4Y-PLCG1 [plasma membrane]	Protein	P19174 (Uniprot-TrEMBL)
p-4Y-PLCG1	Protein	P19174 (Uniprot-TrEMBL)
p-6Y-CD247-1 [plasma membrane]	Protein	P20963-1 (Uniprot-TrEMBL)
p-6Y-SYK [cytosol]	Protein	P43405 (Uniprot-TrEMBL)
p-PLCG	Protein	REACT_160862 (Reactome)
p-S,T508-LIMK1 [cytosol]	Protein	P53667 (Uniprot-TrEMBL)
p-S144,T423-PAK1 [cytosol]	Protein	Q13153 (Uniprot-TrEMBL)
p-S144,T423-PAK1	Protein	Q13153 (Uniprot-TrEMBL)
p-S3-CFL1 [cytosol]	Protein	P23528 (Uniprot-TrEMBL)
p-T508-LIMK1 [cytosol]	Protein	P53667 (Uniprot-TrEMBL)
p-T508-LIMK1	Protein	P53667 (Uniprot-TrEMBL)
p-WRC:IRSp53/58:RAC1-GTP:PIP3	Complex	REACT_160497 (Reactome)
p-WRC:IRSp53/58:RAC1-GTP:PIP3	Complex	REACT_161191 (Reactome)
p-Y160,Y171-CD3G [plasma membrane]	Protein	P09693 (Uniprot-TrEMBL)
p-Y172-VAV2 [cytosol]	Protein	P52735 (Uniprot-TrEMBL)
p-Y173-VAV3 [cytosol]	Protein	Q9UKW4 (Uniprot-TrEMBL)
p-Y174-VAV1 [cytosol]	Protein	P15498 (Uniprot-TrEMBL)
p-Y256-WASL [cytosol]	Protein	O00401 (Uniprot-TrEMBL)
p-Y288,Y304-FCGR2A [plasma membrane]	Protein	P12318 (Uniprot-TrEMBL)
p-Y291-WAS [cytosol]	Protein	P42768 (Uniprot-TrEMBL)
p-Y753,Y759,Y1217-PLCG2 [plasma membrane]	Protein	P16885 (Uniprot-TrEMBL)
pCofilin: Active LIMK-1	Complex	REACT_20103 (Reactome)
pLIMK dimer:HSP-90	Complex	REACT_19543 (Reactome)

Annotated Interactions

View all...

Source	Target	Type	Database reference	Comment
	2-Lysophosphatidylcholine	Arrow	REACT_160241 (Reactome)
ABL1		mim-catalysis	REACT_160185 (Reactome)
	ADP	Arrow	REACT_12062 (Reactome)
	ADP	Arrow	REACT_160105 (Reactome)
	ADP	Arrow	REACT_160161 (Reactome)
	ADP	Arrow	REACT_160185 (Reactome)
	ADP	Arrow	REACT_160224 (Reactome)
	ADP	Arrow	REACT_160233 (Reactome)
	ADP	Arrow	REACT_160238 (Reactome)
	ADP	Arrow	REACT_160260 (Reactome)
	ADP	Arrow	REACT_160265 (Reactome)
	ADP	Arrow	REACT_160287 (Reactome)
	ADP	Arrow	REACT_160304 (Reactome)
	ADP	Arrow	REACT_19168 (Reactome)
	ADP	Arrow	REACT_19276 (Reactome)
ARP2/3 complex (ATP bound)			REACT_160118 (Reactome)
ATP			REACT_12062 (Reactome)
ATP			REACT_160090 (Reactome)
ATP			REACT_160105 (Reactome)
ATP			REACT_160161 (Reactome)
ATP			REACT_160185 (Reactome)
ATP			REACT_160224 (Reactome)
ATP			REACT_160233 (Reactome)
ATP			REACT_160238 (Reactome)
ATP			REACT_160257 (Reactome)
ATP			REACT_160260 (Reactome)
ATP			REACT_160265 (Reactome)
ATP			REACT_160287 (Reactome)
ATP			REACT_160304 (Reactome)
ATP			REACT_19168 (Reactome)
ATP			REACT_19276 (Reactome)
	Actin filament bound Myosin-X	Arrow	REACT_160257 (Reactome)
	Actin:ADP	Arrow	REACT_160291 (Reactome)
	Activated WAVE2 and WASP/N-WASP:ARP2/3 complex:G-actin	Arrow	REACT_160118 (Reactome)
Activated WAVE2 and WASP/N-WASP:ARP2/3 complex:G-actin			REACT_160206 (Reactome)
	Activated WAVE2 and WASP/N-WASP	Arrow	REACT_160164 (Reactome)
Activated WAVE2 and WASP/N-WASP			REACT_160118 (Reactome)
