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Figure 7


Fig. 7. FAK interacts preferentially with tyrosine phosphorylated paxillin in vitro and in vivo. Purified GST-fusion proteins of wild-type, phosphomimetic (Y2E) or non-phosphorylatable (Y2F) paxillin were used to pull down proteins from equal amounts of endothelial cell extract, followed by western blotting for FAK. A representative blot is shown (A) as well as quantification of the mean (± s.e.) of four separate pull-down experiments (B). Localization of phosphorylated FAK (Y397) was examined by staining in PAECs expressing mutant paxillin alongside non-transfected (N.T) neighboring cells. Images in C are colored according to an intensity scale, as indicated. For convenience of comparison, squares mark adhesions in transfected and non-transfected neighboring cells. (D) Eight transfected or non-transfected cells were segmented and the intensity of pYFAK (means ± s.d.) in each adhesion was calculated. Bar, 5 µm.





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