Evidence map›Paper›PMID 25877867›Full record

ArticleMolecular biology of the cell2015

The ribosome quality control pathway can access nascent polypeptides stalled at the Sec61 translocon.

Karina von der Malsburg, Sichen Shao, Ramanujan S Hegde

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.9field-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

48 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Quality control and signaling pathways at stalled ribosomes.Experimental & molecular medicine · 2026
    Review
  5. Article
  6. Article
  7. Review
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  14. RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Detecting and Rescuing Stalled Ribosomes.Trends in biochemical sciences · 2021
    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

3 authors at 1 institution in 1 country.

Karina von der MalsburgMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.
Sichen ShaoMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.
Ramanujan S HegdeMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom rhegde@mrc-lmb.cam.ac.uk.
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_UP_A022_1007
6 · The paper itself

Abstract

Cytosolic ribosomes that stall during translation are split into subunits, and nascent polypeptides trapped in the 60S subunit are ubiquitinated by the ribosome quality control (RQC) pathway. Whether the RQC pathway can also target stalls during cotranslational translocation into the ER is not known. Here we report that listerin and NEMF, core RQC components, are bound to translocon-engaged 60S subunits on native ER membranes. RQC recruitment to the ER in cultured cells is stimulated by translation stalling. Biochemical analyses demonstrated that translocon-targeted nascent polypeptides that subsequently stall are polyubiquitinated in 60S complexes. Ubiquitination at the translocon requires cytosolic exposure of the polypeptide at the ribosome-Sec61 junction. This exposure can result from either failed insertion into the Sec61 channel or partial backsliding of translocating nascent chains. Only Sec61-engaged nascent chains early in their biogenesis were relatively refractory to ubiquitination. Modeling based on recent 60S-RQC and 80S-Sec61 structures suggests that the E3 ligase listerin accesses nascent polypeptides via a gap in the ribosome-translocon junction near the Sec61 lateral gate. Thus the RQC pathway can target stalled translocation intermediates for degradation from the Sec61 channel.

Indexed as

Peptide Chain Elongation, TranslationalEndoplasmic Reticulum, RoughHumansMembrane ProteinsModels, MolecularPeptidesProtein TransportRibosome Subunits, Large, EukaryoticSEC Translocation ChannelsUbiquitinationUbiquitin-Protein LigasesLTN1 protein, humanMembrane ProteinsPeptidesSEC Translocation ChannelsUbiquitin-Protein Ligases

Identifiers

PMID25877867
PMCPMC4462936
OpenAlexW2067746546

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.