Differential regulation of two palmitoylation sites in the cytoplasmic tail of the beta1-adrenergic receptor.

ABSTRACT: S-Palmitoylation of G protein-coupled receptors (GPCRs) is a prevalent modification, contributing to the regulation of receptor function. Despite its importance, the palmitoylation status of the β(1)-adrenergic receptor, a GPCR critical for heart function, has never been determined. We report here that the β(1)-adrenergic receptor is palmitoylated on three cysteine residues at two sites in the C-terminal tail. One site (proximal) is adjacent to the seventh transmembrane domain and is a consensus site for GPCRs, and the other (distal) is downstream. These sites are modified in different cellular compartments, and the distal palmitoylation site contributes to efficient internalization of the receptor following agonist stimulation. Using a bioorthogonal palmitate reporter to quantify palmitoy

SUBMITTER: Zuckerman DM 

PROVIDER: S-EPMC3099716 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature