Evidence map›Paper›PMID 32203490›Full record

ArticleNature structural & molecular biology2020

RQT complex dissociates ribosomes collided on endogenous RQC substrate SDD1.

Yoshitaka Matsuo, Petr Tesina, Shizuka Nakajima, Masato Mizuno, Akinori Endo, Robert Buschauer, Jingdong Cheng, Okuto Shounai, Ken Ikeuchi, Yasushi Saeki and 3 more

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Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
7.8field-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

95 citing papers in PubMed, 165 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
  6. Quality control and signaling pathways at stalled ribosomes.Experimental & molecular medicine · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Detection and Characterization of the Eukaryotic Vacant Ribosome.International journal of molecular sciences · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. mCell · 2025
    Article
  18. Review
  19. Review
  20. Review

35 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

13 authors at 3 institutions in 2 countries.

Yoshitaka Matsuo *Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
Petr Tesina *Gene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Shizuka NakajimaGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
Masato MizunoGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
Akinori EndoLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo, Japan.
Robert BuschauerGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Jingdong ChengGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID http://orcid.org/0000-0003-4442-377X
Okuto ShounaiGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
Ken IkeuchiGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.ORCID http://orcid.org/0000-0002-9578-7920
Yasushi SaekiLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo, Japan.ORCID http://orcid.org/0000-0002-9202-5453
Thomas BeckerGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID http://orcid.org/0000-0001-8458-2738
Roland BeckmannGene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany. beckmann@genzentrum.lmu.de.ORCID http://orcid.org/0000-0003-4291-3898
Toshifumi InadaGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan. toshifumi.inada.a3@tohoku.ac.jp.ORCID http://orcid.org/0000-0002-2695-588X
Tohoku University · JPCenter for Integrated Protein Science Munich · DETokyo Metropolitan Institute of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosome-associated quality control (RQC) represents a rescue pathway in eukaryotic cells that is triggered upon translational stalling. Collided ribosomes are recognized for subsequent dissociation followed by degradation of nascent peptides. However, endogenous RQC-inducing sequences and the mechanism underlying the ubiquitin-dependent ribosome dissociation remain poorly understood. Here, we identified SDD1 messenger RNA from Saccharomyces cerevisiae as an endogenous RQC substrate and reveal the mechanism of its mRNA-dependent and nascent peptide-dependent translational stalling. In vitro translation of SDD1 mRNA enabled the reconstitution of Hel2-dependent polyubiquitination of collided disomes and, preferentially, trisomes. The distinct trisome architecture, visualized using cryo-EM, provides the structural basis for the more-efficient recognition by Hel2 compared with that of disomes. Subsequently, the Slh1 helicase subunit of the RQC trigger (RQT) complex preferentially dissociates the first stalled polyubiquitinated ribosome in an ATP-dependent manner. Together, these findings provide fundamental mechanistic insights into RQC and its physiological role in maintaining cellular protein homeostasis.

Indexed as

Protein BiosynthesisAdenosine TriphosphateCell Cycle ProteinsPeptidesRibosomesRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSerine EndopeptidasesUbiquitinUbiquitinationUbiquitin-Protein LigasesAdenosine TriphosphateCell Cycle ProteinsHel2 protein, S cerevisiaePeptidesRNA, MessengerSaccharomyces cerevisiae ProteinsSDD1 protein, S cerevisiaeSerine EndopeptidasesUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID32203490
OpenAlexW3010254892

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.