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Activation and regulation of ATM kinase activity in response to DNA double-strand breaks
Abstract
The ataxia-telangiectasia-mutated (ATM) protein kinase is rapidly and specifically activated in response to DNA double-strand breaks in eukaryotic cells. In this review, we summarize recent insights into the mechanism of ATM activation, focusing on the role of the Mre11/Rad50/Nbs1 (MRN) complex in this process. We also compare observations of the ATM activation process in different biological systems and highlight potential candidates for cellular factors that may participate in regulating ATM activity in human cells.
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“The Mre11/Rad50/Nbs1 (MRN) complex recognizes the resulting DSBs and facilitates ATM recruitment and activation [20–23].”
From ATR- and ATM-Mediated DNA Damage Response Is Dependent on Excision Repair Assembly during G1 but Not in S Phase of Cell Cycle (2016) · cites this paper as [20]
In the citing paper
“DSB recruits MRN complex, which subsequently facilitates ATM recruitment, H2AX phosphorylation, and DNA repair by HR pathway [20;21;40].”
From ATR- and ATM-Mediated DNA Damage Response Is Dependent on Excision Repair Assembly during G1 but Not in S Phase of Cell Cycle (2016) · cites this paper as [20]
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Cites
DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation
Bakkenist, C. J., & Kastan, M. B. (2003) · Nature · doi:10.1038/nature01368 · Cited by 3,466
A Single Ataxia Telangiectasia Gene with a Product Similar to PI-3 Kinase
Savitsky, K., Bar-Shira, A., Gilad, S., Rotman, G., Ziv, Y., Vanagaite, L., Tagle, D. A., Smith, S., Uziel, T., Sfez, S., et al. (1995) · Science · doi:10.1126/science.7792600 · Cited by 2,785
ATM Activation by DNA Double-Strand Breaks Through the Mre11-Rad50-Nbs1 Complex
Lee, J.-H., & Paull, T. T. (2005) · Science · doi:10.1126/science.1108297 · Cited by 1,424
Self-citationConserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage
Falck, J., Coates, J., & Jackson, S. P. (2005) · Nature · doi:10.1038/nature03442 · Cited by 1,304
Carney, J. P., Maser, R. S., Olivares, H., Davis, E. M., Le Beau, M., Yates, J. R., Hays, L., Morgan, W. F., & Petrini, J. H. J. (1998) · Cell · doi:10.1016/s0092-8674(00)81175-7 · Cited by 1,226
Nibrin, a Novel DNA Double-Strand Break Repair Protein, Is Mutated in Nijmegen Breakage Syndrome
Varon, R., Vissinga, C., Platzer, M., Cerosaletti, K. M., Chrzanowska, K. H., Saar, K., Beckmann, G., Seemanová, E., Cooper, P. R., Nowak, N. J., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81174-5 · Cited by 1,079
Requirement of the MRN complex for ATM activation by DNA damage
Uziel, T., Lerenthal, Y., Moyal, L., Andegeko, Y., Mittelman, L., & Shiloh, Y. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg541 · Cited by 1,075
Stewart, G. S., Maser, R. S., Stankovic, T., Bressan, D. A., Kaplan, M. I., Jaspers, N. G. J., Raams, A., Byrd, P. J., Petrini, J. H. J., & Taylor, A. M. R. (1999) · Cell · doi:10.1016/s0092-8674(00)81547-0 · Cited by 1,060
Cortez, D., Wang, Y., Qin, J., & Elledge, S. J. (1999) · Science · doi:10.1126/science.286.5442.1162 · Cited by 1,020
Botuyan, M. V., Lee, J., Ward, I. M., Kim, J., Thompson, J. R., Chen, J., & Mer, G. (2006) · Cell · doi:10.1016/j.cell.2006.10.043 · Cited by 1,011
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Luo, Y., Lou, S., Deng, X., Liu, Z., Li, Y., Kleiboeker, S. B., & Qiu, J. (2011) · Journal of Virology · doi:10.1128/jvi.00831-11 · Cited by 75
Du, L., Kayalı, R., Bertoni, C., Fike, F. M., Hu, H., Iversen, P. L., & Gatti, R. A. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr217 · Cited by 74
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Yoo, H. Y., Kumagai, A., Shevchenko, A., Shevchenko, A., & Dunphy, W. G. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1190 · Cited by 76
