Evidence map›Paper›PMID 27716483›Full record

ArticleMolecular cell2016

VCP/p97 Extracts Sterically Trapped Ku70/80 Rings from DNA in Double-Strand Break Repair.

Johannes van den Boom, Markus Wolf, Lena Weimann, Nina Schulze, Fanghua Li, Farnusch Kaschani, Anne Riemer, Christian Zierhut, Markus Kaiser, George Iliakis and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

77 citing papers in PubMed, 112 citations in OpenAlex.

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  15. Identification of the main barriers to Ku accumulation in chromatin.bioRxiv : the preprint server for biology · 2024
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17 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

12 authors at 2 institutions in 2 countries.

Johannes van den BoomMolecular Biology I, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Markus WolfMolecular Biology I, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Lena WeimannMolecular Biology I, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Nina SchulzeICCE, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Fanghua LiInstitute of Medical Radiation Biology, Medical School, University of Duisburg-Essen, 45122 Essen, Germany.
Farnusch KaschaniChemical Proteomics, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Anne RiemerMolecular Biology I, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
Christian ZierhutLaboratory of Chromosome and Cell Biology, The Rockefeller University, New York, NY 10065, USA.
Markus KaiserChemical Proteomics, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany.
George IliakisInstitute of Medical Radiation Biology, Medical School, University of Duisburg-Essen, 45122 Essen, Germany.
Hironori FunabikiLaboratory of Chromosome and Cell Biology, The Rockefeller University, New York, NY 10065, USA.
Hemmo MeyerMolecular Biology I, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany. Electronic address: hemmo.meyer@uni-due.de.
University of Duisburg-Essen · DERockefeller University · US

Funding

Roles of Chromosomal Factors in Chromosome SegregationR01GM075249 · NIGMS · ROCKEFELLER UNIVERSITY · PI FUNABIKI, HIRONORI · 2005 to 2018
$4.5M
NIGMS NIH HHS R01 GM075249
6 · The paper itself

Abstract

During DNA double-strand break (DSB) repair, the ring-shaped Ku70/80 complex becomes trapped on DNA and needs to be actively extracted, but it has remained unclear what provides the required energy. By means of reconstitution of DSB repair on beads, we demonstrate here that DNA-locked Ku rings are released by the AAA-ATPase p97. To achieve this, p97 requires ATP hydrolysis, cooperates with the Ufd1-Npl4 ubiquitin-adaptor complex, and specifically targets Ku80 that is modified by K48-linked ubiquitin chains. In U2OS cells, chemical inhibition of p97 or siRNA-mediated depletion of p97 or its adapters impairs Ku80 removal after non-homologous end joining of DSBs. Moreover, this inhibition attenuates early steps in homologous recombination, consistent with p97-driven Ku release also affecting repair pathway choice. Thus, our data answer a central question regarding regulation of Ku in DSB repair and illustrate the ability of p97 to segregate even tightly bound protein complexes for release from DNA.

Indexed as

DNA End-Joining RepairRecombinational DNA RepairAdenosine TriphosphatasesAdenosine TriphosphateAmphibian ProteinsAnimalsCell Cycle ProteinsCell Line, TumorDNADNA Breaks, Double-StrandedGene Expression RegulationHumansHydrolysisKu AutoantigenMicrospheresOsteoblastsAdenosine TriphosphatasesAdenosine TriphosphateAmphibian ProteinsCell Cycle ProteinsDNAKu AutoantigenRNA, Small InterferingValosin Containing ProteinVCP protein, humanchromatinDNA repairdouble strand breakhomologous recombinationKuKu80NHEJp97VCP

Identifiers

PMID27716483
PMCPMC5161236
OpenAlexW2527759270

What OpenQuestion holds

Textmetadata
LicenceTDM
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.