Evidence map›Paper›PMID 19332554›Full record

ArticleMolecular and cellular biology2009

Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4.

Peï-Yu Wu, Philippe Frit, SriLakshmi Meesala, Stéphanie Dauvillier, Mauro Modesti, Sara N Andres, Ying Huang, JoAnn Sekiguchi, Patrick Calsou, Bernard Salles and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. 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
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

77 citing papers in PubMed, 148 citations in OpenAlex.

  1. Article
  2. BRCA1-A and LIG4 complexes mediate ecDNA biogenesis and cancer drug resistance.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Biomolecular NMR assignments · 2021
    Article
  17. Review
  18. Article
  19. Review
  20. Article

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

11 authors at 5 institutions in 3 countries.

Peï-Yu WuCNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), Toulouse, France.
Philippe Frit
SriLakshmi Meesala
Stéphanie Dauvillier
Mauro Modesti
Sara N Andres
Ying Huang
JoAnn Sekiguchi
Patrick Calsou
Bernard Salles
Murray S Junop
McMaster University · CACentre National de la Recherche Scientifique · FRUniversité Fédérale de Toulouse Midi-Pyrénées · FRUniversité Toulouse III - Paul Sabatier · FRUniversity of Michigan · US

Funding

Roles of the Artemis nuclease in DNA repair and diseaseR01AI063058 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SEKIGUCHI, JOANN · 2005 to 2013
$3.0M
NIAID NIH HHS R01 AI063058
6 · The paper itself

Abstract

Nonhomologous end-joining represents the major pathway used by human cells to repair DNA double-strand breaks. It relies on the XRCC4/DNA ligase IV complex to reseal DNA strands. Here we report the high-resolution crystal structure of human XRCC4 bound to the carboxy-terminal tandem BRCT repeat of DNA ligase IV. The structure differs from the homologous Saccharomyces cerevisiae complex and reveals an extensive DNA ligase IV binding interface formed by a helix-loop-helix structure within the inter-BRCT linker region, as well as significant interactions involving the second BRCT domain, which induces a kink in the tail region of XRCC4. We further demonstrate that interaction with the second BRCT domain of DNA ligase IV is necessary for stable binding to XRCC4 in cells, as well as to achieve efficient dominant-negative effects resulting in radiosensitization after ectopic overexpression of DNA ligase IV fragments in human fibroblasts. Together our findings provide unanticipated insight for understanding the physical and functional architecture of the nonhomologous end-joining ligation complex.

Indexed as

DNA RepairAmino Acid SequenceBinding, CompetitiveCell LineDNA-Binding ProteinsDNA Breaks, Double-StrandedDNA Ligase ATPDNA LigasesDNA Repair EnzymesDown-RegulationHumansMolecular Sequence DataProtein BindingProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryDNA-Binding ProteinsDNA Ligase ATPDNA LigasesDNA Repair EnzymesDNL4 protein, S cerevisiaeLIG4 protein, humanNHEJ1 protein, humanXRCC4 protein, human

Identifiers

PMID19332554
PMCPMC2682001
OpenAlexW2161115929

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.