Caveolins make up a family of proteins that are principal structural components of hairpin-like domains in the plasma membrane (1). It is believed that caveolins serve as scaffolding proteins for the integration of signal transduction. Three members of caveolins (caveolin-1, -2 and -3) have been identified, possessing different tissue distributions (2). Caveolins interact with multiple signaling molecules, such as the G-protein alpha subunit (1), tyrosine kinase receptors, PKCs, Src family tyrosine kinases and eNOS (2,3). Caveolin-1 has been implicated in the pathogenesis of mammary epithelial cell hyperplasia (4). Endothelial cell (EC) migration is a critical event during multiple physiological and pathological processes. The phosphorylatable Tyr14 residue of caveolin-1 is required for polarization of the protein during transmigration but does not alter polarization during planar movement.
EGFR1 Signaling Pathway
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