Evidence map›Paper›PMID 28528489›Full record

ReviewCurrent genetics2017

The ribosome-bound quality control complex: from aberrant peptide clearance to proteostasis maintenance.

Quentin Defenouillère, Micheline Fromont-Racine

Abstract readReview
PubMed Publisher
In one paragraph

Review in Current genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Proteostasis in aging-associated ocular disease.Molecular aspects of medicine · 2022
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. The proteostasis network and its decline in ageing.Nature reviews. Molecular cell biology · 2019
    Review
  17. Article
  18. Review
  19. Review
  20. Article
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.

Quentin DefenouillèreInstitut Pasteur, Génétique des Interactions Macromoléculaires, Centre National de la Recherche Scientifique, UMR 3525, 75724, Paris Cedex 15, France. quentin.defenouillere@ijm.fr.ORCID http://orcid.org/0000-0003-2255-4859
Micheline Fromont-RacineInstitut Pasteur, Génétique des Interactions Macromoléculaires, Centre National de la Recherche Scientifique, UMR 3525, 75724, Paris Cedex 15, France.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteostasis in eukaryotes is maintained by compartment-specific quality control pathways, which enable the refolding or the degradation of defective polypeptides to prevent the toxicity that may arise from their aggregation. Among these processes, translational protein quality control is performed by the Ribosome-bound Quality Control complex (RQC), which recognizes nascent peptides translated from aberrant mRNAs, polyubiquitylates these aberrant peptides, extracts them from the stalled 60S subunit and finally escorts them to the proteasome for degradation. In this review, we focus on the mechanism of action of the RQC complex from stalled 60S binding to aberrant peptide delivery to the proteasome and describe the cellular consequences of a deficiency in the RQC pathway, such as aberrant protein aggregation. In addition, this review covers the recent discoveries concerning the role of cytosolic chaperones, as well as Tom1, to prevent the accumulation of aberrant protein aggregates in case of a deficiency in the RQC pathway.

Indexed as

Protein BiosynthesisAnimalsHumansMolecular ChaperonesProteasome Endopeptidase ComplexProtein AggregatesProteolysisProteostasisRibosome Subunits, Large, EukaryoticSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationUbiquitin-Protein LigasesMolecular ChaperonesProteasome Endopeptidase ComplexProtein AggregatesSaccharomyces cerevisiae ProteinsTOM1 protein, S cerevisiaeUbiquitin-Protein LigasesAggregationProtein degradationProteostasisRQC complexTranslational quality control

Identifiers

PMID28528489
OpenAlexW2615215135

What OpenQuestion holds

Textmetadata
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.