Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1933244 | Biochemical and Biophysical Research Communications | 2009 | 5 Pages |
Abstract
Vinexin is an adaptor-type focal adhesion protein that interacts with vinculin. Here, we report the tyrosine phosphorylation of vinexin α in v-Src-transformed NIH3T3 cells. Point mutational analysis of vinexin α clarified that three tyrosine residues in vinexin α were phosphorylated. A non-phosphorylatable mutant of vinexin α had higher binding affinity for vinculin than its wild-type counterpart. In conclusion, vinexin α is tyrosine phosphorylated in v-Src-transformed cells, and this tyrosine phosphorylation of vinexin α attenuates the association of vinexin α with vinculin.
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Authors
Tsutomu Umemoto, Kana Tanaka, Kazumitsu Ueda, Noriyuki Kioka,