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.
Original language | English |
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Pages (from-to) | 275-281 |
Number of pages | 7 |
Journal | Methods in molecular biology (Clifton, N.J.) |
Volume | 259 |
DOIs | |
Publication status | Published - 2004 |
Externally published | Yes |
ASJC Scopus subject areas
- Molecular Biology
- Genetics