| Interacting proteins: O43294 and Q05397 |
Pubmed |
SVM Score :0.86675878 |
| Here we show that Hic 5 binds to focal adhesion kinase ( FAK ) by its N terminal domain , and is localized to focal adhesions by its C terminal LIM domains . 0.86675878^^^ |
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| Interacting proteins: O43294 and Q05397 |
Pubmed |
SVM Score :0.70861893 |
| Interestingly , the interaction of Hic 5 with FAK was regulated by specific cysteines near the binding site and decreased in cells under oxidative conditions . 0.70861893^^^ |
|
| Interacting proteins: O43294 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In addition , GST hic 5 precipitates the focal adhesion kinase pp 125 ( FAK ) and talin from platelet extracts . ^^^ |
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| Interacting proteins: O43294 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Although Hic 5 was originally characterized as a TGF beta inducible gene and proposed to be a transcription factor involved in senescence , the studies here demonstrate that Hic 5 is localized to focal adhesion in REF 52 cells and can interact with the focal adhesion proteins , Fak , Frnk , and vinculin . ^^^ |
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| Interacting proteins: O43294 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Hic 5 is also known to associate with focal adhesion kinase ( FAK ) or the related CAKbeta , and with vinculin . ^^^ Mouse Hic 5 contains three LD domains in its N terminal half , and the first LD domain ( LD 1 ) appears to be involved in interaction with FAK . ^^^ However , this interaction was not essential for recruitment of Hic 5 to focal adhesions , since its subcellular localization was similar in FAK ( / ) cells . ^^^ Forced expression of Hic 5 decreased colony forming ability of MEF from FAK ( + / + ) mice , but not of FAK ( / ) cells . ^^^ |
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| Interacting proteins: O43294 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Here we show that overexpression of CAKbeta or Fyn , but not FAK , enhanced the tyrosine phosphorylation of coexpressed Hic 5 in COS 7 cells . ^^^ |
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| Interacting proteins: O43294 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Hic 5 and paxillin share structural homology and interacting factors such as focal adhesion kinase ( FAK ) , Pyk2 / CAKbeta / RAFTK , and PTP PEST . ^^^ The overexpression of Hic 5 sequestered FAK from paxillin , reduced tyrosine phosphorylation of paxillin and FAK , and prevented paxillin Crk complex formation . ^^^ In addition , Hic 5 mediated inhibition of spreading was not observed in mouse embryo fibroblasts ( MEFs ) derived from FAK ( / ) mice . ^^^ The activity of c Src following fibronectin stimulation was decreased by about 30 % in Hic 5 expressing cells , and the effect of Hic 5 was restored by the overexpression of FAK and the constitutively active forms of Rho family GTPases , Rac 1 V12 and Cdc 42 V12 , but not RhoA V 14 . ^^^ These observations suggested that Hic 5 inhibits cell spreading through competition with paxillin for FAK and subsequent prevention of downstream signal transduction . ^^^ |
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| Interacting proteins: O43294 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We showed that cyclic strain ( CS ) of osteoblastic cells induced tyrosine phosphorylation of two homologous tyrosine kinases FAK and PYK 2 , and of two homologous adaptor proteins paxillin and Hic 5 , with similar kinetics . ^^^ While FAK and paxillin remained at the focal contact , Hic 5 and PYK 2 translocated outside ventral focal contacts as early as 30 min after CS and were sequestered by the cytoskeleton . ^^^ Co immunoprecipitation showed that the association of PYK2 / Hic 5 and PYK2 / FAK increased with time after strain while that of paxillin and Hic 5 decreased . ^^^ Altogether these results suggested that CS regulates focal contact activity in osteoblasts by modulating PYK 2 containing complexes in particular by shuttling out of the focal contact the adaptor Hic 5 and favoring the anchorage of FAK within contacts . . ^^^ |
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| Interacting proteins: O43294 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O43294 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
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