Regular ArticlePalmitoylation of Muscarinic Acetylcholine Receptor m2 Subtypes: Reduction in Their Ability to Activate G Proteins by Mutation of a Putative Palmitoylation Site, Cysteine 457, in the Carboxyl-Terminal Tail☆
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2014, Advances in Insect PhysiologyCitation Excerpt :Changes in the palmitoylation state of GPCRs have been shown to markedly influence receptor coupling to G proteins (for a review, see: Chini and Parenti, 2009). Several studies have indicated palmitoylation of the cytoplasmic tail as necessary for normal receptor coupling to particular G proteins (Hayashi and Haga, 1997; Hukovic et al., 1998; O’Dowd et al., 1989; Sachs et al., 2000). The mechanisms underlying the uncoupling can possibly be explained by the fact that depalmitoylation of a receptor increases the accessibility of the cytoplasmic loops for protein kinases leading to receptor desensitisation (Sections 2.3.1.2.1 and 2.3.1.2.2) (Moffett et al., 1993, 1996).
Palmitoylation of protease-activated receptor-1 regulates adaptor protein complex-2 and -3 interaction with tyrosine-based motifs and endocytic sorting
2013, Journal of Biological ChemistryCitation Excerpt :This suggests that the secondary structure created by receptor palmitoylation is important for proper engagement of AP-2 with sorting motifs. In addition to PAR1 and TPβ receptor, ∼30 other mammalian GPCRs harbor canonical tyrosine-based motifs within their C-tail domain (45), and in some cases nearby cysteine residues are known to be palmitoylated (46–52). Thus, GPCR palmitoylation may have a broad function in regulating adaptor protein interaction with sorting signals and is likely to be important for maintaining appropriate expression of receptors on the cell surface.
Sf9 cells: A versatile model system to investigate the pharmacological properties of G protein-coupled receptors
2010, Pharmacology and TherapeuticsCitation Excerpt :Metabolic labeling with [3H]palmitate showed that M2R is palmitoylated in Sf9 cells. Expression of a C-terminally truncated receptor and the C457A mutant revealed that C457 is the site of palmitoylation (Hayashi & Haga, 1997). The non-palmitoylated mutants were purified from Sf9 cells and reconstituted with G-proteins in phospholipid vesicles. [
Constitutive G<inf>s</inf>-mediated, but not G<inf>12</inf>-mediated, activity of the 5-hydroxytryptamine 5-HT<inf>7(a)</inf> receptor is modulated by the palmitoylation of its C-terminal domain
2009, Biochimica et Biophysica Acta - Molecular Cell ResearchLipid-protein interactions in GPCR-associated signaling
2007, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :Accordingly, an increase in palmitate turnover can be provoked in response to extracellular stimuli [46]. Indeed, for a variety of GPCRs, such as the β2-adrenergic and α2A-adrenergic receptor, the palmitoylation/depalmitoylation cycle is activation-dependent [20,47–51]. However, when considering the effect of GPCR palmitoylation on G protein coupling the situation is somewhat less clear (Table 1).
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This work was supported in part by research grants from the Ministry of Education, Science, and Culture of Japan, and Japan Health Science Foundation.
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