Histone H2AX participates the DNA damage-induced ATM activation through interaction with NBS1

Junya Kobayashi, Hiroshi Tauchi, Benjamin Chen, Sandeep Bruma, Satoshi Tashiro, Shinya Matsuura, Keiji Tanimoto, David J. Chen, Kenshi Komatsu

Research output: Contribution to journalArticlepeer-review

24 Scopus citations


Phosphorylated histone H2AX (γ-H2AX) functions in the recruitment of DNA damage response proteins to DNA double-strand breaks (DSBs) and facilitates DSB repair. ATM also co-localizes with γ-H2AX at DSB sites following its auto-phosphorylation. However, it is unclear whether γ-H2AX has a role in activation of ATM-dependent cell cycle checkpoints. Here, we show that ATM as well as NBS1 is recruited to damaged-chromatin in a γ-H2AX-dependent manner. Foci formation of phosphorylated ATM and ATM-dependent phosphorylation is repressed in H2AX-knockdown cells. Furthermore, anti-γ-H2AX antibody co-immunoprecipitates an ATM-like protein kinase activity in vitro and recombinant H2AX increases in vitro kinase activity of ATM from un-irradiated cells. Moreover, H2AX-deficient cells exhibited a defect in ATM-dependent cell cycle checkpoints. Taken together, γ-H2AX has important role for effective DSB-dependent activation of ATM-related damage responses via NBS1.

Original languageEnglish (US)
Pages (from-to)752-757
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Mar 20 2009


  • ATM
  • Cell cycle checkpoint
  • DNA double-strand breaks
  • Histone H2AX
  • NBS1

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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