Article ID Journal Published Year Pages File Type
1933244 Biochemical and Biophysical Research Communications 2009 5 Pages PDF
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.

Related Topics
Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
Authors
, , , ,