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. 1998 Sep 11;281(5383):1674-7.
doi: 10.1126/science.281.5383.1674.

Enhanced phosphorylation of p53 by ATM in response to DNA damage (V体育平台登录)

S Banin  1 , L Moyal, S Shieh, Y Taya, C W Anderson, L Chessa, N I Smorodinsky, C Prives, Y Reiss, Y Shiloh, Y Ziv
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Enhanced phosphorylation of p53 by ATM in response to DNA damage

S Banin et al. Science. .

Abstract (V体育ios版)

The ATM protein, encoded by the gene responsible for the human genetic disorder ataxia telangiectasia (A-T), regulates several cellular responses to DNA breaks. ATM shares a phosphoinositide 3-kinase-related domain with several proteins, some of them protein kinases. A wortmannin-sensitive protein kinase activity was associated with endogenous or recombinant ATM and was abolished by structural ATM mutations VSports手机版. In vitro substrates included the translation repressor PHAS-I and the p53 protein. ATM phosphorylated p53 in vitro on a single residue, serine-15, which is phosphorylated in vivo in response to DNA damage. This activity was markedly enhanced within minutes after treatment of cells with a radiomimetic drug; the total amount of ATM remained unchanged. Various damage-induced responses may be activated by enhancement of the protein kinase activity of ATM. .

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