Evidence map›Paper›PMID 25622294›Full record

ArticleNature structural & molecular biology2015

K63 polyubiquitination is a new modulator of the oxidative stress response.

Gustavo M Silva, Daniel Finley, Christine Vogel

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed
10.5field-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

131 citing papers in PubMed, 223 citations in OpenAlex.

  1. Article
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  12. Ribosome-associated proteins: unwRAPping ribosome heterogeneity in the twenty-first century.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  13. Article
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  20. Review

71 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

3 authors at 2 institutions in 1 country.

Gustavo M SilvaCenter for Genomics and Systems Biology, New York University, New York, New York, USA.ORCID 000000019476069X
Daniel FinleyDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.
Christine VogelCenter for Genomics and Systems Biology, New York University, New York, New York, USA.ORCID 0000000228563118
New York University · USHarvard University · US

Funding

Functional Analysis of the Proteasome BaseR37GM043601 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FINLEY, DANIEL J · 2004 to 2013
$5.9M
UBIQUITIN-PROTEIN CONJUGATES AND FUSIONSR01GM043601 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FINLEY, DANIEL J · 1990 to 2020
$4.3M
Robust statistical approaches for decoding protein and mRNA expression regulationR01GM113237 · NIGMS · NEW YORK UNIVERSITY · PI VOGEL, CHRISTINE · 2014 to 2017
$1.5M
NIGMS NIH HHS GM43601NIGMS NIH HHS R01 GM043601NIGMS NIH HHS R01 GM113237NIGMS NIH HHS R37 GM043601
6 · The paper itself

Abstract

Ubiquitination is a post-translational modification that signals multiple processes, including protein degradation, trafficking and DNA repair. Polyubiquitin accumulates globally during the oxidative stress response, and this has been mainly attributed to increased ubiquitin conjugation and perturbations in protein degradation. Here we show that the unconventional Lys63 (K63)-linked polyubiquitin accumulates in the yeast Saccharomyces cerevisiae in a highly sensitive and regulated manner as a result of exposure to peroxides. We demonstrate that hydrogen peroxide inhibits the deubiquitinating enzyme Ubp2, leading to accumulation of K63 conjugates assembled by the Rad6 ubiquitin conjugase and the Bre1 ubiquitin ligase. Using linkage-specific isolation methods and stable isotope labeling by amino acids in cell culture (SILAC)-based quantitative proteomics, we identified >100 new K63-polyubiquitinated targets, which were substantially enriched in ribosomal proteins. Finally, we demonstrate that impairment of K63 ubiquitination during oxidative stress affects polysome stability and protein expression, rendering cells more sensitive to stress, and thereby reveal a new redox-regulatory role for this modification.

Indexed as

EndopeptidasesLysineOxidative StressPolyubiquitinProtein Processing, Post-TranslationalProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationUbiquitin-Conjugating EnzymesBre1 protein, S cerevisiaeEndopeptidasesLysinePolyubiquitinRAD6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating Enzymesubiquitin-Nalpha-protein hydrolase

Identifiers

PMID25622294
PMCPMC4318705
OpenAlexW2010691148

What OpenQuestion holds

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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.