Hladik, D., Höfig, I., Oestreicher, U., Beckers, J., Matjanovski, M., Bao, X., Scherthan, H., Atkinson, M. J., & Rosemann, M. (2019) · Stem Cell Research & Therapy · doi:10.1186/s13287-019-1334-6 · Cited by 72
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Hogg, M., Sauer-Eriksson, A. E., & Johansson, E. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr1102 · Cited by 71
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Cannon, B. L., Kuhnlein, J., Yang, S.-H., Cheng, A., Schindler, D., Stark, J. M., Russell, R., & Paull, T. T. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1309816110 · Cited by 76
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Fell, V. L., & Schild‐Poulter, C. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05661-11 · Cited by 67
Balasubramanian, N., Bai, P., Buchek, G., Korza, G., & Weller, S. K. (2010) · Journal of Virology · doi:10.1128/jvi.01506-10 · Cited by 71
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Stracker, T. H., Couto, S. S., Cordon‐Cardo, C., Matos, T., & Petrini, J. H. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.028 · Cited by 64
Chiang, S., Carroll, J., & El‐Khamisy, S. F. (2010) · Cell Cycle · doi:10.4161/cc.9.3.10598 · Cited by 65
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Tavecchio, M., Munck, J. M., Cano, C., Newell, D. R., & Curtin, N. J. (2011) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-011-1662-4 · Cited by 63
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Wei, F., Yan, J. J., & Tang, D. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711798194388 · Cited by 63
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Zhang, T., Cronshaw, J. M., Kanu, N., Snijders, A. P., & Behrens, A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1400230111 · Cited by 61
Zhang, X., Qin, X., Wei, R., Song, H., Mi, J., Lin, Z., Yang, Y., Sun, Z., & Zou, K. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.04.009 · Cited by 61
Oh, K.-S., Bustin, M., Mazur, S. J., Appella, E., & Kraemer, K. H. (2011) · DNA Repair · doi:10.1016/j.dnarep.2010.09.004 · Cited by 60
Hong, Z., Liu, T., Wan, L., Fa, P., Kumar, P., Cao, Y., Prasad, C. B., Qiu, Z., Liu, J., Wang, H., et al. (2022) · Cancer Research · doi:10.1158/0008-5472.can-21-2229 · Cited by 60
Lu, C.-S., Truong, L. N., Aslanian, A., Shi, L. Z., Li, Y., Hwang, P. Y.-H., Koh, K. H., Hunter, T. R., Yates, J. R., Berns, M. W., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.421545 · Cited by 63
Osipov, A. N., Pustovalova, M. V., Grekhova, A., Eremin, P. S., Vorobyova, N. Y., Pulin, A. A., Zhavoronkov, A. A., Roumiantsev, S. A., Klokov, D. Y., & Eremin, I. I. (2015) · Oncotarget · doi:10.18632/oncotarget.4739 · Cited by 60
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Xiong, J., Todorova, D., Su, N., Kim, J., Lee, P.-J., Shen, Z., Briggs, S. P., & Xu, Y. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201408106 · Cited by 56
Zhang, Q., Zhao, B., Yan, J., Song, S., Min, R., & Fan, C. (2011) · Analytical Chemistry · doi:10.1021/ac2023684 · Cited by 55
El-Sherbeeny, N. A., Soliman, N., Youssef, A. M., El‐Fadeal, N. M. A., El-Abaseri, T. B., Hashish, A. A., Abdelbasset, W. K., Batiha, G. E., & Zaitone, S. A. (2020) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2020.111344 · Cited by 53
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Lee, H.-J., Lan, L., Peng, G., Chang, W., Hsu, M., Wang, Y., Cheng, C. C., Wei, L., Nakajima, S., Chang, S.-S., et al. (2015) · Cell Research · doi:10.1038/cr.2015.8 · Cited by 57
Lee, A. Y., Chiba, T., Truong, L. N., Cheng, A. N., Do, J. P. H., Cho, M. J., Chen, L., & Wu, X. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.291104 · Cited by 55