	Active LIMK1	Arrow	REACT_19168 (Reactome)
Active LIMK1			REACT_19276 (Reactome)
Active LIMK1		mim-catalysis	REACT_19276 (Reactome)
Active RAC1/CDC42			REACT_160204 (Reactome)
Antigen-antibody complex			REACT_160141 (Reactome)
Antigen-antibody complex			REACT_160169 (Reactome)
Antigen-antibody complex			REACT_160317 (Reactome)
	Arachidonic acid	Arrow	REACT_160241 (Reactome)
BAIAP2			REACT_160150 (Reactome)
CDC42-GDP			REACT_160236 (Reactome)
	CDC42-GTP:WASP/N-WASP:WIP:SH3 proteins	Arrow	REACT_160166 (Reactome)
CDC42-GTP:WASP/N-WASP:WIP:SH3 proteins			REACT_160238 (Reactome)
	CDC42-GTP:WASP/N-WASP	Arrow	REACT_160173 (Reactome)
CDC42-GTP:WASP/N-WASP			REACT_160166 (Reactome)
	CDC42-GTP:p-WASP/p-N-WASP:WIP:SH3 proteins	Arrow	REACT_160238 (Reactome)
	CDC42:GTP	Arrow	REACT_160236 (Reactome)
CDC42:GTP			REACT_160173 (Reactome)
CFL1			REACT_19276 (Reactome)
CRK:DOCK180:ELMO			REACT_160134 (Reactome)
	CRKII:DOCK180:ELMO complex recruited to phagocytic cup	Arrow	REACT_160134 (Reactome)
CRKII:DOCK180:ELMO complex recruited to phagocytic cup		mim-catalysis	REACT_160127 (Reactome)
	Ca2+	Arrow	REACT_12074 (Reactome)
Ca2+			REACT_12074 (Reactome)
	DAGs	Arrow	REACT_12078 (Reactome)
	DAGs	Arrow	REACT_160284 (Reactome)
ERK		mim-catalysis	REACT_160224 (Reactome)
F-actin			REACT_160206 (Reactome)
FCGR2A			REACT_160141 (Reactome)
FCGRIA:CD3G homodimer			REACT_160317 (Reactome)
FCGRIIIA:CD3G/CD3Z dimers			REACT_160169 (Reactome)
G-actin			REACT_160118 (Reactome)
G-actin			REACT_160291 (Reactome)
	GDP	Arrow	REACT_160127 (Reactome)
	GDP	Arrow	REACT_160236 (Reactome)
	GDP	Arrow	REACT_160258 (Reactome)
GTP			REACT_160127 (Reactome)
GTP			REACT_160236 (Reactome)
GTP			REACT_160258 (Reactome)
H2O			REACT_12078 (Reactome)
H2O			REACT_160135 (Reactome)
H2O			REACT_160241 (Reactome)
H2O			REACT_160284 (Reactome)
	HSP-90	Arrow	REACT_19168 (Reactome)
HSP-90			REACT_19307 (Reactome)
	I(1,4,5)P3	Arrow	REACT_12078 (Reactome)
I(1,4,5)P3			REACT_12008 (Reactome)
IP3 receptor homotetramer			REACT_12008 (Reactome)
	IP3 receptor:IP3 complex	Arrow	REACT_12008 (Reactome)
IP3 receptor:IP3 complex		mim-catalysis	REACT_12074 (Reactome)
	IgG-Ag:FCGRIA:CD3G homodimer	Arrow	REACT_160317 (Reactome)
	IgG-Ag:FCGRIIA	Arrow	REACT_160141 (Reactome)
	IgG-Ag:FCGRIIIA:CD3G/CD3Z dimers	Arrow	REACT_160169 (Reactome)
LIMK1			REACT_160233 (Reactome)
	Mother filament:ARP2/3:actin:GDP	Arrow	REACT_160164 (Reactome)
Mother filament:ARP2/3:actin:GDP			REACT_160291 (Reactome)
	Mother filament:branching complex:daughter filament	Arrow	REACT_160291 (Reactome)
Mother filament:branching complex:daughter filament			REACT_160090 (Reactome)
Mother filament:branching complex:daughter filament			REACT_160257 (Reactome)
	Mother filament:branching complex	Arrow	REACT_160206 (Reactome)
Mother filament:branching complex			REACT_160164 (Reactome)
