Evidence map›Paper›PMID 23932713›Full record

ArticleMolecular cell2013

Quality control of integral membrane proteins by assembly-dependent membrane integration.

Matthias J Feige, Linda M Hendershot

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
4.1field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

58 citing papers in PubMed, 91 citations in OpenAlex.

  1. Review
  2. Article
  3. Structural insights into SARS-CoV-2 nonstructural protein 4 (nsp4) biogenesis.Protein science : a publication of the Protein Society · 2025
    Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. The mechanisms of integral membrane protein biogenesis.Nature reviews. Molecular cell biology · 2022
    Review
  12. TheProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Matthias J FeigeDepartment of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA. matthias.feige@stjude.org
Linda M Hendershot
St. Jude Children's Research Hospital · US

Funding

Role of Molecular Chaperones in Ig Biosynthesis 11-2008R01GM054068 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI HENDERSHOT, LINDA M · 1996 to 2018
$5.7M
Novel mechanisms of TCR quality controlR03AI097733 · NIAID · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI HENDERSHOT, LINDA M · 2012 to 2013
$166k
NIAID NIH HHS R03 AI097733NIGMS NIH HHS R01 GM054068NIGMS NIH HHS R01 GM54068
6 · The paper itself

Abstract

Cell-surface multiprotein complexes are synthesized in the endoplasmic reticulum (ER), where they undergo cotranslational membrane integration and assembly. The quality control mechanisms that oversee these processes remain poorly understood. We show that less hydrophobic transmembrane (TM) regions derived from several single-pass TM proteins can enter the ER lumen completely. Once mislocalized, they are recognized by the Hsp70 chaperone BiP. In a detailed analysis for one of these proteins, the αβT cell receptor (αβTCR), we show that unassembled ER-lumenal subunits are rapidly degraded, whereas specific subunit interactions en route to the native receptor promote membrane integration of the less hydrophobic TM segments, thereby stabilizing the protein. For the TCR α chain, both complete ER import and subunit assembly depend on the same pivotal residue in its TM region. Thus, membrane integration linked to protein assembly allows cellular quality control of membrane proteins and connects the lumenal ER chaperone machinery to membrane protein biogenesis.

Indexed as

AnimalsCarrier ProteinsCD3 ComplexCell MembraneChlorocebus aethiopsCOS CellsEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHydrophobic and Hydrophilic InteractionsMembrane ProteinsProtein FoldingProtein TransportReceptors, Antigen, T-Cell, alpha-betaCarrier ProteinsCD3 ComplexEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSP70 Heat-Shock ProteinsMembrane ProteinsReceptors, Antigen, T-Cell, alpha-beta

Identifiers

PMID23932713
PMCPMC3770350
OpenAlexW1975098839

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.