Src kinase activity and SH2 domain regulate the dynamics of Src association with lipid and protein targets.

ABSTRACT: Src functions depend on its association with the plasma membrane and with specific membrane-associated assemblies. Many aspects of these interactions are unclear. We investigated the functions of kinase, SH2, and SH3 domains in Src membrane interactions. We used FRAP beam-size analysis in live cells expressing a series of c-Src-GFP proteins with targeted mutations in specific domains together with biochemical experiments to determine whether the mutants can generate and bind to phosphotyrosyl proteins. Wild-type Src displays lipid-like membrane association, whereas constitutively active Src-Y527F interacts transiently with slower-diffusing membrane-associated proteins. These interactions require Src kinase activity and SH2 binding, but not SH3 binding. Furthermore, overexpression of paxill

SUBMITTER: Shvartsman DE 

PROVIDER: S-EPMC2064473 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature