Does tyrosine phosphorylation of cortactin by the FAK-Src complex at focal adhesions regulate cell motility?
Our results suggest that cortactin acts as a bridging molecule between actin filaments and focal adhesions. The cortactin N-terminus associates with F-actin, while its C-terminus interacts with focal adhesions. The tyrosine phosphorylation of cortactin by the FAK-Src complex modulates its interaction with FAK and increases its turnover at focal adhesions to promote cell motility.
Eyes with RPD have significantly larger areas of choriocapillaris non-perfusion compared to eyes with drusen and no RPD. The correlation between PCAN and VA in this RPD population provides a potential mechanistic explanation for vision compromise in RPD compared to other forms of drusen in AMD.