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PMID: 18385944, 8132624, 8327512, 9581795
Because SFKs have been reported to associate with Fcg receptors [135–138], this association may represent the mechanism dictating proximity between SFKs and ITAM-containing adaptors.
PMID: 18385944
Syk binds to phosphorylated tyrosine residues of ITAM-containing adaptors and is phosphorylated and activated by SFKs.
PMID: 18385944
Syk binds to phosphorylated tyrosine residues of ITAM-containing adaptors and is phosphorylated and activated by SFKs.
PMID: 18385944
Syk binds to phosphorylated tyrosine residues of ITAM-containing adaptors and is phosphorylated and activated by SFKs.
PMID: 18385944, 17420256, 15519852
Other receptors, such as trimeric G protein-coupled receptors for chemoattractants [14 – 17] and c-Fms [18, 19] seem to implicate only SFKs, but not Syk.
PMID: 18385944
As indicated, interaction of SFK with integrins, c-Cbl and b-arrestin have been reported to occur via the SH3 domain.
PMID: 18385944, 9916742, 10527858, 10973280
Other receptors, such as trimeric G protein-coupled receptors for chemoattractants [14 – 17] and c-Fms [18, 19] seem to implicate only SFKs, but not Syk.
PMID: 18385944, 17420256
SFKs bind to c-Fms in myeloid leukocytes and recruit a c-Cbl/PI3-kinase complex to the membrane.
PMID: 18395944, 17632516
PSGL-1, the major leukocyte ligand for endothelial selectins, implicates SFKs for phosphorylation of its associated molecule Naf1 which in turn binds PI3-kinase.
PMID: 18395944, 17632516
PSGL-1, the major leukocyte ligand for endothelial selectins, implicates SFKs for phosphorylation of its associated molecule Naf1 which in turn binds PI3-kinase.
PMID: 18395944, 17632516
PSGL-1, the major leukocyte ligand for endothelial selectins, implicates SFKs for phosphorylation of its associated molecule Naf1 which in turn binds PI3-kinase.
PMID: 18385944, 12387735
PSGL-1 also triggers phosphorylation of ezrin and moesin, two ITAM-containing molecules associated with its cytoplasmic tail [20]; it is conceivable that ezrin and moesin phosphorylation is mediated by SFKs.
PMID: 18385944
Receptors for chemokines bind SFKs in phagocytes likely via binding to beta-arrestin.
PMID: 18385944
As indicated, interaction of SFK with integrins, c-Cbl and b-arrestin have been reported to occur via the SH3 domain.
PMID: 18385944
In the case of integrins, both SFKs and Syk have been reported to bind to the integrin beta3 or beta2 chain.
PMID: 18385944
As indicated, interaction of SFK with integrins, c-Cbl and b-arrestin have been reported to occur via the SH3 domain.
PMID: 18385944
In the case of integrins, both SFKs and Syk have been reported to bind to the integrin beta3 or beta2 chain.
PMID: 18385944
As indicated, interaction of SFK with integrins, c-Cbl and b-arrestin have been reported to occur via the SH3 domain.
PMID: 18385944
In the case of integrins, both SFKs and Syk have been reported to bind to the integrin beta3 or beta2 chain.
PMID: 18385944
In the case of integrins, both SFKs and Syk have been reported to bind to the integrin beta3 or beta2 chain.
PMID: 18385944, 10527858, 10973280, 7535337
Receptors for chemokines (CCR3, CXCR1) directly [15] or indirectly [16] interacts with Fgr and Hck in granulocytes and the urokinase plasminogen-activator-receptor, a powerful chemoattractant, forms a membrane signaling complex containing the Srcfamily kinases, Fgr, Fyn, Lyn and Hck, as well as b2 integrins, in monocytes [6].
PMID: 18385944, 10527858, 10973280, 7535337
Receptors for chemokines (CCR3, CXCR1) directly [15] or indirectly [16] interacts with Fgr and Hck in granulocytes and the urokinase plasminogen-activator-receptor, a powerful chemoattractant, forms a membrane signaling complex containing the Srcfamily kinases, Fgr, Fyn, Lyn and Hck, as well as b2 integrins, in monocytes [6].