	Myosin-Actin filaments	Arrow	REACT_160090 (Reactome)
Myosin-X dimer			REACT_160257 (Reactome)
Myosin-X dimer		mim-catalysis	REACT_160257 (Reactome)
Myosin			REACT_160090 (Reactome)
	PA	Arrow	REACT_160135 (Reactome)
PAK1 dimer			REACT_160204 (Reactome)
PAK1		mim-catalysis	REACT_160161 (Reactome)
PA			REACT_160284 (Reactome)
PC			REACT_160135 (Reactome)
PI(3,4)P2			REACT_160257 (Reactome)
	PI(3,4,5)P3	Arrow	REACT_160203 (Reactome)
	PI(3,4,5)P3	Arrow	REACT_160265 (Reactome)
PI(3,4,5)P3			REACT_160105 (Reactome)
PI(3,4,5)P3			REACT_160150 (Reactome)
PI(3,4,5)P3			REACT_160201 (Reactome)
PI(4,5)P2			REACT_12078 (Reactome)
PI(4,5)P2			REACT_160173 (Reactome)
PI(4,5)P2			REACT_160265 (Reactome)
	PI3K:p-6Y-SYK	Arrow	REACT_160316 (Reactome)
PI3K:p-6Y-SYK		mim-catalysis	REACT_160265 (Reactome)
PI3K			REACT_160316 (Reactome)
PKC-delta/epsilon			REACT_12062 (Reactome)
PKC-delta/epsilon		mim-catalysis	REACT_12062 (Reactome)
PLA2G6		mim-catalysis	REACT_160241 (Reactome)
PLC gamma1/2			REACT_160294 (Reactome)
PLD		mim-catalysis	REACT_160135 (Reactome)
Phosphatidate phosphatase		mim-catalysis	REACT_160284 (Reactome)
Phosphatidylcholine			REACT_160241 (Reactome)
	Phospho-PKC-delta/epsilon	Arrow	REACT_12062 (Reactome)
	Pi	Arrow	REACT_160090 (Reactome)
	Pi	Arrow	REACT_160257 (Reactome)
	Pi	Arrow	REACT_160284 (Reactome)
	Pi	Arrow	REACT_160291 (Reactome)
RAC1-GDP			REACT_160127 (Reactome)
RAC1-GDP			REACT_160258 (Reactome)
	RAC1-GTP	Arrow	REACT_160127 (Reactome)
	RAC1-GTP	Arrow	REACT_160258 (Reactome)
RAC1-GTP			REACT_160150 (Reactome)
	RAC1/CDC42:PAK dimer	Arrow	REACT_160204 (Reactome)
RAC1/CDC42:PAK dimer			REACT_160161 (Reactome)
	RAC1/CDC42:p-S144,T423-PAK	Arrow	REACT_160161 (Reactome)
			REACT_12008 (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.
			REACT_12062 (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.
			REACT_12074 (Reactome)	IP3 promotes the release of intracellular calcium.
			REACT_12078 (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).
			REACT_160090 (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).
			REACT_160094 (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).
			REACT_160105 (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.
			REACT_160118 (Reactome)	Once activated the VCA region in WAVE2 or WASP/N-WASP becomes available for binding to ARP2/3 and actin monomer. 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 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).
			REACT_160127 (Reactome)	RAC1 is activated from inactive GDP-bound state to active GTP-bound form by the GEF activity of DOCK180:ELMO complex.
			REACT_160134 (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).
			REACT_160135 (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).
			REACT_160141 (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).
