Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2133007 | Experimental Cell Research | 2007 | 14 Pages |
Src controls the dynamic actin cytoskeleton in fibroblasts and in cancer cells, although it is not known how direct its effects are. Using FRET/FLIM imaging, we found that wild type Src associates directly, or indirectly, with peripheral β-actin at integrin adhesions after serum stimulation, and that an active Src kinase domain is essential. β-Actin can be directly tyrosine-phosphorylated by Src in vitro, and in a Src-dependent manner in cells. Moreover, β-actin dynamics are suppressed when Src is rendered kinase-inactive. Surprisingly, debilitating mutations in the Src SH2 or SH3 domains do not suppress association of Src with β-actin. This may therefore be an example of a spatially regulated Src kinase/substrate interaction that is controlling peripheral actin dynamics. Interestingly, there is no FRET between Src and β-actin at cadherin-mediated cell–cell contacts, despite apparent co-localization there, demonstrating precise spatial specificity of Src/β-actin complexes.