Tyrosine phosphorylation of vinexin in v-Src-transformed cells attenuates the affinity for vinculin

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.