| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| We now report that SH2D1A associates with Dok 1 , a protein that interacts with Ras GAP , Csk , and Nck . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Dok 4 and dok 5 do not associate with rasGAP or Nck , in contrast to p62dok and dok 2 . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| In both M 23 and MM 55 cells , HGF induces association with MET / HGFR and increased tyrosine phosphorylation of the SH 2 domain containing proteins PI3K , GAP and NCK . ^^^ We therefore suggest that the second messenger proteins PI3K , GAP and NCK , and possibly the protein products of the c fos , c jun , junB , junD and c myc genes , are important elements in the HGF induced mitogenic pathway in the normal mouse epithelial cell lines M 23 and MM55 . . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| By using antisera specific to other mediators of signal transduction that contain SH 2 domains for immunoprecipitation , it was demonstrated that VEGF promotes phosphorylation of phosphatidylinositol 3 kinase , Ras GTPase activating protein ( GAP ) , and the oncogenic adaptor protein NcK . ^^^ Tyrosine phosphorylated Nck , PLC gamma , and two GAP associated proteins , p 190 and p 62 , were in GAP immunoprecipitates of VEGF stimulated BAEC , and tyrosine phosphorylated NcK was in phosphatidylinositol 3 kinase immunoprecipitates . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| The SH 2 domains of PLC gamma Nterm . , Nck , Grb 2 , GAP and Abl have been model built with high affinity phosphopeptides fitted into the putative binding sites . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| We present evidence demonstrating that the Nck bound p 62 is related to the previously identified GTPase activating protein ( GAP ) associated phosphotyrosine protein p 62 . ( 1 ) The Nck bound and the GAP bound p 62 proteins co migrate with each other in SDS PAGE . ( 2 ) SH 2 domains from Nck and GAP compete for binding to p 62 in vitro . ( 3 ) Purified GST Nck SH 2 binds directly to the GAP associated p 62 . ^^^ Under these conditions , SH 2 domains from PLCgamma , PI 3 kinase , SHC , and Grb 2 did not bind p 62 . ( 4 ) Tryptic phosphopeptide maps of the Nck and the GAP associated p 62 proteins are identical . ^^^ However , Nck and GAP do not co immunoprecipitate with each other and apparently bind to different pools of p 62 . ^^^ This study suggests that the GAP associated p 62 acts as an SH 2 domain docking protein and mediates the interaction between Nck and EGF receptor in response to EGF stimulation . . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| The levels of PI 3 kinase , GLUT 4 , p 70 S6 kinase and Ras mRNA were significantly increased by 89 , 40 , 38 , and 47 % , respectively , with running training ; however , the Nck mRNA level was decreased by 24 % . mRNA levels of SHP 2 , Grb 2 , Sos , Shc , GAP , p 62 and p 90 S6 kinase were unaltered by running training . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Co expression of a FLAG epitope tagged form of DokR ( FLAG DokR ) with Lyn in embryonic kidney 293T cells resulted in constitutive phosphorylation of FLAG DokR on tyrosine residues and consequential physical association with RasGTPase activating protein ( GAP ) and the Nck adaptor protein . ^^^ The molecular basis of the interactions involving DokR with GAP and Nck was investigated using a novel glutathione S transferase fusion protein binding assay and / or site directed mutagenesis . ^^^ Tandem SH 2 binding sites containing Tyr 276 and Tyr 304 were shown to mediate binding of DokR to GAP , whereas Tyr 351 mediated the binding of DokR to Nck . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| In addition , GC GAP contains several classic proline rich motifs , and it interacts with the first SH 3 domain of Crk and full length Nck in vitro . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Nck encodes one SH 2 and three SH 3 domains , the Src homology motifs found in nonreceptor tyrosine kinases , Ras GTPase activating protein , phosphatidylinositol 3 kinase , and phospholipase C gamma . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| In addition , we demonstrate that phospholipase C gamma 1 , the p 85 subunit of phosphatidylinositol 3 ' kinase , Shc , Grb 2 , and Src family tyrosine kinases , but not Ras GTPase activating protein , Vav , or Nck , physically associate with the Flk2 / Flt3 cytoplasmic domain . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| The in vivo interaction with the EGFr / p185c neu heterodimer of several signal transduction proteins , including phospholipase C gamma 1 ( PLC gamma 1 ) , the p 85 subunit of phosphotidylinositol 3 kinase , the ras GTPase activating protein , SHC , NCK , p72RAF , and the tyrosine phosphatase SHPTP 2 , was measured by coimmunoprecipitation . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| The activated EphB 2 receptor induced the tyrosine phosphorylation of a 62 64 kDa protein ( p 62 [ dok ] ) , which in turn formed a complex with the Ras GTPase activating protein ( RasGAP ) and SH2 / SH3 domain adaptor protein Nck . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Tyrosine phosphorylation of p62Dok resulted in its complex formation with the Ras GTPase activating protein ( RasGAP ) and the Nck adaptor protein . