Activation of the ATM kinase by ionizing radiation and phosphorylation of p53.

Journal Article (Journal Article)

The p53 tumor suppressor protein is activated and phosphorylated on serine-15 in response to various DNA damaging agents. The gene product mutated in ataxia telangiectasia, ATM, acts upstream of p53 in a signal transduction pathway initiated by ionizing radiation. Immunoprecipitated ATM had intrinsic protein kinase activity and phosphorylated p53 on serine-15 in a manganese-dependent manner. Ionizing radiation, but not ultraviolet radiation, rapidly enhanced this p53-directed kinase activity of endogenous ATM. These observations, along with the fact that phosphorylation of p53 on serine-15 in response to ionizing radiation is reduced in ataxia telangiectasia cells, suggest that ATM is a protein kinase that phosphorylates p53 in vivo.

Full Text

Duke Authors

Cited Authors

  • Canman, CE; Lim, DS; Cimprich, KA; Taya, Y; Tamai, K; Sakaguchi, K; Appella, E; Kastan, MB; Siliciano, JD

Published Date

  • September 11, 1998

Published In

Volume / Issue

  • 281 / 5383

Start / End Page

  • 1677 - 1679

PubMed ID

  • 9733515

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.281.5383.1677


  • eng

Conference Location

  • United States