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

FEBS Letters

Ishino, Masaho¹  Sasaski, Hiroko¹  Sasaki, Terukatsu¹  Suzuki, Rumiko¹  Aoto, Hiroshi¹ 

[1] Department of Biochemistry, Cancer Research Institute, Sapporo Medical University School of Medicine, South-1, West-17, Chuo-Ku, Sapporo 060-8556, Japan

关键词: Cell adhesion kinase β;    Fyn;    Hic-5;    Tyrosine phosphorylation;    Osmotic stress;    CAKβ;    cell adhesion kinase β;    FAK;    focal adhesion kinase;    SH;    Src homology;    Csk;    C-terminal Src kinase;    GST;    glutathione S-transferase;   

DOI  :  10.1016/S0014-5793(00)01597-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Hic-5 is a CAKβ-binding protein localized at focal adhesions. Here we show that overexpression of CAKβ 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 CAKβ required the kinase activation of CAKβ and binding of Hic-5 by CAKβ. Specific phosphorylation of Hic-5 by CAKβ and Fyn may activate a signaling pathway mediated by Hic-5.

【 授权许可】

Unknown