Interaction between ATM protein and c-Abl in response to DNA damage

Timothy Shafman, Kum Kum Khanna, Padmini Kedar, Kevin Spring, Sergei Kozlov, Tim Yen, Karen Hobson, Magtouf Gatei, Ning Zhang, Dianne Watters, Mark Egerton, Yosef Shiloh, Surender Kharbanda, Donald Kufe and Martin F. Laving
Additional contact information
Timothy Shafman: Dana-Farber Cancer Institutes
Kum Kum Khanna: University of Queensland, Royal Brisbane Hospital
Padmini Kedar: University of Queensland, Royal Brisbane Hospital
Kevin Spring: University of Queensland, Royal Brisbane Hospital
Sergei Kozlov: University of Queensland, Royal Brisbane Hospital
Tim Yen: Fox Chase Cancer Center
Karen Hobson: University of Queensland, Royal Brisbane Hospital
Magtouf Gatei: University of Queensland, Royal Brisbane Hospital
Ning Zhang: University of Queensland, Royal Brisbane Hospital
Dianne Watters: University of Queensland, Royal Brisbane Hospital
Mark Egerton: University of Queensland, Royal Brisbane Hospital
Yosef Shiloh: Tel Aviv University
Surender Kharbanda: Dana-Farber Cancer Institutes
Donald Kufe: Dana-Farber Cancer Institutes
Martin F. Laving: University of Queensland, Royal Brisbane Hospital

Nature, 1997, vol. 387, issue 6632, 520-523

Abstract: Abstract The gene mutated in the autosomal recessive disorder ataxia telangiectasia (AT), designated ATM (for 'AT mutated'), is a member of a family of phosphatidylinositol-3-kinase-like enzymes that are involved in cell-cycle control, meiotic recombination, telomere length monitoring and DNA-damage response1–4. Previous results have demonstrated that AT cells are hypersensitive to ionizing radiation5–7 and are defective at the Gl/S checkpoint after radiation damage8–10. Because cells lacking the protein tyrosine kinase c-Abl are also defective in radiation-induced Gl arrest11, we investigated the possibility that ATM might interact with c-Abl in response to radiation damage. Here we show that ATM binds c-Abl constitutively in control cells but not in AT cells. Our results demonstrate that the SH3 domain of c-Abl interacts with a DPAPNPPHFP motif (residues 1,373–1,382) of ATM. The results also reveal that radiation-induction of c-Abl tyrosine kinase activity is diminished in AT cells. These findings indicate that ATM is involved in the activation of c-Abl by DNA damage and this interaction may in part mediate radiation-induced Gl arrest.

Date: 1997
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DOI: 10.1038/387520a0

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