PMID: 18385944, 10527858, 10973280, 7535337
Receptors for chemokines (CCR3, CXCR1) directly [15] or indirectly [16] interacts with Fgr and Hck in granulocytes and the urokinase plasminogen-activator-receptor, a powerful chemoattractant, forms a membrane signaling complex containing the Srcfamily kinases, Fgr, Fyn, Lyn and Hck, as well as b2 integrins, in monocytes [6].
PMID: 18385944, 7535337
The first strong evidence suggesting a link between a chemoattractant receptor, b2 integrins and SFKs in regulating mononuclear phagocyte migration derives from studies showing that the urokinase type plasminogen activator-receptor (uPA-R), the b2 integrins LFA-1 and CR3, and the SFK members Hck, Fgr, Lyn nd Fyn form a large molecular complex in human monocytes [6].
Indirect
PMID: 18385944, 8810279, 7650013
Neutrophil stimulation with chemoattractants activates a Lyn/Shc/p85-p110 phosphatidylinositol 3-kinase pathway (PI-3K) [93, 94].
PMID: 18385944, 12208881
Interaction of the chemokine Stromal cell-derived factor (SDF/CXCL12) with its receptor (CXCR4) triggers a signalling pathway implicatingLyn and PI-3K in HL-60 cells and hematopoietic progenitors and SDF-induced cell migration is defective in Lyndeficient bone marrow cells [99].
PMID: 18385944, 12208881
Interaction of the chemokine Stromal cell-derived factor (SDF/CXCL12) with its receptor (CXCR4) triggers a signalling pathway implicatingLyn and PI-3K in HL-60 cells and hematopoietic progenitors and SDF-induced cell migration is defective in Lyndeficient bone marrow cells [99].
Indirect
PMID: 18385944, 12208881
Interaction of the chemokine Stromal cell-derived factor (SDF/CXCL12) with its receptor (CXCR4) triggers a signalling pathway implicatingLyn and PI-3K in HL-60 cells and hematopoietic progenitors and SDF-induced cell migration is defective in Lyndeficient bone marrow cells [99].
PMID: 18385944, 11157475
SDF/CXCL12-induced cell migration in CXCR4 expressing pre-B lymphoma cells involves formation of complexes between CXCR4, the tyrosine phosphatase SHP2, Cbl and Fyn [102].
Indirect
PMID: 18385944, 11157475
SDF/CXCL12-induced cell migration in CXCR4 expressing pre-B lymphoma cells involves formation of complexes between CXCR4, the tyrosine phosphatase SHP2, Cbl and Fyn [102].
PMID: 18385944, 15955842
Chemoattractant receptor engagement in a T cell line induces Fyn-dependent PI-3K activation, and overexpression of a Fyn mutant form inhibits chemoattractant-induced cell migration [105].
PMID: 18385944, 15955842
Chemoattractant receptor engagement in a T cell line induces Fyn-dependent PI-3K activation, and overexpression of a Fyn mutant form inhibits chemoattractant-induced cell migration [105].
PMID: 18385944, 15955842
Chemoattractant receptor engagement in a T cell line induces Fyn-dependent PI-3K activation, and overexpression of a Fyn mutant form inhibits chemoattractant-induced cell migration [105].
PMID: 18385944, 15955842
Chemoattractant receptor engagement in a T cell line induces Fyn-dependent PI-3K activation, and overexpression of a Fyn mutant form inhibits chemoattractant-induced cell migration [105].
Indirect
PMID: 18385944, 15955842
Chemoattractant receptor engagement in a T cell line induces Fyn-dependent PI-3K activation, and overexpression of a Fyn mutant form inhibits chemoattractant-induced cell migration [105].
PMID: 18385944, 10747947
MIP-1b/CCL4-CCR5 interaction induces formation of a signaling complex which includes Syk [109].
PMID: 18385944, 10747947
MIP-1b/CCL4-CCR5 interaction induces formation of a signaling complex which includes Syk [109].
PMID: 18385944, 10547366, 15561106, 11149930
Pyk2 is a substrate of Hck and Fgr and interacts with Fgr in murine macrophages and Src in osteoclasts [32, 36, 41].
PMID: 18385944, 10547366, 15561106, 11149930
Pyk2 is a substrate of Hck and Fgr and interacts with Fgr in murine macrophages and Src in osteoclasts [32, 36, 41].
