Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2010-08-29

AUTHORS

Kyle M Miller, Jorrit V Tjeertes, Julia Coates, Gaëlle Legube, Sophie E Polo, Sébastien Britton, Stephen P Jackson

ABSTRACT

How changes in chromatin can modulate the repair pathway of DNA double-strand breaks is now investigated. The work shows that histone deacetylases HDAC1 and HDAC2 are recruited to sites of DNA damage, where they mediate the removal of H3K56 acetyl marks, and their activity is important for repair via non-homologous end-joining. More... »

PAGES

1144-1151

References to SciGraph publications

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  • 2007-06-20. Chromatin dynamics and the preservation of genetic information in NATURE
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  • 2005-04. DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis in NATURE
  • 2005-04. Activation of the DNA damage checkpoint and genomic instability in human precancerous lesions in NATURE
  • 2005-12-11. Histone acetylation by Trrap–Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks in NATURE CELL BIOLOGY
  • 2006-11-01. Oncogene-induced senescence is part of the tumorigenesis barrier imposed by DNA damage checkpoints in NATURE
  • 2005-03-13. Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer in NATURE GENETICS
  • 2008-11-13. γH2AX and cancer in NATURE REVIEWS CANCER
  • 2010-01-06. DNA resection in eukaryotes: deciding how to fix the break in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2007-08-13. Histone deacetylases and cancer in ONCOGENE
  • 2008-07. Living on a break: cellular senescence as a DNA-damage response in NATURE REVIEWS CANCER
  • 2008-03. The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men in NATURE REVIEWS MOLECULAR CELL BIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nsmb.1899

    DOI

    http://dx.doi.org/10.1038/nsmb.1899

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1019375204

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/20802485


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