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.
|Number of pages||7|
|Journal||Methods in molecular biology (Clifton, N.J.)|
|Publication status||Published - 2004|
ASJC Scopus subject areas
- Molecular Biology