ATM associates with and phosphorylates p53: mapping the region of interaction View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1998-12

AUTHORS

Kum Kum Khanna., Katherine E. Keating, Sergei Kozlov, Shaun Scott, Magtouf Gatei, Karen Hobson, Yoichi Taya, Brian Gabrielli, Doug Chan, Susan P. Lees-Miller, Martin F. Lavin

ABSTRACT

The human genetic disorder ataxia-telangiectasia (AT) is characterized by immunodeficiency, progressive cerebellar ataxia, radiosensitivity, cell cycle checkpoint defects and cancer predisposition1. The gene mutated in this syndrome, ATM (for AT mutated), encodes a protein containing a phosphatidyl-inositol 3-kinase (PI-3 kinase)-like domain2,3. ATM also contains a proline-rich region4 and a leucine zipper2,5, both of which implicate this protein in signal transduction. The proline-rich region has been shown to bind to the SH3 domain of c-Abl, which facilitates its phosphorylation and activation by ATM (Refs 4,6). Previous results have demonstrated that AT cells are defective in the G1/S checkpoint activated after radiation damage and that this defect is attributable to a defective p53 signal transduction pathway7,8. We report here direct interaction between ATM and p53 involving two regions in ATM, one at the amino terminus and the other at the carboxy terminus, corresponding to the PI-3 kinase domain. Recombinant ATM protein phosphorylates p53 on serine 15 near the N terminus. Furthermore, ectopic expression of ATM in AT cells restores normal ionizing radiation (IR)-induced phosphorylation of p53, whereas expression of ATM antisense RNA in control cells abrogates the rapid IR-induced phosphorylation of p53 on serine 15. These results demonstrate that ATM can bind p53 directly and is responsible for its serine 15 phosphorylation, thereby contributing to the activation and stabilization of p53 during the IR-induced DNA damage response. More... »

PAGES

398-400

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/3882

DOI

http://dx.doi.org/10.1038/3882

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012299542

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9843217


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