TY - JOUR
T1 - Regulation of G protein-coupled receptor export trafficking
AU - Dong, Chunmin
AU - Filipeanu, Catalin M.
AU - Duvernay, Matthew T.
AU - Wu, Guangyu
N1 - Funding Information:
This work was supported by National Institutes of Health grants GM76167 (to G. W.) and RR18766 (Project PI: G.W. and Program Director: Stephen M. Lanier), an American Heart Association Southeast Affiliate postdoctoral fellowship (to C. D.) and a Louisiana Board Regents graduate fellowship (to M. T. D.). We apologize to numerous colleagues whose work could not be cited in this article due to space limitation.
PY - 2007/4
Y1 - 2007/4
N2 - 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.
AB - 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.
KW - Biosynthesis
KW - Chemical chaperone
KW - ER chaperone
KW - ER export motif
KW - ER retention motif
KW - Endoplasmic reticulum
KW - Export
KW - Folding
KW - G protein-coupled receptor
KW - GPCR-interacting protein
KW - Golgi
KW - Intracellular trafficking
KW - Pharmacological chaperone
KW - Signal transduction
KW - Sorting and targeting
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U2 - 10.1016/j.bbamem.2006.09.008
DO - 10.1016/j.bbamem.2006.09.008
M3 - Review article
C2 - 17074298
AN - SCOPUS:33947362949
SN - 0005-2736
VL - 1768
SP - 853
EP - 870
JO - Biochimica et Biophysica Acta - Biomembranes
JF - Biochimica et Biophysica Acta - Biomembranes
IS - 4
ER -