Evidence map›Paper›PMID 25487737›Full record

ArticleNature communications2014

Critical role of lysine 134 methylation on histone H2AX for γ-H2AX production and DNA repair.

Kenbun Sone, Lianhua Piao, Makoto Nakakido, Koji Ueda, Thomas Jenuwein, Yusuke Nakamura, Ryuji Hamamoto

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

68 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Lewy body dementia promotion by air pollutants.Science (New York, N.Y.) · 2025
    Article
  6. Article
  7. The Roles of H3K9me3 Writers, Readers, and Erasers in Cancer Immunotherapy.International journal of molecular sciences · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Histone H2A variants: Diversifying chromatin to ensure genome integrity.Seminars in cell & developmental biology · 2023
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Review

8 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

7 authors at 4 institutions in 3 countries.

Kenbun SoneSection of Hematology/Oncology, Department of Medicine, University of Chicago, 5841 South Maryland Avenue, MC2115, Chicago, Illinois 60637, USA.
Lianhua PiaoSection of Hematology/Oncology, Department of Medicine, University of Chicago, 5841 South Maryland Avenue, MC2115, Chicago, Illinois 60637, USA.
Makoto NakakidoSection of Hematology/Oncology, Department of Medicine, University of Chicago, 5841 South Maryland Avenue, MC2115, Chicago, Illinois 60637, USA.
Koji UedaGraduate School of Frontier Sciences, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
Thomas JenuweinMax Planck Institute of Immunobiology and Epigenetics, Stübeweg 51, D-79108 Freiburg, Germany.
Yusuke NakamuraSection of Hematology/Oncology, Department of Medicine, University of Chicago, 5841 South Maryland Avenue, MC2115, Chicago, Illinois 60637, USA.
Ryuji Hamamoto1] Section of Hematology/Oncology, Department of Medicine, University of Chicago, 5841 South Maryland Avenue, MC2115, Chicago, Illinois 60637, USA [2] Laboratory of Molecular Medicine, Human Genome Center, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
University of Chicago · USMax Planck Institute of Immunobiology and Epigenetics · DEThe University of Tokyo · JPTokyo University of Science · JP

Funding

Re-Engineering Translational Research at the University of ChicagoUL1TR000430 · NCATS · UNIVERSITY OF CHICAGO · PI SOLWAY, JULIAN · 2012 to 2016
$20.2M
NCATS NIH HHS UL1 TR000430
6 · The paper itself

Abstract

The presence of phosphorylated histone H2AX (γ-H2AX) is associated with the local activation of DNA-damage repair pathways. Although γ-H2AX deregulation in cancer has previously been reported, the molecular mechanism involved and its relationship with other histone modifications remain largely unknown. Here we find that the histone methyltransferase SUV39H2 methylates histone H2AX on lysine 134. When H2AX was mutated to abolish K134 methylation, the level of γ-H2AX became significantly reduced. We also found lower γ-H2AX activity following the introduction of double-strand breaks in Suv39h2 knockout cells or on SUV39H2 knockdown. Tissue microarray analyses of clinical lung and bladder tissues also revealed a positive correlation between H2AX K134 methylation and γ-H2AX levels. Furthermore, introduction of K134-substituted histone H2AX enhanced radio- and chemosensitivity of cancer cells. Overall, our results suggest that H2AX methylation plays a role in the regulation of γ-H2AX abundance in cancer.

Indexed as

DNA DamageDNA RepairGene Expression RegulationAnimalsCell SeparationChlorocebus aethiopsChromatinCOS CellsDNA Breaks, Double-StrandedFibroblastsFlow CytometryGamma RaysGenes, DominantHeLa CellsHistonesHumansChromatinHistonesLysineRNA, Small Interfering

Identifiers

PMID25487737
PMCPMC4268694
OpenAlexW2005715240

What OpenQuestion holds

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LicenceCC BY
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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.