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- Title
Enhanced phosphorylation of p53 by ATM in response to DNA damage.
- Authors
Banin, S; Moyal, L; Shieh, S; Taya, Y; Anderson, C W; Chessa, L; Smorodinsky, N I; Prives, C; Reiss, Y; Shiloh, Y; Ziv, Y
- 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 wortmannin-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-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.
- Publication
Science (New York, N.Y.), 1998, Vol 281, Issue 5383, p1674
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.281.5383.1674