Caveolins (Caveolin 1, 2, and 3) are a family of caveolae-associated integral membrane proteins. Caveolae are cholesterol/sphingolipid-rich microdomains of the plasma membrane that have been implicated in signal transduction and vesicular trafficking (1). Caveolin 2 is a principal component of caveolae membranes. It interacts directly with heterotrimeric guanine nucleotide binding proteins (G proteins) and can functionally regulate their activity. Caveolins 1 and 2 are similar in most respects; however, they differ in their functional interactions with heterotrimeric G proteins, possibly explaining why Caveolin-1 and -2 are coexpressed within a single cell (2). Caveolin-2 is up-regulated in response to the mechanical injury of differentiated PC12 cells, which is strictly dependent on continued treatment with NGF. Both Caveolin-1 and -2 are more abundantly expressed in white adipose tissue and are induced during adipocyte differentiation. Robust expression of Caveolin-1 and -2 is also observed along the entire cell surface of DRG neurons, including high levels on growth cones (1). Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3 (2).
EGFR1 Signaling Pathway
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Flow cytometric analysis of permeabilized HUVEC cells, untreated (green) or pervanadate-treated (red) using anti-Caveolin 2 Phospho (pY19) RabMAb, and pervanadate-treated HUVEC cells using the same antibody preincubated with phospho-Caveolin 2 Phospho (pY19) peptide (blue) or non-phospho-Caveolin 2 Phospho (pY19) peptide (orange).
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