| Interacting proteins: Q14451 and Q05397 |
Pubmed |
SVM Score :0.95760329 |
| Here , we report that the SH 2 domain of Grb 7 can directly interact with FAK through Tyr 397 , a major autophosphorylation site in vitro and in vivo . 0.95760329^^^ |
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| Interacting proteins: Q14451 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We have previously described Grb 7 association with focal adhesion kinase ( FAK ) and its possible roles in cell migration . ^^^ In this paper , we investigated the mechanisms by which Grb 7 and its association with FAK regulate cell migration . ^^^ We also found that Grb 7 could be phosphorylated by FAK , which was dependent on the FAK kinase activity but not the presence of the Src family kinases . ^^^ Cell adhesion also enhanced Grb 7 phosphorylation in FAK+ / + cells but not FAK / cells , suggesting that Grb 7 is a physiological substrate of FAK . ^^^ Furthermore , both Grb 7 and the chimeric molecule did not increase migration of FAK / cells , although the chimeric molecule was targeted to the focal contacts . ^^^ |
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| Interacting proteins: Q14451 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The ability of FAK to mediate integrin signaling in the regulation of cell cycle progression depends on the phosphorylation of Tyr 397 , which implies a functional significance for the formation of FAK signaling complexes with Src , phosphatidylinositol 3 kinase ( PI3K ) and Grb 7 . ^^^ We also show that mutation of D 395 to A disrupted FAK association with Grb 7 . ^^^ This suggests that a FAK / Grb7 complex is not involved in the cell cycle regulation either , which is supported by direct analysis of cells expressing a dominant negative Grb 7 construct . ^^^ |
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| Interacting proteins: Q14451 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Differential regulation of cell migration and cell cycle progression by FAK complexes with Src , PI3K , Grb 7 and Grb 2 in focal contacts . ^^^ |
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| Interacting proteins: Q14451 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Grb 7 has been implicated as a downstream mediator of integrin FAK signal pathways in the regulation of cell migration , although the molecular mechanisms are still not well understood . ^^^ It was also shown to be necessary for Grb 7 phosphorylation by FAK , although it was not required for Grb 7 interaction with FAK or recruitment to the focal contacts . ^^^ In addition , both FAK binding to PI 3 kinase via its autophosphorylated Tyr ( 397 ) and integrin mediated cell adhesion increased Grb 7 association with phosphoinositides . ^^^ Together , these results identified the Grb 7 PH domain interaction with phosphoinositides and suggested a potential mechanism by which several signaling molecules including Grb 7 , FAK , and PI 3 kinase and their interactions cooperate to mediate signal transduction pathways in integrin mediated cell migration . . ^^^ |
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| Interacting proteins: Q14451 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Recent studies have suggested that various isoforms of Grb 10 play important roles in mediating insulin / insulin like growth factor regulation of cell proliferation and apoptosis , whereas Grb 7 mediates signaling pathways from FAK and EphB 1 receptor to regulate cell migration , which is also implicated in tumor progression . ^^^ |
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| Interacting proteins: Q14451 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Increased phosphorylation of Grb 7 and its upstream signaling protein , focal adhesion kinase ( FAK ) , was detected in low viability eosinophils such as those from healthy donors or in cultured eosinophils ( AML14 . 3D10 cells ) treated with dexamethasone . ^^^ |
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