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Palmitoylation of caveolin-1 at a single site (Cys-156) controls its coupling to the c-Src tyrosine kinase: targeting of dually acylated molecules (GPI-linked, transmembrane, or cytoplasmic) to caveolae effectively uncouples c-Src and caveolin-1 (TYR-14).
Lee H, Woodman SE, Engelman JA, Volonté D, Galbiati F, Kaufman HL, Lublin DM, Lisanti MP. Lee H, et al. Among authors: lublin dm. J Biol Chem. 2001 Sep 14;276(37):35150-8. doi: 10.1074/jbc.M104530200. Epub 2001 Jul 12. J Biol Chem. 2001. PMID: 11451957 Free article.
The dually acylated NH2-terminal domain of gi1alpha is sufficient to target a green fluorescent protein reporter to caveolin-enriched plasma membrane domains. Palmitoylation of caveolin-1 is required for the recognition of dually acylated g-protein alpha subunits in vivo.
Galbiati F, Volonte D, Meani D, Milligan G, Lublin DM, Lisanti MP, Parenti M. Galbiati F, et al. Among authors: lublin dm. J Biol Chem. 1999 Feb 26;274(9):5843-50. doi: 10.1074/jbc.274.9.5843. J Biol Chem. 1999. PMID: 10026207 Free article.
94 results