Regulation of G Protein-coupled Receptor Export Trafficking.
From: Department of Pharmacology and Experimental Therapeutics, Louisiana State University Health Sciences Center, New Orleans, LA 70112, USA.
Biochimica et biophysica acta
- Publish Date: Apr 2007
- ISSN: 0006-3002
- Volume: 1768
- Issue: 4
- Pages: 853-70
- Medium: Print
- Language: English
- Citation (JAMA): Dong Chunmin, Filipeanu Catalin M, Duvernay Matthew T, et al. Regulation of G Protein-coupled Receptor Export Trafficking.. Biochim. Biophys. Acta Apr 2007;1768:853-70
Abstract
G protein-coupled receptors (GPCRs) constitute a superfamily of cell-surface receptors which share a common topology of seven transmembrane domains and modulate a variety of cell functions through coupling to heterotrimeric G proteins by responding to a vast array of stimuli. The magnitude of cellular response elicited by a given signal is dictated by the level of GPCR expression at the plasma membrane, which is the balance of elaborately regulated endocytic and exocytic trafficking. This review will cover recent advances in understanding the molecular mechanism underlying anterograde transport of the newly synthesized GPCRs from the endoplasmic reticulum (ER) through the Golgi to the plasma membrane. We will focus on recently identified motifs involved in GPCR exit from the ER and the Golgi, GPCR folding in the ER and the rescue of misfolded receptors from within, GPCR-interacting proteins that modulate receptor cell-surface targeting, pathways that mediate GPCR traffic, and the functional role of export in controlling GPCR signaling.
Mesh Headings (Keywords): Amino Acid Motifs, Animals, Endoplasmic Reticulum, Golgi Apparatus, Protein Folding, Protein Transport, Proteins, Receptors, G-Protein-Coupled
Check for Full Text / PubMed Unique Identifier (PMID): 17074298
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