Evidence map›Paper›PMID 25349383›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Structural basis for translational surveillance by the large ribosomal subunit-associated protein quality control complex.

Dmitry Lyumkis, Dario Oliveira dos Passos, Erich B Tahara, Kristofor Webb, Eric J Bennett, Staal Vinterbo, Clinton S Potter, Bridget Carragher, Claudio A P Joazeiro

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

79 citing papers in PubMed, 131 citations in OpenAlex.

  1. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
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  5. Review
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  9. Structure of a Gcn2 dimer in complex with the large 60S ribosomal subunit.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Review
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  18. Listerin promotes cGAS protein degradation through the ESCRT pathway to negatively regulate cGAS-mediated immune response.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. Article

19 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

9 authors at 2 institutions in 1 country.

Dmitry LyumkisNational Resource for Automated Molecular Microscopy and Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037;
Dario Oliveira dos PassosDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037; and.
Erich B TaharaDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037; and.
Kristofor WebbDivisions of Biological Sciences, Section of Cell and Developmental Biology, and.
Eric J BennettDivisions of Biological Sciences, Section of Cell and Developmental Biology, and.
Staal VinterboBiomedical Informatics, University of California, San Diego, La Jolla, CA 92093.
Clinton S PotterNational Resource for Automated Molecular Microscopy and Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037;
Bridget CarragherNational Resource for Automated Molecular Microscopy and Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037; bcarr@scripps.edu joazeiro@scripps.edu.
Claudio A P JoazeiroDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037; and bcarr@scripps.edu joazeiro@scripps.edu.
Scripps Research Institute · USUniversity of California, San Diego · US

Funding

TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
A New E3 Ligase Implicated in Protein Quality Control and NeurodegenerationR01NS075719 · NINDS · SCRIPPS RESEARCH INSTITUTE, THE · PI JOAZEIRO, CLAUDIO A.P. · 2012 to 2016
$2.0M
Small Molecule Inhibitors of Mdm2 E3 Ubiquitin Ligase Activity for Cancer TherapyR01CA152103 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI JOAZEIRO, CLAUDIO A.P. · 2012 to 2016
$1.9M
NCI NIH HHS CA152103NCI NIH HHS R01 CA152103NIGMS NIH HHS GM103310NIGMS NIH HHS P41 GM103310NIGMS NIH HHS P41 GM103311NINDS NIH HHS NS075719NINDS NIH HHS R01 NS075719PHS HHS NIGMS P41-GM103311
6 · The paper itself

Abstract

All organisms have evolved mechanisms to manage the stalling of ribosomes upon translation of aberrant mRNA. In eukaryotes, the large ribosomal subunit-associated quality control complex (RQC), composed of the listerin/Ltn1 E3 ubiquitin ligase and cofactors, mediates the ubiquitylation and extraction of ribosome-stalled nascent polypeptide chains for proteasomal degradation. How RQC recognizes stalled ribosomes and performs its functions has not been understood. Using single-particle cryoelectron microscopy, we have determined the structure of the RQC complex bound to stalled 60S ribosomal subunits. The structure establishes how Ltn1 associates with the large ribosomal subunit and properly positions its E3-catalytic RING domain to mediate nascent chain ubiquitylation. The structure also reveals that a distinguishing feature of stalled 60S particles is an exposed, nascent chain-conjugated tRNA, and that the Tae2 subunit of RQC, which facilitates Ltn1 binding, is responsible for selective recognition of stalled 60S subunits. RQC components are engaged in interactions across a large span of the 60S subunit surface, connecting the tRNA in the peptidyl transferase center to the distally located nascent chain tunnel exit. This work provides insights into a mechanism linking translation and protein degradation that targets defective proteins immediately after synthesis, while ignoring nascent chains in normally translating ribosomes.

Indexed as

ProteolysisProteasome Endopeptidase ComplexProtein BiosynthesisProtein Structure, TertiaryRibosome Subunits, Large, EukaryoticRNA-Binding ProteinsRNA, Transfer, Amino AcylSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipUbiquitinationUbiquitin-Protein LigasesLtn1 protein, S cerevisiaeProteasome Endopeptidase ComplexRNA-Binding ProteinsRNA, Transfer, Amino AcylSaccharomyces cerevisiae ProteinsTae2 protein, S cerevisiaetRNA, peptidyl-Ubiquitin-Protein Ligasescryo-EMlisterin/Ltn1 E3 ubiquitin ligaseprotein quality controlTae2/Nemftranslational surveillance

Identifiers

PMID25349383
PMCPMC4234556
OpenAlexW2068090915

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.