Phosphorylation of H2AX at S139 by ATM at the site of DSB

Stable Identifier
R-GGA-351434
Type
Reaction [transition]
Species
Gallus gallus
Compartment
nucleoplasm
ReviewStatus
5/5
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Phosphorylation of H2AX at S139 by ATM at the site of DSB
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The DNA double strand break triggers various checkpoint switches and repair processes. One of the earliest responses is the phosphorylation of histone H2AX at serine 139 (yielding gamma-H2AX) by phosphotidylinositol-3-kinase family kinases DNA-PK, ATR and ATM. The response is highly amplified with several hundred to several thousand H2AX molecules being phosphorylated in the chromatin around each DSB. A role for gamma-H2AX in the DNA damage signaling cascade has been suggested by the findings that gamma-H2AX facilitates the recruitment and retention of a number of damage-sensitive checkpoint proteins, such as the Mre11/Nbs1/Rad50 (MRN) complex, Brca1, 53BP1, and NFBD1/MDC1 to the DSB site.
Literature References
PubMed ID Title Journal Year
15059890 ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation

Stiff, T, O'Driscoll, M, Rief, N, Iwabuchi, K, Lobrich, M, Jeggo, PA

Cancer Res 2004
17123873 Collaborative roles of gammaH2AX and the Rad51 paralog Xrcc3 in homologous recombinational repair

Sonoda, E, Zhao, GY, Kohzaki, M, Dhar, PK, Kikuchi, K, Redon, C, Pilch, DR, Bonner, WM, Nakano, A, Watanabe, M, Nakayama, T, Takeda, S, Takami, Y

DNA Repair (Amst) 2007
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Output
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as an event of
Catalyst Activity

protein serine/threonine kinase activity of PI3-kinase family [nucleoplasm]

Physical Entity
PI3-kinase family [nucleoplasm] (Gallus gallus)
Activity
protein serine/threonine kinase activity (GO:0004674)
Authored
Saxena, A  (2008-07-07)
Reviewed
Borowiec, JA  (2009-04-24)
Created
Saxena, A  (2008-05-23)
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