Palmitoylation: a post-translational modification that regulates signalling from G-protein coupled receptors
- 1 July 1996
- journal article
- review article
- Published by Canadian Science Publishing in Biochemistry and Cell Biology
- Vol. 74 (4) , 449-457
- https://doi.org/10.1139/o96-049
Abstract
Protein acylation is a post-translational modification that has seized much attention in the last few years. Depending on the nature of the fatty acid added, protein acylation can take the form of palmitoylation, myristoylation, or prenylation. Palmitoylation has been implicated in the modification of several different proteins and is particularly prevalent in G-protein coupled receptors and their cognate G-proteins, where it is thought to have an important regulatory function. Given that palmitoylation of these proteins is a dynamic phenomenon in which turnover rate is modulated by agonist activation, it is thought to be implicated in processes such as receptor phosphorylation and desensitization as well as in G-protein membrane translocation. A better understanding of the regulation of signal transduction mediated by G-protein coupled receptors will require the identification and characterization of those enzymes implicated in the palmitoylation and depalmitoylation process of this large class of receptors and their signalling allies.Key words: palmitoylation, β-adrenergic receptor, G-protein, phosphorylation, desensitization.Keywords
This publication has 38 references indexed in Scilit:
- Functional Importance of the Carboxyl Tail Cysteine Residues in the Human D1 Dopamine ReceptorJournal of Neurochemistry, 1995
- The Metabotropic Glutamate Receptor mGluR4, but Not mGluR1α, Is Palmitoylated when Expressed in BHK CellsJournal of Neurochemistry, 1995
- Phosphorylation and Palmitoylation of the Human D2L Dopamine Receptor in Sf9 CellsJournal of Neurochemistry, 1994
- Roles of Lipid Modifications of Transducin Subunits in Their GDP-Dependent Association and Membrane BindingBiochemistry, 1994
- Fluorescence Studies of the Location and Membrane Accessibility of the Palmitoylation Sites of RhodopsinBiochemistry, 1994
- Desensitization, phosphorylation and palmitoylation of the human dopamine D1 receptorEuropean Journal of Pharmacology: Molecular Pharmacology, 1994
- Novel inhibitory action of tunicamycin homologues suggests a role for dynamic protein fatty acylation in growth cone-mediated neurite extensionThe Journal of cell biology, 1994
- The G protein .alpha.s subunit incorporates [3H]palmitic acid and mutation of cysteine-3 prevents this modificationBiochemistry, 1993
- Fatty acylated proteins as components of intracellular signaling pathwaysBiochemistry, 1990
- Two adjacent cysteine residues in the C‐terminal cytoplasmic fragment of bovine rhodopsin are palmitylatedFEBS Letters, 1988