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.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 27, 2002, 5:43 a.m.) |
Deposited | 1 year, 7 months ago (Jan. 12, 2024, 10:25 p.m.) |
Indexed | 3 days, 11 hours ago (Aug. 26, 2025, 2:50 a.m.) |
Issued | 26 years, 11 months ago (Sept. 11, 1998) |
Published | 26 years, 11 months ago (Sept. 11, 1998) |
Published Print | 26 years, 11 months ago (Sept. 11, 1998) |
@article{Banin_1998, title={Enhanced Phosphorylation of p53 by ATM in Response to DNA Damage}, volume={281}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.281.5383.1674}, DOI={10.1126/science.281.5383.1674}, number={5383}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Banin, S. and Moyal, L. and Shieh, S.-Y. and Taya, Y. and Anderson, C. W. and Chessa, L. and Smorodinsky, N. I. and Prives, C. and Reiss, Y. and Shiloh, Y. and Ziv, Y.}, year={1998}, month=sep, pages={1674–1677} }