Evidence map›Paper›PMID 31219035›Full record

ArticleeLife2019

The endonuclease Cue2 cleaves mRNAs at stalled ribosomes during No Go Decay.

Karole N D'Orazio, Colin Chih-Chien Wu, Niladri Sinha, Raphael Loll-Krippleber, Grant W Brown, Rachel Green

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.

0numbers the graph read from it
0cells of the map it votes in
139citing papers in PubMed
10.1field-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

139 citing papers in PubMed, 226 citations in OpenAlex.

  1. Article
  2. Collided ribosomes are rescued by the endonuclease Rae1 andbioRxiv : the preprint server for biology · 2026
    Article
  3. Ribosome stalling position, spacing, and A-site occupancy impact translation and cotranslational mRNA decay in plants.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Plant MutS2 proteins function in plastid ribosome quality control.bioRxiv : the preprint server for biology · 2025
    Article
  19. Review
  20. Article

79 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

6 authors at 2 institutions in 2 countries.

Karole N D'OrazioDepartment of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, United States.ORCID 0000-0003-1954-4406
Colin Chih-Chien WuDepartment of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, United States.ORCID 0000-0002-6013-0224
Niladri SinhaDepartment of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, United States.ORCID 0000-0002-9143-495X
Raphael Loll-KrippleberDonnelly Centre for Cellular and Biomolecular Research, Department of Biochemistry, University of Toronto, Toronto, Canada.
Grant W BrownDonnelly Centre for Cellular and Biomolecular Research, Department of Biochemistry, University of Toronto, Toronto, Canada.
Rachel GreenDepartment of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, United States.ORCID 0000-0001-9337-2003
Howard Hughes Medical Institute · USUniversity of Toronto · CA

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
Molecular mechanisms of ribosome pausing and the cellular responseR37GM059425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 2014 to 2023
$3.5M
NIGMS NIH HHS R37 GM059425NIGMS NIH HHS T32 GM007445NIH HHS 5T32GM007445-39NIH HHS R37GM059425
6 · The paper itself

Abstract

Translation of problematic sequences in mRNAs leads to ribosome collisions that trigger a series of quality control events including ribosome rescue, degradation of the stalled nascent polypeptide, and targeting of the mRNA for decay (No Go Decay or NGD). Using a reverse genetic screen in yeast, we identify Cue2 as the conserved endonuclease that is recruited to stalled ribosomes to promote NGD. Ribosome profiling and biochemistry provide strong evidence that Cue2 cleaves mRNA within the A site of the colliding ribosome. We demonstrate that NGD primarily proceeds via Xrn1-mediated exonucleolytic decay and Cue2-mediated endonucleolytic decay normally constitutes a secondary decay pathway. Finally, we show that the Cue2-dependent pathway becomes a major contributor to NGD in cells depleted of factors required for the resolution of stalled ribosome complexes. Together these results provide insights into how multiple decay processes converge to process problematic mRNAs in eukaryotic cells.​.

Indexed as

Protein BiosynthesisCytokinesisExoribonucleasesRibosomesRNA, FungalRNA, MessengerRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsExoribonucleasesRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsXRN1 protein, S cerevisiaeendonucleasegeneticsgenomicsmRNANo Go DecayS. cerevisiaeubiquitin

Identifiers

PMID31219035
PMCPMC6598757
OpenAlexW2950813204

What OpenQuestion holds

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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.