Article abstract
Nature Cell Biology 3, 492 - 498 (2001)
Published online: 17 April 2001 | doi:10.1038/35074561
Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein
Jason C. Bermak1, Ming Li1, Clayton Bullock1 & Qun-Yong Zhou1
Abstract
Many structural determinants for G protein-coupled receptor (GPCR) functions have been defined, but little is known concerning the regulation of their transport from the endoplasmic reticulum (ER) to the cell surface. Here we show that a carboxy-terminal hydrophobic motif, FxxxFxxxF, which is highly conserved among GPCRs, functions independently as an ER-export signal for the dopamine D1 receptor. A newly identified ER-membrane-associated protein, DRiP78, binds to this motif. Overexpression or sequestration of DRiP78 leads to retention of D1 receptors in the ER, reduced ligand binding, and a slowdown in the kinetics of receptor glycosylation. Our results indicate that DRiP78 may regulate the transport of a GPCR by binding to a specific ER-export signal.
- Department of Pharmacology, University of California, Irvine, California 92697, USA
Correspondence to: Qun-Yong Zhou1 e-mail: qzhou@msx.hsis.uci.edu
