Evidence map›Paper›PMID 24454762›Full record

ArticlePloS one2014

Ubiquitin-specific protease 5 is required for the efficient repair of DNA double-strand breaks.

Satoshi Nakajima, Li Lan, Leizhen Wei, Ching-Lung Hsieh, Vesna Rapić-Otrin, Akira Yasui, Arthur S Levine

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

39 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
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  5. Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025
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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

7 authors at 2 institutions in 2 countries.

Satoshi NakajimaDepartment of Microbiology and Molecular Genetics and University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, United States of America.
Li LanDepartment of Microbiology and Molecular Genetics and University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, United States of America.
Leizhen WeiDepartment of Microbiology and Molecular Genetics and University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, United States of America.
Ching-Lung HsiehDepartment of Microbiology and Molecular Genetics and University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, United States of America.
Vesna Rapić-OtrinDepartment of Microbiology and Molecular Genetics and University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, United States of America.
Akira YasuiDivision of the Dynamic Proteome, Institute of Development, Aging, and Cancer, Tohoku University, Sendai, Japan.
Arthur S LevineDepartment of Microbiology and Molecular Genetics and University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, United States of America.
UPMC Hillman Cancer Center · USTohoku University · JP

Funding

VECTOR CORE FACILITYP30CA047904 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Jessie Nedrow · 1988 to 2026
$158.0M
UNIVERSITY OF PITTSBURGH CLINICAL AND TRANSLATIONAL SCIENCE INSTITUTE: BPCAUL1RR024153 · NCRR · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI REIS, STEVEN E · 2006 to 2011
$73.9M
University of Pittsburgh Clinical and Translational Science InstituteUL1TR000005 · NCATS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI REIS, STEVEN E · 2012 to 2015
$50.8M
Oxidative DNA base damage and repair at telomeres and the relevance to cell senesR21AG045545 · NIA · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI LAN, LI, OPRESKO, PATRICIA L · 2013 to 2014
$422k
NCATS NIH HHS UL1 TR000005NCATS NIH HHS UL1TR000005NCI NIH HHS P30 CA047904NCI NIH HHS P30CA047904NCRR NIH HHS UL1 RR024153NIA NIH HHS R21 AG045545
6 · The paper itself

Abstract

During the DNA damage response (DDR), ubiquitination plays an important role in the recruitment and regulation of repair proteins. However, little is known about elimination of the ubiquitination signal after repair is completed. Here we show that the ubiquitin-specific protease 5 (USP5), a deubiquitinating enzyme, is involved in the elimination of the ubiquitin signal from damaged sites and is required for efficient DNA double-strand break (DSB) repair. Depletion of USP5 sensitizes cells to DNA damaging agents, produces DSBs, causes delayed disappearance of γH2AX foci after Bleocin treatment, and influences DSB repair efficiency in the homologous recombination pathway but not in the non-homologous end joining pathway. USP5 co-localizes to DSBs induced by laser micro-irradiation in a RAD18-dependent manner. Importantly, polyubiquitin chains at sites of DNA damage remained for longer periods in USP5-depleted cells. Our results show that disassembly of polyubiquitin chains by USP5 at sites of damage is important for efficient DSB repair.

Indexed as

DNA Breaks, Double-StrandedDNA RepairCell LineCell SurvivalDNA-Binding ProteinsEndopeptidasesGene Knockdown TechniquesHistonesHomologous RecombinationHumansKineticsUbiquitinUbiquitin-Protein LigasesX-RaysDNA-Binding ProteinsEndopeptidasesH2AX protein, humanHistonesRAD18 protein, humanUbiquitinubiquitin isopeptidaseUbiquitin-Protein Ligases

Identifiers

PMID24454762
PMCPMC3891734
OpenAlexW2054666944

What OpenQuestion holds

Textmetadata
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.