caveolin-2 Background Information Two major coat proteins, caveolin-1 and -2, interact near focal adhesions in the plasma membrane, where they function in the formation of caveolae and negative regulation of signal molecules localizing therein. The phosphorylation of caveolin-2 regulates this activity via three important sites: serine residues 23 and 36, and tyrosine residue 19. Mutation of the serine residues reduces the number of plasmalemma-attached caveolae and increases the accumulation of noncoated vesicles, but does not effect the interaction with caveolin-1. In contrast, phosphorylation of tyrosine 19 leads to dissociation of caveolin-2 from caveolin-1, though it still does not effect caveolin-2 localization. Rather caveolin-2 Tyr19(P) remains near focal adhesions, where it may function as a docking site for SH2 domain containing proteins to regulate signal transduction.
p-caveolin-2 (Tyr 19)-R
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p-caveolin-2 (Tyr 19)-R: sc-27998-R. Western blot analysis of caveolin-2 phosphorylation in rat skeletal muscle tissue extract.
