Author: ["Jason C. Bermak","Ming Li","Clayton Bullock","Qun-Yong Zhou"]
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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.Cite this article
Bermak, J., Li, M., Bullock, C. et al. Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein. Nat Cell Biol 3, 492–498 (2001). https://doi.org/10.1038/35074561 