H2AX post-translational modifications in the ionizing radiation response and homologous recombination
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Histone H2AX phosphorylation on a C-terminal serine residue to form "γ-H2AX" is a critical early event in the chromatin response to chromosomal DNA double strand breaks in eukaryotes. In mammalian cells, γ-H2AX is formed when H2AX is phosphorylated on serine 139 by ATM or by other DNA damage response kinases. H2AX prevents genomic instability and tumorigenesis, and supports class-switch recombination at immunoglobulin heavy chain loci in mammals. We showed previously that H2AX controls double strand break repair by homologous recombination (HR) between sister chromatids. The HR functions of H2AX are mediated by interaction of γ-H2AX with the chromatin-associated adaptor protein MDC1. H2AX is potentially subject to additional post-translational modifications associated with the DNA damage response and with other chromatin functions. To test this idea, we used mass spectroscopy to identify H2AX residues additional to serine 139 that are post-translationally modified following exposure of cells to ionizing radiation (IR) and identified several new IR-responsive residues of H2AX. We determined the impact of IR-responsive H2AX residues on cellular resistance to IR and on H2AX-dependent HR, and also analyzed the contribution to HR of other known or potential post-translationally modified residues of H2AX. The results suggest that the HR and IR-resistance functions of H2AX are controlled in large part by specific MDC1-interacting residues of H2AX, but that additional H2AX residues modulate these core functions of H2AX.
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ATR- and ATM-mediated phosphorylation of BRCA1 and H2AX is needed for S and G2/M checkpoints and HR-mediated DNA repair during S and G2.
“Moreover, ATR- and ATM-mediated phosphorylation of BRCA1 and H2AX [22, 23] is required for S and G2/M phase checkpoints and homologous recombination (HR)-mediated DNA repair during S and G2 phases.”
From NER initiation factors, DDB2 and XPC, regulate UV radiation response by recruiting ATR and ATM kinases to DNA damage sites (2013) · cites this paper as [22]
ATR and ATM allow H2AX phosphorylation and spreading at damage sites, which changes chromatin structure near the damage and executes DNA repair through the HR pathway.
“Additionally, it is well established that ATR and ATM allow H2AX phosphorylation and spreading at the damage site, which changes the chromatin structure near the damage site and executes DNA repair through the HR pathway [21-23, 26, 63].”
From NER initiation factors, DDB2 and XPC, regulate UV radiation response by recruiting ATR and ATM kinases to DNA damage sites (2013) · cites this paper as [22]
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- Authors
- Xie, A., Odate, S., Chandramouly, G., & Scully, R. A.
- Affiliations
- Beth Israel Deaconess Medical Center (US)
- Harvard University (US)
- Corresponding author
- Scully, Ralph A.
- Venue
- Cell Cycle
- Publisher
- Informa UK Limited
- Published
- 2010-09
- Volume
- 9
- Issue
- 17
- Pages
- 3602-3610
- ISSN
- 1538-4101 (ISSN-L)
- 1551-4005
- PMC
- PMC2980696
- OpenAlex
- W1964303708
- Cited by
- 59
- References
- 46
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 4 · 2022: 5 · 2021: 2 · 2020: 3 · 2019: 4 · 2018: 3 · 2017: 2 · 2016: 3 · 2015: 4 · 2014: 3 · 2013: 6 · 2012: 6
- FWCI
- 2.47
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cell Cycle (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Leukemia and Lymphoma Society (GM073894)
- National Institutes of Health
- National Cancer Institute (RC1CA145867, CA095175, R01CA095175)
- National Institute of General Medical Sciences (GM 073894, R01GM073894)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Effects of Radiation Exposure
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- H2AX, post-translational modification, ionizing radiation response, homologous recombination, DNA double-strand break repair, MDC1, ATM, DNA damage response, ionizing radiation resistance, genomic instability, class switch recombination
- MeSH terms
- Animals, DNA Repair, DNA-Binding Proteins, Histones, Mutation, Protein Processing, Post-Translational, Radiation, Ionizing, Recombination, Genetic, Mass Spectrometry, Cell Cycle Proteins, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Mice, Embryonic Stem Cells, DNA Breaks, Double-Stranded
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