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All stressed out without ATM kinase

Publication Type : Journal Article

Publisher : Science Signaling

Source : Science Signaling, Volume 4, Number 167 (2011)

Url : http://www.scopus.com/inward/record.url?eid=2-s2.0-79953855430&partnerID=40&md5=94b0af72486a6d172ce9ec065248538a

Keywords : antioxidant, article, ataxia telangiectasia, ATM protein, cell cycle, cell cycle protein, Cell Cycle Proteins, chemical structure, chemistry, dimerization, DNA binding protein, DNA damage, DNA dependent protein kinase, DNA strand breakage, DNA-Activated Protein Kinase, DNA-Binding Proteins, DsbA protein, gene mutation, human, Humans, ionizing radiation, Mammalia, mammalian target of rapamycin, metabolism, Models, Molecular, nerve cell, Neurons, neuropathology, nonhuman, oxidation, oxidation reduction reaction, Oxidation-Reduction, oxidative stress, pathology, physiology, priority journal, protein serine threonine kinase, Protein-Serine-Threonine Kinases, reactive oxygen metabolite, Reactive Oxygen Species, redox effector factor 1, review, signal transduction, target of rapamycin kinase, TOR Serine-Threonine Kinases, tumor suppressor protein, Tumor Suppressor Proteins

Campus : Amritapuri

School : School of Biotechnology

Department : biotechnology

Year : 2011

Abstract : Ataxia-telangiectasia (A-T) is a rare, neurodegenerative, inherited disease arising from mutations in the kinase A-T mutated (ATM), which promotes cell cycle checkpoints and DNA double-strand break repair. Puzzlingly, these ATM activities fail to fully explain A-T neuropathologies, which instead have links to stress induced by reactive oxygen species (ROS). However, a landmark discovery reveals an unexpected intersection of ROS and kinase signaling: ATM can be directly activated by oxidation to form a disulfide-linked dimer in a mechanism distinct from DNA damage activation. When combined with notable structural-based insights into the ATM homolog DNA-PK (DNA-protein kinase) and mTOR (mammalian target of rapamycin), these results suggest conformation and assembly mechanisms to signal oxidative stress through an ATM nodal point. These findings fundamentally affect our understanding of ROS and ATM signaling and of the A-T phenotype, with implications for altering signaling in cancer cells to increase sensitivities to current therapeutic interventions. © 2011 American Association for the Advancement of Science. All Rights Reserved.

Cite this Research Publication : J. J. Pab Perry and Tainer, J. Aac, “All stressed out without ATM kinase”, Science Signaling, vol. 4, 2011.

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