ATM recognizes H2AFX-Nucleosomes

Stable Identifier
R-HSA-5693602
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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H2AFX (also known as H2AX) is a variant of histone H2A and is present in a portion of nucleosomes. While H2AFX-containing nucleosomes (H2AFX-nucleosomes) are not specifically recruited to the sites of DNA double strand breaks (DSBs), ATM recognizes the carboxyl tails of H2AFX on H2AFX-nucleosomes in the vicinity of DSBs as a suitable phosphorylation substrate. The phosphorylated H2AFX (gamma-H2AX) plays a crucial role in the retention of DNA repair proteins at DSBs, manifested in the formation of ionizing radiation-induced foci (Paull et al. 2000, Celeste et al. 2002, Redon et al. 2002, Celeste et al. 2003, Fernandez-Capetillo et al. 2004).

Literature References
PubMed ID Title Journal Year
11934988 Genomic instability in mice lacking histone H2AX

Celeste, A, Petersen, S, Romanienko, PJ, Fernandez-Capetillo, O, Chen, HT, Sedelnikova, OA, Reina-San-Martin, B, Coppola, V, Meffre, E, Difilippantonio, MJ, Redon, C, Pilch, DR, Olaru, A, Eckhaus, M, Camerini-Otero, RD, Tessarollo, L, Livak, F, Manova, K, Bonner, WM, Nussenzweig, MC, Nussenzweig, A

Science 2002
11893489 Histone H2A variants H2AX and H2AZ

Redon, C, Pilch, D, Rogakou, E, Sedelnikova, O, Newrock, K, Bonner, W

Curr. Opin. Genet. Dev. 2002
10959836 A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage.

Paull, TT, Rogakou, EP, Yamazaki, V, Kirchgessner, CU, Gellert, M, Bonner, WM

Curr Biol 2000
12792649 Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks.

Celeste, A, Fernandez-Capetillo, O, Kruhlak, MJ, Pilch, DR, Staudt, DW, Lee, A, Bonner, RF, Bonner, WM, Nussenzweig, A

Nat Cell Biol 2003
15279782 H2AX: the histone guardian of the genome

Fernandez-Capetillo, O, Lee, A, Nussenzweig, M, Nussenzweig, A

DNA Repair (Amst.) 2004
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