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PMID: 15574327 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A pathway of double-strand break rejoining dependent upon ATM, Artemis, and proteins locating to gamma-H2AX foci.

Molecular cell ·Vol. 16 ·No. 5 ·2004-12-03 ·Pages 715-24

Riballo E, Kühne M, Rief N, Doherty A, Smith GC, Recio MJ, Reis C, Dahm K, Fricke A, Krempler A, Parker AR, Jackson SP, Gennery A, Jeggo PA, Löbrich M

Abstract

The hereditary disorder ataxia telangiectasia (A-T) is associated with striking cellular radiosensitivity that cannot be attributed to the characterized cell cycle checkpoint defects. By epistasis analysis, we show that ataxia telangiectasia mutated protein (ATM) and Artemis, the protein defective in patients with RS-SCID, function in a common double-strand break (DSB) repair pathway that also requires H2AX, 53BP1, Nbs1, Mre11, and DNA-PK. We show that radiation-induced Artemis hyperphosphorylation is ATM dependent. The DSB repair process requires Artemis nuclease activity and rejoins approximately 10% of radiation-induced DSBs. Our findings are consistent with a model in which ATM is required for Artemis-dependent processing of double-stranded ends with damaged termini. We demonstrate that Artemis is a downstream component of the ATM signaling pathway required uniquely for the DSB repair function but dispensable for ATM-dependent cell cycle checkpoint arrest. The significant radiosensitivity of Artemis-deficient cells demonstrates the importance of this component of DSB repair to survival.

MeSH Terms
Animals Ataxia Telangiectasia Mutated Proteins Cell Cycle Proteins/metabolism Cell Line Cells, Cultured DNA Damage DNA Repair DNA Repair Enzymes DNA, Complementary/metabolism DNA-Binding Proteins/metabolism Dose-Response Relationship, Radiation Endonucleases Epistasis, Genetic Gamma Rays Genetic Complementation Test Histones/metabolism Humans Infrared Rays Intracellular Signaling Peptides and Proteins/metabolism MRE11 Homologue Protein Mice Nuclear Proteins/metabolism,physiology Phenotype Phosphoproteins/metabolism Phosphorylation Protein Serine-Threonine Kinases/metabolism Severe Combined Immunodeficiency Signal Transduction Time Factors Tumor Suppressor Proteins Tumor Suppressor p53-Binding Protein 1 X-Rays
Chemicals
Cell Cycle Proteins DNA, Complementary DNA-Binding Proteins Histones Ifi202b protein, mouse Intracellular Signaling Peptides and Proteins MRE11 protein, human Mre11a protein, mouse NBN protein, human Nuclear Proteins Phosphoproteins TP53BP1 protein, human Tumor Suppressor Proteins Tumor Suppressor p53-Binding Protein 1 gamma-H2AX protein, mouse ATM protein, human Ataxia Telangiectasia Mutated Proteins Atm protein, mouse Protein Serine-Threonine Kinases DCLRE1C protein, human Endonucleases MRE11 Homologue Protein Dclre1c protein, mouse DNA Repair Enzymes
Authors & Affiliations
15 authors, click to expand affiliations / ORCID
Riballo Enriqueta
Genome Damage and Stability Centre, University of Sussex, East Sussex, BN1 9RQ, United Kingdom.
Kühne Martin
Rief Nicole
Doherty Aidan
Smith Graeme C M
Recio María-José
Reis Caroline
Dahm Kirsten
Fricke Andreas
Krempler Andrea
Parker Antony R
Jackson Stephen P
Gennery Andrew
Jeggo Penny A
Löbrich Markus
Article Info
Journal
Molecular cell
Abbr.
Mol Cell
ISSN
1097-2765
Published
2004-12-03
Pages
715-24
Language
English
Region
United States
NLM ID
9802571
Subset
IM
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