Cited by 281Receptor Mechanisms and SignalingCellular transport and secretionEndoplasmic Reticulum Stress and Disease

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

Bermak, Jason C., Li, Ming, Bullock, Clayton, Zhou, Qun-Yong·2001·Nature Cell Biology

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.

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Crossref · 10.1038/35074561

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  • A DRIP78 binding sequence (FxxxFxxxF) is conserved in the C-termini of a subset of group B and group C surreal-GPCR sequences.

    “In line with such a role, we find a dopamine receptor interacting protein 78 (DRIP78) binding sequence (FxxxFxxxF) (Bermak et al., 2001) conserved in the C-termini of a subset of sequences ( SPU_006834, SPU_008884, SPU_010318, SPU_010318; SPU_000576, SPU_015119, SPU_006431).”

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Authors
Bermak, J. C., Li, M., Bullock, C., & Zhou, Q.-Y.
Affiliations
University of California, Irvine (US)
Corresponding author
Zhou, Qun-Yong
Venue
Nature Cell Biology
Published
2001-04-17
Volume
3
Issue
5
Pages
492-498
ISSN
  • 1465-7392 (ISSN-L)
  • 1476-4679
OpenAlex
W1527823690
Cited by
281
References
38
Citations by year
2026: 3 · 2025: 3 · 2024: 1 · 2023: 7 · 2022: 5 · 2021: 4 · 2020: 5 · 2019: 6 · 2018: 4 · 2017: 8 · 2016: 12 · 2015: 10 · 2014: 7 · 2013: 14 · 2012: 20
FWCI
5.82
Type
journal article
Language
en
Open access
closed
Locations
  • Nature Cell Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Alfred P. Sloan Foundation
  • National Institutes of Health
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Keywords
dopamine D1 receptor, G protein-coupled receptors, receptor transport, receptor glycosylation, ligand binding, receptor trafficking
MeSH terms
Cyclic AMP, Amino Acid Sequence, Animals, Biological Transport, Cell Line, Cell Membrane, Endoplasmic Reticulum, Humans, Kinetics, Ligands, Luminescent Proteins, Microscopy, Fluorescence, Models, Biological, Molecular Sequence Data, Receptors, Cell Surface, Recombinant Fusion Proteins, Time Factors, Mutagenesis, Site-Directed, CD8 Antigens, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Receptors, Dopamine D1, Microscopy, Confocal, Two-Hybrid System Techniques, Amino Acid Motifs, Green Fluorescent Proteins

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