Evidence map›Paper›PMID 26943317›Full record

ArticleeLife2016

The Rqc2/Tae2 subunit of the ribosome-associated quality control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation.

Ryo Yonashiro, Erich B Tahara, Mario H Bengtson, Maria Khokhrina, Holger Lorenz, Kai-Chun Chen, Yu Kigoshi-Tansho, Jeffrey N Savas, John R Yates, Steve A Kay and 4 more

Abstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing 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

87 citing papers in PubMed.

  1. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
  2. Quality control and signaling pathways at stalled ribosomes.Experimental & molecular medicine · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. A tunable affinity fusion tag for protein self-assembly.bioRxiv : the preprint server for biology · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

27 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

14 authors.

Ryo YonashiroDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, United States.
Erich B TaharaDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, United States.
Mario H BengtsonDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, United States.
Maria KhokhrinaZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Deutsches Krebsforschungszentrum (DKFZ), DKFZ-ZMBH Alliance, Heidelberg, Germany.
Holger LorenzZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Deutsches Krebsforschungszentrum (DKFZ), DKFZ-ZMBH Alliance, Heidelberg, Germany.
Kai-Chun ChenDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, United States.
Yu Kigoshi-TanshoDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, United States.
Jeffrey N SavasDepartment of Chemical Physiology, The Scripps Research Institute, La Jolla, United States.
John R YatesDepartment of Chemical Physiology, The Scripps Research Institute, La Jolla, United States.
Steve A KayDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, United States.
Elizabeth A CraigDepartment of Biochemistry, University of Wisconsin - Madison, Madison, United States.
Axel MogkZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Deutsches Krebsforschungszentrum (DKFZ), DKFZ-ZMBH Alliance, Heidelberg, Germany.
Bernd BukauZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Deutsches Krebsforschungszentrum (DKFZ), DKFZ-ZMBH Alliance, Heidelberg, Germany.
Claudio A P JoazeiroDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, United States.ORCID http://orcid.org/0000-0003-1433-8013

Funding

TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
Quantitative Proteome Analysis of Brain DevelopmentR01MH067880 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI YATES III, JOHN R · 2003 to 2017
$7.1M
REGULATION AND FUNCTION OF THE YEAST HEAT SHOCK RESPONSER37GM031107 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ELIZABETH A · 1999 to 2008
$3.3M
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
REGULATION AND FUNCTION OF THE YEAST HEAT SHOCK RESPONSER01GM031107 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ELIZABETH A · 1985 to 2012
$1.9M
Quantitative Proteomic Approach to Identify the Mechanism of Alzheimer's DiseaseF32AG039127 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI SAVAS, JEFFREY NICHOLAS · 2011 to 2014
$117k
NCI NIH HHS CA152103NCI NIH HHS R01 CA152103NIA NIH HHS F32 AG039127NIA NIH HHS F32AG039127NIGMS NIH HHS GM31107NIGMS NIH HHS P41 GM103533NIGMS NIH HHS R01 GM031107NIGMS NIH HHS R37 GM031107NIMH NIH HHS R01 MH067880NINDS NIH HHS NS075719NINDS NIH HHS R01 NS075719
6 · The paper itself

Abstract

Ribosome stalling during translation can potentially be harmful, and is surveyed by a conserved quality control pathway that targets the associated mRNA and nascent polypeptide chain (NC). In this pathway, the ribosome-associated quality control (RQC) complex promotes the ubiquitylation and degradation of NCs remaining stalled in the 60S subunit. NC stalling is recognized by the Rqc2/Tae2 RQC subunit, which also stabilizes binding of the E3 ligase, Listerin/Ltn1. Additionally, Rqc2 modifies stalled NCs with a carboxy-terminal, Ala- and Thr-containing extension-the 'CAT tail'. However, the function of CAT tails and fate of CAT tail-modified ('CATylated') NCs has remained unknown. Here we show that CATylation mediates formation of detergent-insoluble NC aggregates. CATylation and aggregation of NCs could be observed either by inactivating Ltn1 or by analyzing NCs with limited ubiquitylation potential, suggesting that inefficient targeting by Ltn1 favors the Rqc2-mediated reaction. These findings uncover a translational stalling-dependent protein aggregation mechanism, and provide evidence that proteins can become specifically marked for aggregation.

Indexed as

Protein Aggregation, PathologicalProtein BiosynthesisProtein Processing, Post-TranslationalPeptidesRibosomesRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPeptidesRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTae2 protein, S cerevisiaebiochemistryCAT tailcell biology<i>s. cerevisiae</i>listerinltn1NEMFprotein aggregationribosomeRQCrqc2ubiquitination

Identifiers

PMID26943317
PMCPMC4805532

What OpenQuestion holds

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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.