Caveolin-1 (Cav-1), the principal protein component of caveolar membrane domains (Glenney, Jr. and Soppet, 1992; Kurzchalia et al., 1992; Rothberg et al., 1992), was originally identified as a major tyrosine phosphoprotein in Rous sarcoma virus (v-Src) transformed cells (Glenney, Jr. and Zokas, 1989). Although Cav-1 can be phosphorylated on several tyrosine residues (Nomura and Fujimoto, 1999; Schlegel et al., 2001), the most well-characterized phosphorylation site on Cav-1 is tyrosine-14, a site specifically recognized by monoclonal antibodies developed to detect this phosphorylated residue (Lee et al., 2000; Nomura and Fujimoto, 1999).
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Elliott, M.H., Ghalayini, A.J. (2008). Phosphorylation of Caveolin-1 in Bovine Rod Outer Segments in vitro by an Endogenous Tyrosine Kinase. In: Anderson, R.E., LaVail, M.M., Hollyfield, J.G. (eds) Recent Advances in Retinal Degeneration. Advances in Experimental Medicine and Biology, vol 613. Springer, New York, NY. https://doi.org/10.1007/978-0-387-74904-4_39
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