Log in or create a free account to read this content
Gain free access to this article, as well as selected content from this journal and more on nature.com
or
References
Bhatti, S. et al. Cell Mol. Life Sci. 68, 2977–3006 (2011).
Jackson, S. P. & Bartek, J. Nature 461, 1071–1078 (2009).
Lavin, M. F. Nat. Rev. Mol. Cell Biol. 9, 759–769 (2008).
McKinnon, P. J. Annu. Rev. Pathol. 7, 303–321 (2012).
Wang, X. et al. Nat. Commun. 7, 11655 (2016).
Adamowicz, M. J. Immunol. Sci. 2, 26–31 (2018).
Paull, T. T. Annu. Rev. Biochem 84, 711–738 (2015).
Brown, A. L. et al. Proc. Natl Acad. Sci. USA 96, 3745–3750 (1999).
Dupre, A., Boyer-Chatenet, L. & Gautier, J. Nat. Struct. Mol. Biol. 13, 451–457 (2006).
Baretic, D. et al. Sci. Adv. 3, e1700933 (2017).
Yang, H. et al. Nature 497, 217–223 (2013).
Rao, Q. et al. Cell Res. 28, 143–156 (2017).
Guo, Z., Kozlov, S., Lavin, M. F., Person, M. D. & Paull, T. T. Science 330, 517–521 (2010).
Acknowledgements
We thank Center for Biological Imaging (CBI) of Institute of Biophysics (IBP) of Chinese Academy of Sciences (CAS) and National Center for Protein Science Shanghai (NCPSS) for the support on cryo-EM data collection and data analyses. We thank staff members working in Biomedical Core Facility, Fudan University for their help on Mass Spectrometry analyses. This work was supported by grants from the Ministry of Science and Technology of China (2016YFA0500700), the National Natural Science Foundation of China (31830107, 31821002, 31425008), the National Program for support of Top-Notch Young Professionals (Y.X.), the Strategic Priority Research Program of the Chinese Academy of Sciences (grant no. XDB08000000), and the UK Wellcome Trust Investigator Award 206422/Z/17/Z (P.Z.). We acknowledge Diamond for access of the Cryo-EM facilities at the UK national electron bio-imaging centre (eBIC, proposal NT21004), funded by the Wellcome Trust, MRC and BBSRC.
Author information
Authors and Affiliations
Contributions
J.X., M.L., Y.Q., and Y.X. designed the experiments. J.X., C.G., and Y.Q. purified the proteins. M.L., Y.C., Y.Q., P.Z., J. X., Y.T., and Z.Y. prepared the cryo-EM sample, collected the data and determined the structures. M.L., J.L., J. X. built the structural model. J. X., B. P., and Y. X. performed biochemical analyses. J. X., and Y.X. analyzed the data and wrote the manuscript with support from all the authors. Y.X. supervised the project.
Corresponding author
Ethics declarations
Competing interests
The authors declare no competing interests.
Rights and permissions
About this article
Cite this article
Xiao, J., Liu, M., Qi, Y. et al. Structural insights into the activation of ATM kinase. Cell Res 29, 683–685 (2019). https://doi.org/10.1038/s41422-019-0205-0
Received:
Accepted:
Published:
Issue date:
DOI: https://doi.org/10.1038/s41422-019-0205-0
This article is cited by
-
Beyond the BRCA1/2 genes in ovarian cancer: the role of germline pathogenic variants in the ATM gene
Molecular Biology Reports (2025)
-
The synthetic lethality of targeting cell cycle checkpoints and PARPs in cancer treatment
Journal of Hematology & Oncology (2022)
-
Structures of Mec1/ATR kinase endogenously stimulated by different genotoxins
Cell Discovery (2022)
-
Cancer genome datamining and functional genetic analysis implicate mechanisms of ATM/ATR dysfunction underpinning carcinogenesis
Communications Biology (2021)
-
Molecular basis of human ATM kinase inhibition
Nature Structural & Molecular Biology (2021)
