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

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.
Publisher
AMER ASSOC ADVANCEMENT SCIENCE
Issue Date
1998-09
Language
ENG
Keywords

CELL-CYCLE CHECKPOINT; ATAXIA-TELANGIECTASIA CELLS; PROTEIN-KINASE; DNA-DAMAGE; PATHWAYS; RECOMBINATION; INDUCTION; PRODUCT; DEFECT; MDM2

Citation

SCIENCE, v.281, no.5383, pp.1677 - 1679

ISSN
0036-8075
DOI
10.1126/science.281.5383.1677
URI
http://hdl.handle.net/10203/74858
Appears in Collection
BS-Journal Papers(저널논문)
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