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Zheng, L., Kanagaraj, R., Mihaljević, B., Schwendener, S., Sartori, A. A., Gerrits, B., Shevelev, I., & Janščák, P. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp147 · Cited by 53
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Nickoloff, J. A., Haro, L. P. D., Wray, J. W., & Hromas, R. (2008) · Current Opinion in Hematology · doi:10.1097/moh.0b013e328302f711 · Cited by 50
Gadducci, A., & Guerrieri, M. E. (2017) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2017.04.006 · Cited by 51
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Lavin, M. F., & Yeo, A. J. (2020) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2020.111695 · Cited by 51
Stergiou, L., Eberhard, R., Doukoumetzidis, K., & Hengartner, M. O. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.158 · Cited by 48
Paull, T. T., & Deshpande, R. A. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.07.007 · Cited by 54
Self-citationCole, J. B., Waurich, B., Wensch-Dorendorf, M., Bickhart, D. M., & Swalve, H. H. (2014) · Journal of Dairy Science · doi:10.3168/jds.2013-7409 · Cited by 48
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Rattay, T., & Talbot, C. J. (2014) · Clinical Oncology · doi:10.1016/j.clon.2014.02.001 · Cited by 48
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Karen, K. A., Hoey, P. J., Young, C. S. H., & Hearing, P. (2009) · Journal of Virology · doi:10.1128/jvi.00042-09 · Cited by 49
Anderson, C. W., & Appella, E. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00264-3 · Cited by 49
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Garner, E., & Costanzo, V. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.04.015 · Cited by 47
Cho, E.-A., Kim, E., Kwak, S.-J., & Juhnn, Y. (2014) · Molecular Cancer · doi:10.1186/1476-4598-13-36 · Cited by 47
Chandrakesan, P., May, R. J., Weygant, N., Qu, D., Berry, W. L., Sureban, S. M., Ali, N., Rao, C. V., Huycke, M. M., Bronze, M. S., et al. (2016) · Scientific Reports · doi:10.1038/srep37667 · Cited by 47
Simon, A., Kourié, H. R., & Kerger, J. N. (2017) · 癌症:英文版 · doi:10.1186/s40880-017-0179-6 · Cited by 46
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Lee, J. (2024) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2024.102808 · Cited by 50
Self-citationHe, J. N., Shi, L. Z., Truong, L. N., Lu, C.-S., Razavian, N. B., Li, Y., Negrete, A., Shiloach, J., Berns, M. W., & Wu, X. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.384750 · Cited by 47
Alessio, N., Pipino, C., Mandatori, D., Tomo, P. D., Ferone, A., Marchiso, M., Melone, M. A. B., Peluso, G., Pandolfi, A., & Galderisi, U. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26845 · Cited by 45
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Ray, A., Blevins, C., Wani, G., & Wani, A. A. (2016) · PLOS ONE · doi:10.1371/journal.pone.0159344 · Cited by 44
Solhaug, A., Holme, J. A., Haglund, K., Dendelé, B., Sergent, O., Pestka, J. J., Lagadic‐Gossmann, D., & Eriksen, G. S. (2013) · Toxicology Letters · doi:10.1016/j.toxlet.2013.02.012 · Cited by 44
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Luo, Y., & Qiu, J. (2013) · Future Virology · doi:10.2217/fvl.13.5 · Cited by 46
Jin, W., Zhou, L., Yan, B., Li, Y., Liu, F., Tong, P., Yu, W., Dong, X., Xie, L., Zhang, J., et al. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13742 · Cited by 44
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Liang, L., Fan, Y., Cheng, J., Cheng, D., Zhao, Y., Cao, B., Ma, L., An, L., Jia, W., Xu, S., et al. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.09.003 · Cited by 44
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Chesnokova, V., Zonis, S., Barrett, R. J., Kameda, H., Wawrowsky, K., Ben-Shlomo, A., Yamamoto, M., Gleeson, J. P., Bresee, C. J., Gorbunova, V. A., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.125762 · Cited by 43
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Long, X.-D. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.77925 · Cited by 45
