Evidence map›Paper›PMID 37951216›Full record

ArticleMolecular cell2023

RNF14-dependent atypical ubiquitylation promotes translation-coupled resolution of RNA-protein crosslinks.

Shubo Zhao, Jacqueline Cordes, Karolina M Caban, Maximilian J Götz, Timur Mackens-Kiani, Anthony J Veltri, Niladri K Sinha, Pedro Weickert, Selay Kaya, Graeme Hewitt and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
7.4field-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

34 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
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  6. Article
  7. Article
  8. Article
  9. Quality control and signaling pathways at stalled ribosomes.Experimental & molecular medicine · 2026
    Review
  10. Article
  11. Review
  12. E2 variants for probing E3 ubiquitin ligase activities.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  13. Review
  14. Review
  15. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 5 institutions in 3 countries.

Shubo ZhaoDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany.
Jacqueline CordesDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany.
Karolina M CabanGene Center, Ludwig-Maximilians-Universität München, Munich, Germany.
Maximilian J GötzDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany.
Timur Mackens-KianiDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany.
Anthony J VeltriDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, USA.
Niladri K SinhaDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, USA.
Pedro WeickertDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany.
Selay KayaMax Planck Institute of Biochemistry, Martinsried, Germany.
Graeme HewittKing's College London School of Cancer & Pharmaceutical Sciences, London, UK.
Danny D NedialkovaMax Planck Institute of Biochemistry, Martinsried, Germany; Technical University of Munich, TUM School of Natural Sciences, Department of Bioscience, Garching, Germany.
Thomas FröhlichGene Center, Ludwig-Maximilians-Universität München, Munich, Germany.
Roland BeckmannDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany.
Allen R BuskirkDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, USA.
Rachel GreenDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, USA; Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, USA.
Julian StingeleDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany. Electronic address: stingele@genzentrum.lmu.de.
Ludwig-Maximilians-Universität München · DEJohns Hopkins Medicine · USJohns Hopkins University · USMax Planck Institute of Biochemistry · DEKing's College London · GB

Funding

The role of collisions in rescuing stalled ribosomes in bacteriaR01GM136960 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Allen Rowdon Buskirk · 2021 to 2026
$1.9M
European Research CouncilHoward Hughes Medical InstituteNIGMS NIH HHS R01 GM136960
6 · The paper itself

Abstract

Reactive aldehydes are abundant endogenous metabolites that challenge homeostasis by crosslinking cellular macromolecules. Aldehyde-induced DNA damage requires repair to prevent cancer and premature aging, but it is unknown whether cells also possess mechanisms that resolve aldehyde-induced RNA lesions. Here, we establish photoactivatable ribonucleoside-enhanced crosslinking (PAR-CL) as a model system to study RNA crosslinking damage in the absence of confounding DNA damage in human cells. We find that such RNA damage causes translation stress by stalling elongating ribosomes, which leads to collisions with trailing ribosomes and activation of multiple stress response pathways. Moreover, we discovered a translation-coupled quality control mechanism that resolves covalent RNA-protein crosslinks. Collisions between translating ribosomes and crosslinked mRNA-binding proteins trigger their modification with atypical K6- and K48-linked ubiquitin chains. Ubiquitylation requires the E3 ligase RNF14 and leads to proteasomal degradation of the protein adduct. Our findings identify RNA lesion-induced translational stress as a central component of crosslinking damage.

Indexed as

RNAUbiquitinAldehydesHumansProtein BiosynthesisRibosomesUbiquitinationUbiquitin-Protein LigasesAldehydesRNAUbiquitinUbiquitin-Protein Ligasesatypical ubiquitylationformaldehydeGCN1K6-linked ubiquitin chainsribosomeRNA damageRNA-protein crosslinksRNF14RNF25translation

Identifiers

PMID37951216
PMCPMC10783637
OpenAlexW4388551056

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.