TY - JOUR
T1 - Activation of the ATM kinase by ionizing radiation and phosphorylation of p53
AU - Canman, Christine E.
AU - Lim, Dae Sik
AU - Cimprich, Karlene A.
AU - Taya, Yoichi
AU - Tamai, Katsuyuki
AU - Sakaguchi, Kazuyasu
AU - Appella, Ettore
AU - Kastan, Michael B.
AU - Siliciano, Janet D.
PY - 1998/9/11
Y1 - 1998/9/11
N2 - 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.
AB - 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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U2 - 10.1126/science.281.5383.1677
DO - 10.1126/science.281.5383.1677
M3 - Article
C2 - 9733515
AN - SCOPUS:0032508608
VL - 281
SP - 1677
EP - 1679
JO - Science
JF - Science
SN - 0036-8075
IS - 5383
ER -