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Papers In Press, published online ahead of print January 6, 2003
Radiation Biology and Oncology, Queensland Institute of Medical Research, Herston, Qld 4029
Corresponding Author: nuriG{at}qimr.edu.au
ATM, mutated in the human disorder ataxia-telangiectasia is rapidly activated by DNA double strand breaks. The mechanism of activation remains unresolved and it is uncertain whether autophosphorylation contributes to activation. We describe an in vitro immunoprecipitation system demonstrating activation of ATM kinase from unirradiated extracts by pre-incubation with ATP. Activation is both time - and ATP concentration - dependent, other nucleotides fail to activate ATM and DNA is not required. ATP activation is specific for ATM since it is not observed with kinase dead ATM, it requires Mn2+ and is inhibited by wortmannin. Exposure of activated ATM to phosphatase abrogates activity and repeat cycles of ATP and phosphatase treatment reveal a requirement for autophosphorylation in the activation process. Phosphopeptide mapping revealed similarities between the patterns of autophosphorylation for irradiated and ATP treated ATM. Caffeine inhibited ATM kinase activity for substrates but did not interefere with ATM autophosphorylation. ATP failed to activate either ATR or DNA-PK under these conditions supporting the specificity for ATM. These data demonstrate that ATP can specifically induce activation of ATM by a mechanism involving autophosphorylation. The relationship of this form of activation to DNA damage activation remains unclear but represents a useful model for understanding in vivo activation.
J. Biol. Chem, 10.1074/jbc.M300003200
Submitted on January 1, 2003
Revised on January 6, 2003
Accepted on January 6, 2003
ATP activates ATM in vitro: importance of autophosphorylation
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