| Interacting proteins: P07949 and Q05397 |
Pubmed |
SVM Score :0.0 |
| These results suggested the presence of Rho dependent and independent signaling pathways downstream of PI 3 ' kinase that mediate tyrosine phosphorylation of FAK , paxillin and p130Cas through Ret kinase . . ^^^ |
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| Interacting proteins: P07949 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Expression and phosphorylation of Ret , activation of focal adhesion kinase ( FAK ) and mitogen associated protein kinase ( MAPK ) signaling pathways , and phosphorylation of paxillin by GDNF were investigated by immunoprecipitation and Western blot analysis in primary human corneal epithelial cells and a corneal epithelial cell line . ^^^ Herbimycin A strongly inhibited the activation of Ret , FAK , c Raf , and Erk 1 and 2 ; the phosphorylation of paxillin ; and corneal epithelial cell migration . ^^^ |
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| Interacting proteins: P07949 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Association of NCAM with GFRalpha 1 , a GPI anchored receptor for GDNF , downregulates NCAM mediated cell adhesion and promotes high affinity binding of GDNF to p 140 ( NCAM ) , resulting in rapid activation of cytoplasmic protein tyrosine kinases Fyn and FAK in cells lacking RET , a known GDNF signaling receptor . ^^^ |
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| Interacting proteins: P07949 and Q05397 |
Pubmed |
SVM Score :0.0 |
| RET activation in other cell types has been shown to cause phosphorylation of the focal adhesion associated proteins focal adhesion kinase ( FAK ) , paxillin , and p 130 ( CAS ) . ^^^ |
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| Interacting proteins: P07949 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In cells lacking RET , GDNF binds with high affinity to the NCAM and GFRalpha 1 complex , which activates Fyn and FAK . . ^^^ |
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| Interacting proteins: P07949 and Q05397 |
Pubmed |
SVM Score :0.0 |
| BACKGROUND : The RET proto oncogene is implicated in medullary thyroid cancer ( MTC ) and has been shown to signal indirectly to focal adhesion kinase ( FAK ) in cell types other than MTC . ^^^ We hypothesized that inhibition of RET with pharmacologic inhibitors or by depletion with siRNA would decrease FAK phosphorylation in MTC cells , thereby implicating a RET FAK signaling pathway . ^^^ RESULTS : Treatment of MTC cells with the inhibitor PP 2 significantly inhibited RET phosphorylation and , to a lesser extent , FAK phosphorylation . ^^^ RET siRNA significantly decreased RET expression and FAK phosphorylation . ^^^ CONCLUSIONS : RET signals through FAK in MTC cells . ^^^ |
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| Interacting proteins: P07949 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We have previously shown that RET signals through focal adhesion kinase ( FAK ) in medullary thyroid cancer cells and that extracellular signal regulated kinase ( ERK ) activity can be blocked by pp 2 , an inhibitor of both Src and RET . ^^^ We hypothesized that RET could directly phosphorylate FAK and ERK . ^^^ RESULTS : Immunoprecipitated , mutant RET from cells or the recombinant RET kinase domain was able to directly phosphorylate tyrosine residues on FAK . ^^^ Specifically Y576 / 577 , Y 861 , and Y 925 , but not the autophosphorylation site Y 397 of FAK , were phosphorylated by RET . ^^^ CONCLUSIONS : RET directly phosphorylates tyrosine residues on FAK , ERK 1 / 2 , DOK 1 , the p 85 subunit of of phosphatidylinositol 3 ' kinase , JNK 1 and 2 , P 38 , and phospholipase gamma . ^^^ |
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