			REACT_160150 (Reactome)	WASP family verprolin-homologous (WAVE) proteins function downstream of RAC1 and are involved in activation of the ARP2/3 complex. This resulting actin polymerization mediates the projection of the plasma membrane in lamellipodia and membrane ruffles. The WAVE proteins exist as pentameric hetero-complex called WAVE Regulatory Complex (WRC). This WRC consists of WAVE family proteins, ABI (Abelson-interacting protein), NAP1 (also known as p125NAP1), SRA1 (or the closely related PIR121; SRA1 is also known as CYFIP1) and HSPC300 (also known as BRICK). There are three structurally conserved WAVE family proteins (WAVE1, 2, and 3) present in mammals. Among these, WAVE2 is important for the activation of ARP2/3complex in the formation of branched actin filaments. WAVEs are intrinsically inactive and are stimulated by Rac GTPase and phosphatidylinositols. The C-terminal VCA domain in WAVE2 can bind both ARP2/3 complex and actin monomers and is masked in the inactive state. The WAVE2 complex, is activated upon binding PIP3 to the polybasic region of WAVE2 and RAC1-GTP to the SRA1 subunit. This most likely occurs through allosteric changes leading to ARP2/3 interaction. The interactions between WAVEs and RAC are indirect. BAIAP2/IRSp53, an insulin receptor substrate, acts as a linker, binding both activated RAC1, and the proline-rich region of WAVE2 forming a trimolecular complex. SRA1/PIR121 in the WAVE regulatory complex binds directly to RAC1-GTP and link it to WAVE2. (Derivery et al. 2009, Yamazaki et al. 2006, Takenawa & Suetsugu 2007, Chen et al. 2010, Pollard 2007, Lebensohn & Kirschner 2009)
			REACT_160161 (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).
			REACT_160164 (Reactome)	After incorporation at the branch the actin bound to VCA domain in 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).
			REACT_160166 (Reactome)	WASP interacting proteins (WIP) family of proteins which includes WIP, corticosteroids and regional expression-16 (CR16) and WIP related (WIRE/WICH) with their specific proline rich sequence interact with the WH1 domain of WASP/N-WASP. These proteins form heterocomplexes with WASP/N-WASP and may help in the WASP proteins 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 N-WASP/WASP and activate ARP2/3 complex. By binding simultaneously with N-WASP, GRB2 works synergistically with CDC42 in the activation of ARP2/3 complex (Carlier et al. 2000).
			REACT_160169 (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). Between the two isoforms FCGRIIIA is involved in phagocytosis whereas FCGRIIIB is capable of inducing calcium signalling and actin polymerisation, but its role in phagocytosis is still not clear (Garcia Garcia & Rosales 2002). FCGRIIIA 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). 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. 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).
			REACT_160173 (Reactome)	Wiskott-Aldrich syndrome protein (WASP) and Neural-WASP (N-WASP) 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), adjacent to this is a basic region (B) and a C-terminal containing 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 autoinhibition state via interaction of the N-terminal GBD and the C-terminal VCA domains. This prevents access of the ARP2/3 complex to the VCA region. Activated CDC42 binds to the GBD region in N-WASP and this interaction releases the VCA region from autoinhibition enabling binding of the ARP2/3 complex stimulating actin polymerization (Kim et al 2000, Park & Cox 2009). Phosphoinositides (PtdIns(4,5)P2) interact with the basic (B) region in WASP and this interaction is important for activation of the WASP and ARP2/3 complex.(Higgs & Pollard 2000).
			REACT_160185 (Reactome)	Abelson interactor-1 (ABL) tyrosine kinase phosphorylates the strictly conserved tyrosine 150 in WAVE2 (Y151 in WAVE1 and 3) (Leng et al. 2003, Chen et al. 2010).
			REACT_160201 (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.
			REACT_160203 (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.
			REACT_160204 (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).
			REACT_160206 (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 subunit binds 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 subunit would incorporate into the mother filament at the barbed end, thus positioning ARP2/3 complex to initiate the daughter branch on the side of the the mother filament. ARP2/3 nucleates the formation of a 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 and mimics an actin nucleus and initiates lateral branch (Le Clainche & Carlier 2008, Amann & Pollard 2001).
			REACT_160224 (Reactome)	The ARP2/3 complex shows higher affinity for the phosphorylated VCA domain of WAVE2 than for the unphosphorylated VCA domain. WAVE proteins are phosphorylated by various stimulations. 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) contribute 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).
			REACT_160233 (Reactome)	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. LIMK is one of the downstream targets of PAK1 and is activated through phosphorylation by PAK1 on T508 within its activation loop.
			REACT_160236 (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).
			REACT_160238 (Reactome)	WASP is phosphorylated on Tyr291 (Cory et al. 2002) and N-WASP 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).
			REACT_160241 (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.
			REACT_160257 (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).
			REACT_160258 (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).
			REACT_160260 (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.
			REACT_160265 (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.
			REACT_160284 (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.
			REACT_160287 (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).
			REACT_160291 (Reactome)	ATP bound G-actin monomers are added to the fast growing barbed ends of both the mother and the daughter filaments and the polymerization of these filaments drives membrane protrusion. Pseudopodia extend around the antibody bound particle to form the phagocytic cup. This elongation continues until the filament reaches a steady state equilibrium with free G-actin monomers.
