Abstract
It is now clear that nearly all G-protein-coupled receptors (GPCRs) are phosphorylated and palmitolyated. The process of receptor phosphorylation has been extensively studied because it offers a regulatory mechanism that is both rapid and dynamic. However, it has recently become clear that palmitoyaltion of GPCRs at C-terminal cysteine residues may also offer dynamic receptor modification. A growing number of GPCRs have been demonstrated to undergo rapid agonist-mediated changes in their palmitoylation status with functional implications to receptor signaling. This chapter aims to outline the methods we have used to investigate agonist-mediated changes in GPCR phosphorylation and palmitoylation.
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Tobin, A.B., Wheatley, M. (2004). G-Protein-Coupled Receptor Phosphorylation and Palmitoylation. In: Willars, G.B., Challiss, R.A.J. (eds) Receptor Signal Transduction Protocols. Methods in Molecular Biology, vol 259. Humana Press. https://doi.org/10.1385/1-59259-754-8:275
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DOI: https://doi.org/10.1385/1-59259-754-8:275
Publisher Name: Humana Press
Print ISBN: 978-1-58829-329-9
Online ISBN: 978-1-59259-754-3
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