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[Cancer Research 64, 9152-9159, December 15, 2004]
© 2004 American Association for Cancer Research

Regular Articles

Identification and Characterization of a Novel and Specific Inhibitor of the Ataxia-Telangiectasia Mutated Kinase ATM

Ian Hickson1, Yan Zhao2, Caroline J. Richardson1, Sharon J. Green1, Niall M. B. Martin1, Alisdair I. Orr1, Philip M. Reaper3, Stephen P. Jackson3, Nicola J. Curtin2 and Graeme C. M. Smith1

1 KuDOS Pharmaceuticals Ltd., Cambridge Science Park, Milton Road, Cambridge; 2 Northern Institute for Cancer Research, Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne; and 3 Wellcome Trust and Cancer Research UK Gurdon Institute and Department of Zoology, Cambridge University, Cambridge, United Kingdom

The serine/threonine protein kinase ATM signals to cell cycle and DNA repair components by phosphorylating downstream targets such as p53, CHK2, NBS1, and BRCA1. Mutation of ATM occurs in the human autosomal recessive disorder ataxia-telangiectasia, which is characterized by hypersensitivity to ionizing radiation and a failure of cells to arrest the cell cycle after the induction of DNA double-strand breaks. It has thus been proposed that ATM inhibition would cause cellular radio- and chemosensitization. Through screening a small molecule compound library developed for the phosphatidylinositol 3'-kinase–like kinase family, we identified an ATP-competitive inhibitor, 2-morpholin-4-yl-6-thianthren-1-yl-pyran-4-one (KU-55933), that inhibits ATM with an IC50 of 13 nmol/L and a Ki of 2.2 nmol/L. KU-55933 shows specificity with respect to inhibition of other phosphatidylinositol 3'-kinase–like kinases. Cellular inhibition of ATM by KU-55933 was demonstrated by the ablation of ionizing radiation-dependent phosphorylation of a range of ATM targets, including p53, {gamma}H2AX, NBS1, and SMC1. KU-55933 did not show inhibition of UV light DNA damage induced cellular phosphorylation events. Exposure of cells to KU-55933 resulted in a significant sensitization to the cytotoxic effects of ionizing radiation and to the DNA double-strand break-inducing chemotherapeutic agents, etoposide, doxorubicin, and camptothecin. Inhibition of ATM by KU-55933 also caused a loss of ionizing radiation-induced cell cycle arrest. By contrast, KU-55933 did not potentiate the cytotoxic effects of ionizing radiation on ataxia-telangiectasia cells, nor did it affect their cell cycle profile after DNA damage. We conclude that KU-55933 is a novel, specific, and potent inhibitor of the ATM kinase.




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Inhibition of poly (ADP-ribose) polymerase activates ATM which is required for subsequent homologous recombination repair
Nucleic Acids Res., March 23, 2006; 34(6): 1685 - 1691.
[Abstract] [Full Text] [PDF]

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 Nucleic Acids ResHome page
N. Levy, A. Martz, A. Bresson, C. Spenlehauer, G. de Murcia, and J. Menissier-de Murcia
XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage
Nucleic Acids Res., January 5, 2006; 34(1): 32 - 41.
[Abstract] [Full Text] [PDF]

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 Proc. Natl. Acad. Sci. USAHome page
Y. Pereg, D. Shkedy, P. de Graaf, E. Meulmeester, M. Edelson-Averbukh, M. Salek, S. Biton, A. F. A. S. Teunisse, W. D. Lehmann, A. G. Jochemsen, et al.
Phosphorylation of Hdmx mediates its Hdm2- and ATM-dependent degradation in response to DNA damage
PNAS, April 5, 2005; 102(14): 5056 - 5061.
[Abstract] [Full Text] [PDF]


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