Albino, A. P., Jorgensen, E. D., Rainey, P., Gillman, I. G., Clark, T. J., Gietl, D., Zhao, H. L., Traganos, F., & Darżynkiewicz, Z. (2009) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2009.06.009 · Cited by 43
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Mason, P. A., & Cox, L. S. (2011) · AGE · doi:10.1007/s11357-011-9306-5 · Cited by 46
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Sobeck, A., Stone, S., Landais, I., de Graaf, B., & Hoatlin, M. E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.007690 · Cited by 42
Upadhyay, N., Tilekar, K. N., Loiodice, F., Anisimova, N. Y., Spirina, T. S., Sokolova, D. V., Smirnova, G. B., Choe, J., Meyer‐Almes, F., Pokrovsky, V. S., et al. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104527 · Cited by 42
Spatiotemporal Dynamics of Early DNA Damage Response Proteins on Complex DNA Lesions
Tobias, F., Löb, D., Lengert, N., Durante, M., Drossel, B., Taucher-Scholz, G., & Jakob, B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057953 · Cited by 42
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Nguyen, T. N., Saleem, R. S. Z., Luderer, M. J., Hovde, S., Henry, R. W., & Tepe, J. J. (2011) · ACS Chemical Biology · doi:10.1021/cb200320c · Cited by 41
Boonstra, V., Arends, N. J. T., Stijnen, T., Blum, W. F., Akkerman, O. W., & Hokken-Koelega, A. (2005) · Hormone Research in Paediatrics · doi:10.1159/000090376 · Cited by 41
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Zhang, T., Penicud, K., Bruhn, C., Loizou, J. I., Kanu, N., Wang, Z., & Behrens, A. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.11.002 · Cited by 40
Chailleux, C., Tyteca, S., Papin, C., Boudsocq, F., Puget, N., Courilleau, C., Grigoriev, M., Canitrot, Y., & Trouche, D. (2010) · Biochemical Journal · doi:10.1042/bj20091329 · Cited by 42
Nayak, D., Kumar, A., Chakraborty, S., Rasool, R. U., Amin, H., Katoch, A., Gopinath, V., Mahajan, V., Zilla, M. K., Rah, B., et al. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.70 · Cited by 40
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Michalková, R., Kello, M., Kudlicková, Z., Gazdova, M., Mirossay, L., Mojžišová, G., & Mojžíš, J. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14030503 · Cited by 38
Domenico, E. G. D., Romano, E., Porto, P. D., & Ascenzioni, F. (2014) · BioMed Research International · doi:10.1155/2014/787404 · Cited by 39
Komura, K., Inamoto, T., Tsujino, T., Matsui, Y., Konuma, T., Nishimura, K., Uchimoto, T., Tsutsumi, T., Matsunaga, T., Maenosono, R., et al. (2021) · Oncogene · doi:10.1038/s41388-021-02021-y · Cited by 38
Metadata
- Authors
- Lee, J.-H., & Paull, T. T.
- Affiliations
- The University of Texas at Austin (US)
- Corresponding author
- Paull, T T
- ORCID
- Paull, T T
- Venue
- Oncogene
- Published
- 2007-12-10
- Volume
- 26
- Issue
- 56
- Pages
- 7741-7748
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W2087239831
- Cited by
- 545
- References
- 88
- Citations by year
- 2026: 7 · 2025: 16 · 2024: 24 · 2023: 11 · 2022: 27 · 2021: 35 · 2020: 29 · 2019: 23 · 2018: 23 · 2017: 41 · 2016: 22 · 2015: 30 · 2014: 38 · 2013: 50 · 2012: 34
- FWCI
- 2.46
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Oncogene (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Effects of Radiation Exposure
- Keywords
- ATM kinase, DNA double-strand breaks, kinase activation, MRN complex, MRE11, RAD50, NBS1, DNA damage response, DNA repair
- MeSH terms
- MRE11 Homologue Protein, Animals, Ataxia Telangiectasia, DNA Repair, DNA-Binding Proteins, Humans, Nuclear Proteins, Phosphorylation, Protein Serine-Threonine Kinases, Acid Anhydride Hydrolases, Cell Cycle Proteins, Tumor Suppressor Proteins, DNA Repair Enzymes, DNA Breaks, Double-Stranded, Ataxia Telangiectasia Mutated Proteins
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