PMID: 18385944, 9687507, 12652654, 11149930
c-Cbl is a substrate of SFKs and interacts with Fgr and Lyn in murine macrophages and Src and Pyk2 in osteoclasts [31, 33, 41].
PMID: 18385944, 9687507, 12652654, 11149930
c-Cbl is a substrate of SFKs and interacts with Fgr and Lyn in murine macrophages and Src and Pyk2 in osteoclasts [31, 33, 41].
PMID: 18385944, 15561106
The Rho inhibitor p190RhoGAP associates with Pyk2 in murine macrophages and is a substrate of Hck and Fgr [36].
Indirect
Indirect
PMID: 18385944, 10547366, 15561106, 11149930
Pyk2 is a substrate of Hck and Fgr and interacts with Fgr in murine macrophages and Src in osteoclasts [32, 36, 41].
PMID: 18385944, 10547366, 15561106, 11149930
Pyk2 is a substrate of Hck and Fgr and interacts with Fgr in murine macrophages and Src in osteoclasts [32, 36, 41].
PMID: 18385944, 9687507, 12652654, 11149930
c-Cbl is a substrate of SFKs and interacts with Fgr and Lyn in murine macrophages and Src and Pyk2 in osteoclasts [31, 33, 41].
PMID: 18385944, 9687507, 12652654, 11149930
c-Cbl is a substrate of SFKs and interacts with Fgr and Lyn in murine macrophages and Src and Pyk2 in osteoclasts [31, 33, 41].
PMID: 18385944, 15561106
The Rho inhibitor p190RhoGAP associates with Pyk2 in murine macrophages and is a substrate of Hck and Fgr [36].
PMID: 18385944, 15561106
The Rho inhibitor p190RhoGAP associates with Pyk2 in murine macrophages and is a substrate of Hck and Fgr [36].
PMID: 18385944, 12094222
Vav proteins act as guanine nucleotide exchange factors (GEFs) for Rac and Cdc42 [122].
PMID: 18385944, 12094222
Vav proteins act as guanine nucleotide exchange factors (GEFs) for Rac and Cdc42 [122].
PMID: 18385944, 8805332, 12235133
WASp is a substrate of Hck and Fgr and tyrosine phosphorylated WASp exhibits an enhanced capability to trigger actin polymerization in macrophages [124, 125].
PMID: 18385944, 8805332, 12235133
WASp is a substrate of Hck and Fgr and tyrosine phosphorylated WASp exhibits an enhanced capability to trigger actin polymerization in macrophages [124, 125].
Indirect
PMID: 18385944, 8805332, 12235133
WASp is a substrate of Hck and Fgr and tyrosine phosphorylated WASp exhibits an enhanced capability to trigger actin polymerization in macrophages [124, 125].
PMID: 18385944, 10547366, 10657655
Paxillin, a cytoskeletal adaptor protein recruiting actin-binding and signalling proteins to integrin-based adhesion sites [126], is a substrate of SFKs in macrophages [32, 127, 128].
Indirect
PMID: 18385944, 11149930, 16313344
Notably, SFKs, Pyk2 and c-Cbl also form a molecular complex regulating osteoclast adhesion and migration [41, 42].
PMID: 18385944, 11283727
Although Syk binding to phosphorylated ITAM tyrosine residues of adaptor molecules is essential for full Syk activation and downstream signaling (reviewed in [12]), Syk interacts with SFKs, integrins and c-Cbl in leukocytes.
Indirect
PMID: 18385944, 17339487
The findings summarized above also suggest that implication of SFKs in trimeric G protein-coupled receptors signaling (Figure 1) has not relevance in the context of chemotactic migration, but other neutrophil responses to chemoattractants, such as degranulation [14, 16, 59, 64, 65] and ROIs generation [60].
PMID: 18385944
An early step in neutrophil-endothelium interaction is the binding of PSGL-1 with its endothelial counterreceptors P- and E-selectin.
Indirect
PMID: 18385944
Besides mediating leukocyte rolling, PSGL-1 triggers intracellular signals regulating interaction of b2 integrins with ICAM-1; his interaction mediates “slow rolling” and primes leukocytes for arrest on the endothelial surface.
Indirect
PMID: 18385944
Tyrosine phosphorylated Naf1 recruits the p85-p110delta isoform of PI3-kinase and this results in “inside-out” signals which are essential for full activation of the LFA-1 binding capacity by trimericGprotein-coupled chemoattractant receptors.
