Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527.

摘要: We have characterized the mechanism by which subcellular distribution of c-Src is controlled phosphorylation tyrosine 527. Mutation this dramatically redistributes from endosomal membranes to focal adhesions. Redistribution adhesions occurs independently kinase activity and cellular transformation. In cells lacking regulatory (CSK) that phosphorylates 527, also found predominantly in adhesions, confirming 527 affects location inside cell. The first 251 amino acids are sufficient allow association with indicating at least one signal for positioning resides amino-terminal half. Point mutations deletions reveal requires myristylation site needed membrane attachment, as well SH3 domain. Expression region alters both structural biochemical properties Focal containing non-catalytic portion larger exhibit increased levels phosphotyrosine staining. Our results suggest may regulate adhesion a kinase-independent mechanism.