FEBS Letters | |
Phosphorylation of Hic‐5 at tyrosine 60 by CAKβ and Fyn | |
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
【 预 览 】
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RO201912020309415ZK.pdf | 174KB | download |