Enhanced phosphorylation of p53 by ATM in response to DNA damage

S. Banin, L. Moyal, S. Y. Shieh, Y. Taya, C. W. Anderson, L. Chessa, N. I. Smorodinsky, C. Prives, Y. Reiss, Y. Shiloh*, Y. Ziv

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

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 worthmannin-sensitive protein kinase activity was associated with endogenous or recombinant ATM and was abolished by structural ATM mutations. In vitro substrates included the translation repressor PHAS-1 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.

Original languageEnglish
Pages (from-to)1674-1677
Number of pages4
JournalScience
Volume281
Issue number5383
DOIs
StatePublished - 11 Sep 1998

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