Activation of the ATM kinase by ionizing radiation and phosphorylation of p53
Science, 1998•science.org
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 …
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 …
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.
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