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Multiple sites on Dok R were tyrosine phosphorylated following EGF stimulation ; phosphorylated Tyr 276 and Tyr 304 are proposed to dock the tandem Src homology 2 ( SH 2 ) domains of the p 21 ( Ras ) GTPase activating protein rasGAP and Tyr 351 mediates an association with the SH 2 domain of the adapter protein Nck . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Although it has been proposed to contribute to the control of cell growth and migration through association with the Ras GTPase activating protein and the adapter protein Nck , the role of Dok 1 remains largely unknown . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Insulin receptor mediated p62dok tyrosine phosphorylation at residues 362 and 398 plays distinct roles for binding GTPase activating protein and Nck and is essential for inhibiting insulin stimulated activation of Ras and Akt . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| It is rapidly tyrosine phosphorylated in response to receptor tyrosine activation and interacts with ras GTPase activating protein and Nck , leading to inhibition of ras signaling pathway activation and the c Jun N terminal kinase ( JNK ) and c Jun activation , respectively . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| We have investigated the roles of the phosphotyrosine phosphatase Syp ( also called SH PTP 2 ) , phospholipase C ( PLC ) gamma 1 , rasGTPase Activating Protein ( rasGAP ) and the adapter molecules Nck and Shc in the mitogenic response induced by PDGF in fibroblasts . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Thus , we examined the interactions of various SH 2 containing molecules like PLC gamma 1 , rasGAP , p 85 subunit of PI 3 kinase , Src , Fyn , Crk , Nck , Grb 2 and Shc with HEK 2 using in vitro binding assays , immunoprecipitations and yeast Two Hybrid assays . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| We show that coexpression of Dok R with activated Tek results in tyrosine phosphorylation of Dok R and that rasGAP and Nck coimmunoprecipitate with phosphorylated Dok R . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Insulin promoted the association of tyrosine phosphorylated Dok with the adapter protein NCK and rasGAP . ^^^ In contrast , a mutant Dok ( DokY361F ) , in which Tyr 361 was replaced by phenylalanine , failed to bind NCK but partially retained the ability to bind rasGAP in response to insulin . ^^^ These results identify Dok as a signal transducer that potentially links , through its interaction with NCK or rasGAP , cell adhesion and insulin receptors to the machinery that controls cell motility . . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Although pY 594 in the EphB1R has previously been shown to bind the SH 2 domain of Nck , we found that stimulation of EphB 1 and EphB 2 led predominantly to a complex between NIK / Nck , p 62 ( dok ) , RasGAP , and an unidentified 145 kDa tyrosine phosphorylated protein . ^^^ Tyrosine phosphorylated p 62 ( dok ) most probably binds directly to the SH 2 domain of Nck and RasGAP and indirectly to NIK bound to the SH 3 domain of Nck . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Furthermore , we demonstrate that p 62 ( dok ) can exert its negative effect on the PDGFR / MAPK pathway independently of its ability to associate with RasGAP and Nck . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| In support of this notion , we identify several SH 2 domain containing proteins , namely c Src , NCK , and Ras GAP , that interact with caveolin 2 in a phosphorylation dependent manner . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Tyrosine phosphorylation induces DokR to bind the signal relay molecules , RasGTPase activating protein ( RasGAP ) and Nck . ^^^ Here , we have examined the function of DokR during hematopoietic development and the requirement for RasGAP and Nck binding sites in its biological function . ^^^ Importantly , functional RasGAP and Nck binding sites were found to be essential for the biological effects of DokR in vitro and in vivo . . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Insulin receptor phosphorylated IRS5 / DOK4 associates with RasGAP , Crk , Src , and Fyn , but not phosphatidylinositol 3 kinase p 85 , Grb 2 , SHP 2 , Nck , or phospholipase Cgamma Src homology 2 domains , and activates MAPK in cells . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| These results implicate Dok 1 , Nck , Crk L , and Src kinases especially Lck , Pyk 2 , Zap 70 , Vav , and Ras GAP in intracellular signaling by SDF 1alpha / CXCL12 , and they suggest that Dok 1 plays an important role in SDF 1alpha / CXCL12 induced chemotaxis in T cells . . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Three SH 2 domain containing proteins , c Src , Nck , and Ras GAP , were found to associate with Cav 2 in a phosphorylation dependent manner . ^^^ |
|
| Interacting proteins: P20936 and P16333 |
Pubmed |
SVM Score :0.0 |
| Expression of a partially activated A Raf mutant resulted in decreased tyrosine phosphorylation of the PDGFR , specifically on Y 857 ( autophosphorylation site ) and Y 1021 ( phospholipase Cgamma 1 ( PLCgamma 1 ) binding site ) , but not the binding sites for other signalling proteins ( Nck , phosphatidylinositol 3 ' kinase ( PI3K ) , RasGAP , Grb 2 , SHP ) . ^^^ |
|