| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.92284904 |
| Csk formed a complex with the focal adhesion protein paxillin in cells , and its SH 2 domain was shown to interact with pp125FAK and paxillin in vitro . 0.92284904^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.94249842 |
| We therefore suggest that the competitive binding of overexpressed 5 Crk affects an efficient interaction of Csk with tyrosine phosphorylated paxillin in CT 10 transformed CEF . 0.94249842^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.6900855 |
| Although we have shown that the Csk Src homology 2 domain can bind to several tyrosine phosphorylated proteins , including pp125FAK and paxillin , a majority of protein which bound to Csk was IRS 1 when cells were stimulated by insulin . 0.6900855^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.64953192 |
| The Csk homologous kinase , Chk , binds tyrosine phosphorylated paxillin in human blastic T cells . 0.64953192^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| While PLD activity as a lipid hydrolyzing enzyme is not affected by c Src , wild type PLDs but not catalytically inactive PLD mutants significantly increase c Src kinase activity , up regulating c Src mediated paxillin phosphorylation and extracellular signal regulated kinase activity . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| In normal fibroblasts , tyrosine phosphorylated paxillin and focal adhesion kinase pp125FAK , which colocalize at focal adhesion plaques , were the major proteins to which the Csk SH 2 domain bound . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of paxillin on tyrosine creates binding sites for the SH 2 domains of Crk , Csk , and Src . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| Paxillin has also been implicated in cell signaling by virtue of its association with the protein tyrosine kinases pp60src and Csk ( C terminal Src kinase ) as well as with the adapter / oncoprotein p47gag crk . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| Paxillin physically complexes with two protein tyrosine kinases , pp60src and Csk ( COOH terminal src kinase ) , and the oncoprotein p47gag crk , each of which could function as part of a paxillin signaling complex . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| Paxillin is tyrosine phosphorylated during interphase of the cell cycle by protein tyrosine kinases ( PTK ) such as c Src and Csk , and becomes dephosphorylated during mitosis . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| While overexpression of Csk or the Csk mutants did not significantly affect cell adhesion to the Fn surface or alpha 5 integrin recruitment to the attachment sites , Csk suppressed and mCsk almost abolished Fn mediated tyrosine phosphorylation of paxillin , filamentous actin assembly to podosomes , and cell migration , but mCsk ( ) did not . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| In addition , paxillin , a Src and / or pp 125 ( FAK ) substrate , displayed increased levels of tyrosine phosphorylation in PTPalpha expressing cells and was associated with elevated amounts of Csk . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| In addition , like paxillin , Hic 5 can bind to a negative regulator of Src PTKs , csk but does not bind to the adaptor protein Crk . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| On the other hand , overexpression of Csk DeltaK induced tyrosine phosphorylation of cellular proteins , including the paxillin and focal adhesion kinase ( FAK ) and enhanced to some extent the cytoskeletal organization and the rate of cell spreading on fibronectin , indicating that Src or its relatives was functionally activated in the cells . ^^^ Paxillin was also tyrosine phosphorylated in Csk overexpressing cells , indicating that it can serve as a substrate of Csk . ^^^ The phosphorylation state of paxillin in cells overexpressing Csk was indistinguishable from that in cells expressing Csk DeltaK in that both phosphorylated paxillins bound equally to SH 2 domain of Csk and were co immunoprecipitated with Csk . ^^^ These findings suggest that Csk regulates Src family tyrosine kinases that play essential roles in the regulation of cell adhesion via a FAK dependent mechanism and that the tyrosine phosphorylation of paxillin alone may not be sufficient for the regulation of the cell adhesion mechanism in astrocytes . . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| SHP 2 dephosphorylated paxillin and caused dissociation of Csk , a negative regulator of Src , from paxillin but had no effect on paxillin Src association . ^^^ Together , these results reveal that Gab 1 recruits SHP 2 to dephosphorylate paxillin , leading to dissociation of Csk from the paxillin Src complex and Src activation and that Src is an SHP 2 effector involved in EGF stimulated Erk activation and cell migration . . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| Hyperphosphorylation of key signaling proteins such as Syk and Paxillin in mutant granulocytes further supported breakdown of the activation threshold set by Csk . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| Oxidative stress activates both Src kinases and their negative regulator Csk and induces phosphorylation of two targeting proteins for Csk : caveolin 1 and paxillin . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| The peptide attenuated shear induced association of Csk at beta 1 integrin sites , as well as colocalization of Csk with paxillin and phosphorylated caveolin 1 . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| In addition , negative regulators of these pathways , including CSK ( an inhibitor of SRC activity ) and PTP PEST ( a phosphatase that dephosphorylates p130Cas ) , bind directly to paxillin , thereby bringing them into close proximity with their targets . ^^^ Abbreviations : CAS , CRK associated substrate ; CH , calponin homology domain ; CSK , C terminal SRC kinase ; E 6 , Papillomavirus E 6 protein ; FAK , focal adhesion kinase ; GIT , GRK interacter ; GPCR , heterotrimeric G protein coupled receptor ; GRK , G protein coupled receptor kinase ; MAPK , mitogen activated protein kinase ( ERK , p 38 , JNK ) ; PAK , p 21 activated kinase ; PBS , paxillin binding subdomain ; PIX , PAK interacting exchange factor ; PKL , paxillin kinase linker ; POR 1 , partner of Rac ; PS , phosphoserine ; PT , phosphothreonine ; PY , phosphotyrosine ; RTK , growth factor receptor tyrosine kinase ; SH , SRC homology domain . . ^^^ |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P41240 and P49023 |
Pubmed |
SVM Score :0.0 |
| NA |
|