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Phosphorylation of Hic‐5 at tyrosine 60 by CAKβ and Fyn
Author(s) -
Ishino Masaho,
Aoto Hiroshi,
Sasaski Hiroko,
Suzuki Rumiko,
Sasaki Terukatsu
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01597-0
Subject(s) - fyn , phosphorylation , tyrosine phosphorylation , sh2 domain , tyrosine , microbiology and biotechnology , proto oncogene tyrosine protein kinase src , chemistry , tyrosine kinase , sh3 domain , signal transduction , biology , biochemistry
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.