Evidence map›Paper›PMID 22909820›Full record

ArticleThe EMBO journal2012

The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response.

Laura R Butler, Ruth M Densham, Junying Jia, Alexander J Garvin, Helen R Stone, Vandna Shah, Daniel Weekes, Frederic Festy, James Beesley, Joanna R Morris

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
7.1field-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

102 citing papers in PubMed, 162 citations in OpenAlex.

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  11. DNA damage-induced proteasome phosphorylation controls substrate recognition and facilitates DNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  18. Deubiquitylating Enzymes in Cancer and Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  19. Review
  20. Article

42 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 1 country.

Laura R ButlerSchool of Cancer Sciences, College of Medical & Dental Sciences, University of Birmingham, Birmingham, UK.
Ruth M Densham
Junying Jia
Alexander J Garvin
Helen R Stone
Vandna Shah
Daniel Weekes
Frederic Festy
James Beesley
Joanna R Morris
University of Birmingham · GBBirmingham Dental Hospital · GBBreast Cancer Now · GBKing's College Hospital · GBKing's College London · GB

Funding

Cancer Research UK 15265Cancer Research UK C8820/A15265Cancer Research UK C8820/A9494Medical Research Council 6900577
6 · The paper itself

Abstract

The regulation of Ubiquitin (Ub) conjugates generated by the complex network of proteins that promote the mammalian DNA double-strand break (DSB) response is not fully understood. We show here that the Ub protease POH1/rpn11/PSMD14 resident in the 19S proteasome regulatory particle is required for processing poly-Ub formed in the DSB response. Proteasome activity is required to restrict tudor domain-dependent 53BP1 accumulation at sites of DNA damage. This occurs both through antagonism of RNF8/RNF168-mediated lysine 63-linked poly-Ub and through the promotion of JMJD2A retention on chromatin. Consistent with this role POH1 acts in opposition to RNF8/RNF168 to modulate end-joining DNA repair. Additionally, POH1 acts independently of 53BP1 in homologous recombination repair to promote RAD51 loading. Accordingly, POH1-deficient cells are sensitive to DNA damaging agents. These data demonstrate that proteasomal POH1 is a key de-ubiquitinating enzyme that regulates ubiquitin conjugates generated in response to damage and that several aspects of the DSB response are regulated by the proteasome.

Indexed as

DNA Breaks, Double-StrandedCell LineChromatinDNA-Binding ProteinsDNA RepairHumansIntracellular Signaling Peptides and ProteinsJumonji Domain-Containing Histone DemethylasesLysinePolyubiquitinProteasome Endopeptidase ComplexRad51 RecombinaseTrans-ActivatorsTumor Suppressor p53-Binding Protein 1Ubiquitin-Protein LigasesChromatinDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsJumonji Domain-Containing Histone DemethylasesKDM4A protein, humanLysinePolyubiquitinProteasome Endopeptidase ComplexPSMD14 protein, humanRAD51 protein, humanRad51 RecombinaseRNF168 protein, humanRNF8 protein, humanTP53BP1 protein, humanTrans-ActivatorsTumor Suppressor p53-Binding Protein 1Ubiquitin-Protein Ligases

Identifiers

PMID22909820
PMCPMC3463844
OpenAlexW2128114411

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.