Evidence map›Paper›PMID 32579943›Full record

ArticleMolecular cell2020

The ASC-1 Complex Disassembles Collided Ribosomes.

Szymon Juszkiewicz, Shaun H Speldewinde, Li Wan, Jesper Q Svejstrup, Ramanujan S Hegde

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

119 citing papers in PubMed, 207 citations in OpenAlex.

  1. Review
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  13. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
  14. Quality control and signaling pathways at stalled ribosomes.Experimental & molecular medicine · 2026
    Review
  15. Article
  16. Article
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59 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

Szymon JuszkiewiczMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Shaun H SpeldewindeThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Li WanThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Jesper Q SvejstrupThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Ramanujan S HegdeMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK. Electronic address: rhegde@mrc-lmb.cam.ac.uk.
The Francis Crick Institute · GBMRC Laboratory of Molecular Biology · GB

Funding

Cancer Research UK 11567Cancer Research UK FC001166Medical Research Council FC001166Medical Research Council MC_UP_A022_1007Wellcome Trust FC001166
6 · The paper itself

Abstract

Translating ribosomes that slow excessively incur collisions with trailing ribosomes. Persistent collisions are detected by ZNF598, a ubiquitin ligase that ubiquitinates sites on the ribosomal 40S subunit to initiate pathways of mRNA and protein quality control. The collided ribosome complex must be disassembled to initiate downstream quality control, but the mechanistic basis of disassembly is unclear. Here, we reconstitute the disassembly of a collided polysome in a mammalian cell-free system. The widely conserved ASC-1 complex (ASCC) containing the ASCC3 helicase disassembles the leading ribosome in an ATP-dependent reaction. Disassembly, but not ribosome association, requires 40S ubiquitination by ZNF598, but not GTP-dependent factors, including the Pelo-Hbs1L ribosome rescue complex. Trailing ribosomes can elongate once the roadblock has been removed and only become targets if they subsequently stall and incur collisions. These findings define the specific role of ASCC during ribosome-associated quality control and identify the molecular target of its activity.

Indexed as

Protein BiosynthesisAmino Acid Transport System y+AnimalsCarrier ProteinsCell-Free SystemDNA HelicasesGTP-Binding ProteinsHEK293 CellsHumansMultiprotein ComplexesNuclear ProteinsPeptide Termination FactorsPolyribosomesRabbitsRibosomesRibosome SubunitsAmino Acid Transport System y+ASCC1 protein, humanASCC2 protein, humanASCC3 protein, humanCarrier ProteinsDNA HelicasesETF1 protein, humanGTP-Binding ProteinsHBS1L protein, humanMultiprotein ComplexesNuclear ProteinsPeptide Termination FactorsSLC7A10 protein, humanZNF598 protein, humanASCC3helicasequality controlribosomeRQCtranslation

Identifiers

PMID32579943
PMCPMC7447978
OpenAlexW3035939632

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.