期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1768, 期 4, 页码 853-870出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2006.09.008
关键词
G protein-coupled receptor; intracellular trafficking; export; sorting and targeting; biosynthesis; endoplasmic reticulum; golgi; folding; ER export motif; ER retention motif; ER chaperone; chemical chaperone; pharmacological chaperone; GPCR-interacting protein; signal transduction
资金
- NCRR NIH HHS [P20 RR018766, RR18766] Funding Source: Medline
- NIGMS NIH HHS [GM76167, R01 GM076167] Funding Source: Medline
- NATIONAL CENTER FOR RESEARCH RESOURCES [P20RR018766] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM076167] Funding Source: NIH RePORTER
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. (c) 2006 Elsevier B.V. All rights reserved.
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