Evidence map›Paper›PMID 23337116›Full record

ArticleThe Journal of cell biology2013

A noncatalytic function of the ligation complex during nonhomologous end joining.

Jessica Cottarel, Philippe Frit, Oriane Bombarde, Bernard Salles, Aurélie Négrel, Stéphanie Bernard, Penny A Jeggo, Michael R Lieber, Mauro Modesti, Patrick Calsou

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.9field-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

63 citing papers in PubMed, 99 citations in OpenAlex.

  1. Core NHEJ Factors Maintain Synapsis Across Diverse DNA End Structures.bioRxiv : the preprint server for biology · 2026
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  12. Phosphorylation of DNA-PKcs at the S2056 cluster ensures efficient and productive lymphocyte development in XLF-deficient mice.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
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  16. Article
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  19. Article
  20. Review

3 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

10 authors at 6 institutions in 3 countries.

Jessica CottarelCentre National de la Recherche Scientifique, Institut de Pharmacologie et de Biologie Structurale, Toulouse F-31077, Cedex 4, France.
Philippe Frit
Oriane Bombarde
Bernard Salles
Aurélie Négrel
Stéphanie Bernard
Penny A Jeggo
Michael R Lieber
Mauro Modesti
Patrick Calsou
Université Fédérale de Toulouse Midi-Pyrénées · FRAix-Marseille Université · FRCentre de Recherche en Cancérologie de Marseille · FRInstitut Paoli-Calmettes · FRUniversity of Southern California · USUniversity of Sussex · GB

Funding

MECHANISM AND REGULATION OF NONHOMOLOGOUS DNA ENDJOININGR01CA100504 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LIEBER, MICHAEL R · 2003 to 2021
$5.0M
NCI NIH HHS R01 CA100504Worldwide Cancer Research 09-0633
6 · The paper itself

Abstract

Nonhomologous end joining is the primary deoxyribonucleic acid (DNA) double-strand break repair pathway in multicellular eukaryotes. To initiate repair, Ku binds DNA ends and recruits the DNA-dependent protein kinase (DNA-PK) catalytic subunit (DNA-PKcs) forming the holoenzyme. Early end synapsis is associated with kinase autophosphorylation. The XRCC4 (X4)-DNA Ligase IV (LIG4) complex (X4LIG4) executes the final ligation promoted by Cernunnos (Cer)-X4-like factor (XLF). In this paper, using a cell-free system that recapitulates end synapsis and DNA-PKcs autophosphorylation, we found a defect in both activities in human cell extracts lacking LIG4. LIG4 also stimulated the DNA-PKcs autophosphorylation in a reconstitution assay with purified components. We additionally uncovered a kinase autophosphorylation defect in LIG4-defective cells that was corrected by ectopic expression of catalytically dead LIG4. Finally, our data support a contribution of Cer-XLF to this unexpected early role of the ligation complex in end joining. We propose that productive end joining occurs by early formation of a supramolecular entity containing both DNA-PK and X4LIG4-Cer-XLF complexes on DNA ends.

Indexed as

Cell-Free SystemCells, CulturedDNA-Activated Protein KinaseDNA-Binding ProteinsDNA DamageDNA End-Joining RepairDNA HelicasesDNA Ligase ATPDNA LigasesDNA Repair EnzymesGenomic InstabilityHoloenzymesHumansKu AutoantigenPhosphorylationDNA-Activated Protein KinaseDNA-Binding ProteinsDNA HelicasesDNA Ligase ATPDNA LigasesDNA Repair EnzymesHoloenzymesKu AutoantigenLIG4 protein, humanNHEJ1 protein, humanXRCC4 protein, humanXRCC5 protein, human

Identifiers

PMID23337116
PMCPMC3549972
OpenAlexW2158099110

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.