			REACT_160294 (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 )
			REACT_160304 (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).
			REACT_160316 (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).
			REACT_160317 (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).
			REACT_19168 (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.
			REACT_19276 (Reactome)	Cofilin 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 cofilin on conserved serine 3 (Ser3/S3), located near the actin binding site. After phosphorylation cofilin is inactive and looses its affinity for actin and releases from G-actin monomers. Now the ADP-actin monomers are free and can exchange ADP with cytoplasmic ATP and they are ready for reincorporation at the barbed end of the a growing filament.
			REACT_19307 (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.
SH3 domain proteins			REACT_160166 (Reactome)
SYK			REACT_160094 (Reactome)
Src family kinases (SFKs)		mim-catalysis	REACT_160304 (Reactome)
Src-kinases		mim-catalysis	REACT_160238 (Reactome)
VAV			REACT_160201 (Reactome)
WASP/N-WASP			REACT_160173 (Reactome)
WAVE Regulatory Complex			REACT_160150 (Reactome)
WIP family proteins			REACT_160166 (Reactome)
	WRC:IRSp53/58:RAC1-GTP:PIP3	Arrow	REACT_160150 (Reactome)
WRC:IRSp53/58:RAC1-GTP:PIP3			REACT_160185 (Reactome)
WRC:IRSp53/58:RAC1-GTP:PIP3			REACT_160224 (Reactome)
	choline	Arrow	REACT_160135 (Reactome)
clustered IgG-Ag:FCGRs			REACT_160304 (Reactome)
	clustered IgG-Ag:p-FCGRs:SYK	Arrow	REACT_160094 (Reactome)
clustered IgG-Ag:p-FCGRs:SYK			REACT_160287 (Reactome)
clustered IgG-Ag:p-FCGRs:SYK		mim-catalysis	REACT_160287 (Reactome)
	clustered IgG-Ag:p-FCGRs:p-6Y-SYK:PLCG	Arrow	REACT_160294 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:PLCG			REACT_160105 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:PLCG		mim-catalysis	REACT_160105 (Reactome)
	clustered IgG-Ag:p-FCGRs:p-6Y-SYK:VAV	Arrow	REACT_160201 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:VAV			REACT_160260 (Reactome)
	clustered IgG-Ag:p-FCGRs:p-6Y-SYK:p-3Y-PLCG	Arrow	REACT_160105 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:p-3Y-PLCG			REACT_160203 (Reactome)
	clustered IgG-Ag:p-FCGRs:p-6Y-SYK:p-VAV	Arrow	REACT_160260 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK:p-VAV		mim-catalysis	REACT_160258 (Reactome)
	clustered IgG-Ag:p-FCGRs:p-6Y-SYK	Arrow	REACT_160203 (Reactome)
	clustered IgG-Ag:p-FCGRs:p-6Y-SYK	Arrow	REACT_160287 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK			REACT_160134 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK			REACT_160201 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK			REACT_160294 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK			REACT_160316 (Reactome)
clustered IgG-Ag:p-FCGRs:p-6Y-SYK		mim-catalysis	REACT_160260 (Reactome)
	clustered IgG-Ag:p-FCGRs	Arrow	REACT_160090 (Reactome)
	clustered IgG-Ag:p-FCGRs	Arrow	REACT_160304 (Reactome)
clustered IgG-Ag:p-FCGRs			REACT_160090 (Reactome)
clustered IgG-Ag:p-FCGRs			REACT_160094 (Reactome)
p-4Y-PLCG1		mim-catalysis	REACT_12078 (Reactome)
	p-PLCG	Arrow	REACT_160203 (Reactome)
	p-S144,T423-PAK1	Arrow	REACT_160161 (Reactome)
p-S144,T423-PAK1		mim-catalysis	REACT_160233 (Reactome)
	p-T508-LIMK1	Arrow	REACT_160233 (Reactome)
p-T508-LIMK1			REACT_19307 (Reactome)
	p-WRC:IRSp53/58:RAC1-GTP:PIP3	Arrow	REACT_160185 (Reactome)
	p-WRC:IRSp53/58:RAC1-GTP:PIP3	Arrow	REACT_160224 (Reactome)
	pCofilin: Active LIMK-1	Arrow	REACT_19276 (Reactome)
	pLIMK dimer:HSP-90	Arrow	REACT_19307 (Reactome)
pLIMK dimer:HSP-90			REACT_19168 (Reactome)
pLIMK dimer:HSP-90		mim-catalysis	REACT_19168 (Reactome)