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Updated: Jun 21, 2026

Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques
Published on: November 2, 2018
Tyrosine phosphorylation of vinexin in v-Src-transformed cells attenuates the affinity for vinculin
Tsutomu Umemoto1, Kana Tanaka, Kazumitsu Ueda
1Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, Japan.
Abstract:
Vinexin is an adaptor-type focal adhesion protein that interacts with vinculin. Here, we report the tyrosine phosphorylation of vinexin alpha in v-Src-transformed NIH3T3 cells. Point mutational analysis of vinexin alpha clarified that three tyrosine residues in vinexin alpha were phosphorylated. A non-phosphorylatable mutant of vinexin alpha had higher binding affinity for vinculin than its wild-type counterpart. In conclusion, vinexin alpha is tyrosine phosphorylated in v-Src-transformed cells, and this tyrosine phosphorylation of vinexin alpha attenuates the association of vinexin alpha with vinculin.
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