Evidence map›Paper›PMID 25578875›Full record

ArticleMolecular cell2015

Structure and assembly pathway of the ribosome quality control complex.

Sichen Shao, Alan Brown, Balaji Santhanam, Ramanujan S Hegde

Abstract read
In one paragraph

Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 149 papers.

0numbers the graph read from it
0cells of the map it votes in
149citing papers in PubMed
–field-weighted citation impact
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

149 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
  6. Article
  7. Quality control and signaling pathways at stalled ribosomes.Experimental & molecular medicine · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Interpreting ribosome dynamics during mRNA translation.The Journal of biological chemistry · 2025
    Review

89 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Sichen ShaoMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Alan BrownMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Balaji SanthanamMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Ramanujan S HegdeMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK. Electronic address: rhegde@mrc-lmb.cam.ac.uk.

Funding

Medical Research Council MC_U105184332Medical Research Council MC_UP_A022_1007Wellcome Trust WT096570
6 · The paper itself

Abstract

During ribosome-associated quality control, stalled ribosomes are split into subunits and the 60S-housed nascent polypeptides are poly-ubiquitinated by Listerin. How this low-abundance ubiquitin ligase targets rare stall-generated 60S among numerous empty 60S is unknown. Here, we show that Listerin specificity for nascent chain-60S complexes depends on nuclear export mediator factor (NEMF). The 3.6 Å cryo-EM structure of a nascent chain-containing 60S-Listerin-NEMF complex revealed that NEMF makes multiple simultaneous contacts with 60S and peptidyl-tRNA to sense nascent chain occupancy. Structural and mutational analyses showed that ribosome-bound NEMF recruits and stabilizes Listerin's N-terminal domain, while Listerin's C-terminal RWD domain directly contacts the ribosome to position the adjacent ligase domain near the nascent polypeptide exit tunnel. Thus, highly specific nascent chain targeting by Listerin is imparted by the avidity gained from a multivalent network of context-specific individually weak interactions, highlighting a new principle of client recognition during protein quality control.

Indexed as

Antigens, NeoplasmBinding SitesCryoelectron MicroscopyHEK293 CellsHumansModels, MolecularMolecular ConformationNucleocytoplasmic Transport ProteinsRibosomesRNA, Transfer, Amino AcylUbiquitinationUbiquitin-Protein LigasesAntigens, NeoplasmNEMF protein, humanNucleocytoplasmic Transport ProteinsRNA, Transfer, Amino AcyltRNA, peptidyl-Ubiquitin-Protein Ligases

Identifiers

PMID25578875
PMCPMC4321881

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Registered trials

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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.