Cited by 235Cellular transport and secretionEndoplasmic Reticulum Stress and DiseaseIon Channels and Receptors

Hide and run. Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins

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Michelsen, Kai, Yuan, Hebao, Schwappach, Blanche·2005·The EMBO Reports

Abstract

Arginine-based endoplasmic reticulum (ER)-localization signals are sorting motifs that are involved in the biosynthetic transport of multimeric membrane proteins. After their discovery in the invariant chain of the major histocompatibility complex class II, several hallmarks of these signals have emerged. They occur in polytopic membrane proteins that are subunits of membrane protein complexes; the presence of the signal maintains improperly assembled subunits in the ER by retention or retrieval until it is masked as a result of heteromultimeric assembly. A distinct consensus sequence and their position independence with respect to the distal termini of the protein distinguish them from other ER-sorting motifs. Recognition by the coatomer (COPI) vesicle coat explains ER retrieval. Often, di-leucine endocytic signals occur close to arginine-based signals. Recruitment of 14-3-3 family or PDZ-domain proteins can counteract ER-localization activity, as can phosphorylation. This, and the occurrence of arginine-based signals in alternatively spliced regions, implicates them in the regulated surface expression of multimeric membrane proteins in addition to their function in quality control.

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Crossref · 10.1038/sj.embor.7400480

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  • RRQR motifs are thought to prevent the exit of cargo from the ER and may additionally function as ER retrieval motifs via the binding of the RRXR domain to COPI proteins.

    “RRQR motifs are thought to prevent the exit of cargo from the ER and may additionally function as ER retrieval motifs via the binding of the RRXR domain to COPI proteins (Scott et al., 2001, 2003; Brock et al., 2005; Michelsen et al., 2005).”

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Authors
Michelsen, K., Yuan, H., & Schwappach, B.
Affiliations
Heidelberg University (DE)
Venue
The EMBO Reports
Published
2005-08-01
Volume
6
Issue
8
Pages
717-722
ISSN
  • 1469-221X (ISSN-L)
  • 1469-3178
OpenAlex
W2070136749
Cited by
235
References
35
Citations by year
2026: 1 · 2025: 10 · 2024: 5 · 2023: 6 · 2022: 7 · 2021: 4 · 2020: 6 · 2019: 10 · 2018: 6 · 2017: 5 · 2016: 13 · 2015: 12 · 2014: 19 · 2013: 13 · 2012: 14
FWCI
1.32
Type
journal article
Language
en
Open access
Locations
  • EMBO Reports (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Research Explorer (The University of Manchester) (publishedVersion)
  • GRO (submittedVersion)
Topics
  • 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
  • Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords
polytopic membrane proteins, CD74, 14-3-3 proteins, PDZ domain proteins, protein phosphorylation, alternative splicing, protein quality control
MeSH terms
Animals, Arginine, Cell Membrane, Endocytosis, Endoplasmic Reticulum, Humans, Ions, Membrane Proteins, Models, Biological, Potassium, Protein Structure, Tertiary, Amino Acid Motifs, Protein Transport, Macromolecular Substances, 14-3-3 Proteins

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