Abstract
Caveolin-1 was first identified as an approximately 22-kDa tyrosine-phosphorylated protein in Rous sarcoma virus-transformed cells (Glenney, 1989; Glenney and Soppet, 1992). Caveolin-1 has subsequently attracted much attention because it serves as a major coat protein of caveolae (Rothberg, et al., 1992; Smart, et al., 1999). The caveolar membrane system, comprising plasma membrane invaginations and juxtamembrane uncoated vesicles, mediates certain protein transport processes, including transcytosis, potocytosis, and clathrin-independent endocytosis (Anderson, 1998). Caveolin-1 and caveolae are also involved in mediating cellular cholesterol efflux (Smart et al., 1999; Fielding and Fielding, 2001), and a large body of evidence implicates caveolin-1 in regulating intracellular signaling pathways.
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© 2005 Humana Press Inc., Totowa, NJ
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Liscovitch, M., Burgermeister, E., Jain, N., Ravid, D., Shatz, M., Tencer, L. (2005). Caveolin and Cancer. In: Mattson, M.P. (eds) Membrane Microdomain Signaling. Humana Press. https://doi.org/10.1385/1-59259-803-X:161
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DOI: https://doi.org/10.1385/1-59259-803-X:161
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