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In Rucaparib transformed by active Src or v-Src, focal adhesions are often disorganized, in part due to the elevated tyrosine phosphorylation of focal adhesion proteins. This leads to increased turnover of the adhesion structure and eventual elevated motility [13] and [14]. In addition, tyrosine phosphorylation of focal adhesion proteins has been reported to promote the formation of invasive structures known as invadopodia or podosomes [15], [16], [17], [18] and [19]. From these observations, it is clear that tyrosine phosphorylation of focal adhesion proteins has important roles in the acquisition of increased motility and invasive potential in tumor cells; however, the functions of tyrosine phosphorylation of these proteins in the regulation of biochemical properties, such as an affinity to their binding partners, are not fully understood.
In this study, we demonstrated that vinexin α is tyrosine phosphorylated in v-Src-transformed cells. Point mutational analysis clarified that at least three tyrosine residues of vinexin α are tyrosine phosphorylated and that blockage of tyrosine phosphorylation by mutations increased the binding affinity of vinexin α to vinculin.