Phosphorylation of Hic-5 at tyrosine 60 by CAKβ and Fyn

被引：30

作者：

Ishino, M ^{[1
]}

Aoto, H ^{[1
]}

Sasaski, H ^{[1
]}

Suzuki, R ^{[1
]}

Sasaki, T ^{[1
]}

机构：

[1] Sapporo Med Univ, Sch Med, Inst Canc Res, Dept Biochem,Chuo Ku, Sapporo, Hokkaido 0608556, Japan

来源：

FEBS LETTERS | 2000年 / 474卷 / 2-3期

关键词：

cell adhesion kinase beta; Fyn; Hic-5; tyrosine phosphorylation; osmotic stress;

D O I：

10.1016/S0014-5793(00)01597-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Hic-5 is a CAK beta-binding protein localized at focal adhesions. Here we show that overexpression of CAK beta or Fyn, but not FAK, enhanced the tyrosine phosphorylation of coexpressed Hic-5 in COS-7 cells, These phosphorylations were further augmented by stimulating cells with osmotic stress. The Y60F mutant of Hic-5 was not phosphorylated, and Hic-5 phosphorylated on tyrosine 60 was bound specifically to the SH2 domain of Csk. Coexpression experiments revealed that the phosphorylation of Hic-5 by CAK beta required the kinase activation of CAK beta and binding of Hic-5 by CAB beta. Specific phosphorylation of Hic-5 by CAK beta and Fyn mag activate a signaling pathway mediated by Hic-5. (C) 2000 Federation of European Biochemical Societies.

引用

页码：179 / 183

页数：5

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