Indirect
PMID: 18385944
Altogether, these findings suggest that SFKs and Syk are implicated in selectin-mediated priming of neutrophil adhesion, recruitment and, potentially, in transcription of pro-inflammatory mediators.
Indirect
PMID: 18385944, 17339487, 8666673
It is important to note that SFKs regulate important neutrophil effector functions including superoxide anion generation (see [60, 77] and references contained therein) and degranulation.
Indirect
PMID: 18385944, 11937554, 12947983
Release of reactive oxygen intermediates or granule constituents may regulate expression of counterreceptors for leukocyte integrins by the vascular endothelium or tightness of the endothelial cell layer [86, 87].
PMID: 18385944, 15186216, 10547366, 15561106
Cortactin, an F-actin binding protein interacting with the Arp3 subunit of the Arp2/3 complex and regulating its actin-nucleating activity [129], is a substrate of Hck and Fgr in murine macrophages and Fgr-transfected cell lines [32, 36].
PMID: 18385944, 15186216, 10547366, 15561106
Cortactin, an F-actin binding protein interacting with the Arp3 subunit of the Arp2/3 complex and regulating its actin-nucleating activity [129], is a substrate of Hck and Fgr in murine macrophages and Fgr-transfected cell lines [32, 36].
PMID: 18385944, 15186216, 10547366, 15561106
Cortactin, an F-actin binding protein interacting with the Arp3 subunit of the Arp2/3 complex and regulating its actin-nucleating activity [129], is a substrate of Hck and Fgr in murine macrophages and Fgr-transfected cell lines [32, 36].
PMID: 18385944, 9687507, 12652654, 11149930
c-Cbl is a substrate of SFKs and interacts with Fgr and Lyn in murine macrophages and Src and Pyk2 in osteoclasts [31, 33, 41].
PMID: 18385944, 9687507, 12652654, 11149930
c-Cbl is a substrate of SFKs and interacts with Fgr and Lyn in murine macrophages and Src and Pyk2 in osteoclasts [31, 33, 41].
PMID: 18385944, 9687507, 12652654, 11149930
c-Cbl is a substrate of SFKs and interacts with Fgr and Lyn in murine macrophages and Src and Pyk2 in osteoclasts [31, 33, 41].
PMID: 18385944, 9687507, 12652654, 11149930
c-Cbl is a substrate of SFKs and interacts with Fgr and Lyn in murine macrophages and Src and Pyk2 in osteoclasts [31, 33, 41].
PMID: 18385944, 9687507
Notably, SFKs regulated not only c-Cbl tyrosine phosphorylation but also its capability to bind and redistribute a phosphatidylinositol 3-kinase (PI-3 kinase) activity to a detergent insoluble fraction [31].
PMID: 18385944, 15561106
In macrophages, the Rho inhibitor p190RhoGAP interacts with this complex via direct or indirect binding to Pyk2 [36].
PMID: 18385944, 9687507
Notably, SFKs regulated not only c-Cbl tyrosine phosphorylation but also its capability to bind and redistribute a phosphatidylinositol 3-kinase (PI-3 kinase) activity to a detergent insoluble fraction [31].
PMID: 18385944, 9687507
Notably, SFKs regulated not only c-Cbl tyrosine phosphorylation but also its capability to bind and redistribute a phosphatidylinositol 3-kinase (PI-3 kinase) activity to a detergent insoluble fraction [31].
PMID: 18385944, 11149930, 16313344
Notably, SFKs, Pyk2 and c-Cbl also form a molecular complex regulating osteoclast adhesion and migration [41, 42].
PMID: 18385944
As far as myeloid cells are concerned, Src was reported to bind to the b3 integrin in osteoclasts constitutively [11] and we found that Fgr and Hck associated with b1 in BMDM (unpublished observation).
PMID: 18385944
As far as myeloid cells are concerned, Src was reported to bind to the b3 integrin in osteoclasts constitutively [11] and we found that Fgr and Hck associated with b1 in BMDM (unpublished observation).
PMID: 18385944
An early step in neutrophil-endothelium interaction is the binding of PSGL-1 with its endothelial counterreceptors P- and E-selectin.