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Abl kinase interacts with and phosphorylates vinexin
Author(s) -
Mitsushima Masaru,
Takahashi Honami,
Shishido Tomoyuki,
Ueda Kazumitsu,
Kioka Noriyuki
Publication year - 2006
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/j.febslet.2006.06.072
Subject(s) - microbiology and biotechnology , signal transducing adaptor protein , abl , phosphorylation , tyrosine phosphorylation , actin cytoskeleton , sh3 domain , tyrosine kinase , proto oncogene tyrosine protein kinase src , signal transduction , chemistry , biology , cytoskeleton , biochemistry , cell
Non‐receptor tyrosine kinase Abl is a well known regulator of the actin‐cytoskeleton, including the formation of stress fibers and membrane ruffles. Vinexin is an adapter protein consisting of three SH3 domains, and involved in signal transduction and the reorganization of actin cytoskeleton. In this study, we found that vinexin α as well as β interacts with c‐Abl mainly through the third SH3 domain, and that vinexin and c‐Abl were colocalized at membrane ruffles in rat astrocytes. This interaction was reduced by latrunculin B, suggesting an F‐actin‐mediated regulatory mechanism. We also found that vinexin α but not β was phosphorylated at tyrosine residue when c‐Abl or v‐Abl was co‐expressed. A mutational analysis identified tyrosine 127 on vinexin α as a major site of phosphorylation by c‐ or v‐Abl. These results suggest that vinexin α is a novel substrate for Abl.