Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein.

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.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Animals, Antigens, CD8, Biological Transport, Cell Line, Cell Membrane, Cyclic AMP, Endoplasmic Reticulum, Green Fluorescent Proteins, Humans, Kinetics, Ligands, Luminescent Proteins, Microscopy, Confocal, Microscopy, Fluorescence, Models, Biological, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Structure, Tertiary, Receptors, Cell Surface, Receptors, Dopamine D1, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Time Factors, Two-Hybrid System Techniques
Nat. Cell Biol.
Date: May. 01, 2001
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