Phosphorylation of Hic-5 at tyrosine 60 by CAKbeta and Fyn.
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Ishino M, Aoto H, Sasaski H, Suzuki R, Sasaki T
Phosphorylation of Hic-5 at tyrosine 60 by CAKbeta and Fyn.
FEBS Lett. 2000 Jun 2;474(2-3):179-83.
- PubMed ID
- 10838081 [ View in PubMed]
- Abstract
Hic-5 is a CAKbeta-binding protein localized at focal adhesions. Here we show that overexpression of CAKbeta 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 CAKbeta required the kinase activation of CAKbeta and binding of Hic-5 by CAKbeta. Specific phosphorylation of Hic-5 by CAKbeta and Fyn may activate a signaling pathway mediated by Hic-5.