Evidence map›Paper›PMID 37653243›Full record

ArticleNature structural & molecular biology2023

Specific recognition and ubiquitination of translating ribosomes by mammalian CCR4-NOT.

Eva Absmeier, Viswanathan Chandrasekaran, Francis J O'Reilly, James A W Stowell, Juri Rappsilber, Lori A Passmore

Open access · hybridAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
8.9field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. eLife · 2026
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  7. Phosphorylation-dependent tuning of mRNA deadenylation rates.Nature structural & molecular biology · 2026
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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

6 authors at 3 institutions in 2 countries.

Eva Absmeier *MRC Laboratory of Molecular Biology (LMB), Cambridge, UK.
Viswanathan Chandrasekaran *MRC Laboratory of Molecular Biology (LMB), Cambridge, UK. vish@mrc-lmb.cam.ac.uk.ORCID http://orcid.org/0000-0002-0871-4740
Francis J O'ReillyTechnical University of Berlin, Chair of Bioanalytics, Berlin, Germany.ORCID http://orcid.org/0000-0001-9258-0150
James A W StowellMRC Laboratory of Molecular Biology (LMB), Cambridge, UK.
Juri RappsilberTechnical University of Berlin, Chair of Bioanalytics, Berlin, Germany.ORCID http://orcid.org/0000-0001-5999-1310
Lori A PassmoreMRC Laboratory of Molecular Biology (LMB), Cambridge, UK. passmore@mrc-lmb.cam.ac.uk.ORCID http://orcid.org/0000-0003-1815-3710
MRC Laboratory of Molecular Biology · GBTechnische Universität Berlin · DEWellcome Centre for Cell Biology · GB

Funding

European Research Council 725685Medical Research Council MC_U105184332Medical Research Council MC_U105192715Wellcome Trust 096570Wellcome Trust 203149
6 · The paper itself

Abstract

Translation affects messenger RNA stability and, in yeast, this is mediated by the Ccr4-Not deadenylation complex. The details of this process in mammals remain unclear. Here, we use cryogenic electron microscopy (cryo-EM) and crosslinking mass spectrometry to show that mammalian CCR4-NOT specifically recognizes ribosomes that are stalled during translation elongation in an in vitro reconstituted system with rabbit and human components. Similar to yeast, mammalian CCR4-NOT inserts a helical bundle of its CNOT3 subunit into the empty E site of the ribosome. Our cryo-EM structure shows that CNOT3 also locks the L1 stalk in an open conformation to inhibit further translation. CCR4-NOT is required for stable association of the nonconstitutive subunit CNOT4, which ubiquitinates the ribosome, likely to signal stalled translation elongation. Overall, our work shows that human CCR4-NOT not only detects but also enforces ribosomal stalling to couple translation and mRNA decay.

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAnimalsHumansMammalsMass SpectrometryRabbitsReceptors, CCR4RibonucleasesRibosomesTranscription FactorsUbiquitinationCCR4 protein, humanCCR4 protein, S cerevisiaeCNOT3 protein, humanReceptors, CCR4RibonucleasesSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID37653243
PMCPMC7615087
OpenAlexW4386332720

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.