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dc.contributor.author | Fernandez-Capetillo, Oscar | |
dc.contributor.author | Chen, Hua-Tang | |
dc.contributor.author | Celeste, Arkady | |
dc.contributor.author | Ward, Irene | |
dc.contributor.author | Romanienko, Peter J | |
dc.contributor.author | Morales, Julio C | |
dc.contributor.author | Naka, Kazuhito | |
dc.contributor.author | Xia, Zhenfang | |
dc.contributor.author | Camerini-Otero, R Daniel | |
dc.contributor.author | Motoyama, Noboru | |
dc.contributor.author | Carpenter, Phillip B | |
dc.contributor.author | Bonner, William M | |
dc.contributor.author | Chen, Junjie | |
dc.contributor.author | Nussenzweig, André | |
dc.date.accessioned | 2024-02-09T14:41:51Z | |
dc.date.available | 2024-02-09T14:41:51Z | |
dc.date.issued | 2002-12 | |
dc.identifier.citation | Nat Cell Biol . 2002;4(12):993-7. | es_ES |
dc.identifier.issn | 1465-7392 | es_ES |
dc.identifier.uri | http://hdl.handle.net/20.500.12105/17703 | |
dc.description.abstract | Activation of the ataxia telangiectasia mutated (ATM) kinase triggers diverse cellular responses to ionizing radiation (IR), including the initiation of cell cycle checkpoints. Histone H2AX, p53 binding-protein 1 (53BP1) and Chk2 are targets of ATM-mediated phosphorylation, but little is known about their roles in signalling the presence of DNA damage. Here, we show that mice lacking either H2AX or 53BP1, but not Chk2, manifest a G2-M checkpoint defect close to that observed in ATM(-/-) cells after exposure to low, but not high, doses of IR. Moreover, H2AX regulates the ability of 53BP1 to efficiently accumulate into IR-induced foci. We propose that at threshold levels of DNA damage, H2AX-mediated concentration of 53BP1 at double-strand breaks is essential for the amplification of signals that might otherwise be insufficient to prevent entry of damaged cells into mitosis. | es_ES |
dc.description.sponsorship | These studies were in part motivated by discussions with T. Halazonetis, who suggested examining the effects of low-dose IR, and we thank T. Halazonetis for sharing unpublished results. We also thank M. Lichten, J. Chung, A. Lee, S. Petersen and A. Singer for critical comments on the manuscript, and M. Kruhlack for assistance with microscopy. P.B.C was supported by a grant from The Robert Welch Foundation. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Nature Publishing Group | es_ES |
dc.type.hasVersion | VoR | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject.mesh | Intracellular Signaling Peptides and Proteins | es_ES |
dc.subject.mesh | Phosphoproteins | es_ES |
dc.subject.mesh | Protein Serine-Threonine Kinases | es_ES |
dc.subject.mesh | Animals | es_ES |
dc.subject.mesh | Carrier Proteins | es_ES |
dc.subject.mesh | Cell Line | es_ES |
dc.subject.mesh | Checkpoint Kinase 2 | es_ES |
dc.subject.mesh | Chromosomal Proteins, Non-Histone | es_ES |
dc.subject.mesh | DNA Damage | es_ES |
dc.subject.mesh | DNA-Binding Proteins | es_ES |
dc.subject.mesh | G2 Phase | es_ES |
dc.subject.mesh | Gene Expression Regulation | es_ES |
dc.subject.mesh | Histones | es_ES |
dc.subject.mesh | Mice | es_ES |
dc.subject.mesh | Mitosis | es_ES |
dc.subject.mesh | Phosphorylation | es_ES |
dc.subject.mesh | Protein Kinases | es_ES |
dc.subject.mesh | Tumor Suppressor p53-Binding Protein 1 | es_ES |
dc.title | DNA damage-induced G2-M checkpoint activation by histone H2AX and 53BP1. | es_ES |
dc.type | journal article | es_ES |
dc.rights.license | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.identifier.pubmedID | 12447390 | es_ES |
dc.format.volume | 4 | es_ES |
dc.format.number | 12 | es_ES |
dc.format.page | 993 | es_ES |
dc.identifier.doi | 10.1038/ncb884 | es_ES |
dc.description.peerreviewed | Sí | es_ES |
dc.relation.publisherversion | https://doi.org/10.1038/ncb884 | es_ES |
dc.identifier.journal | Nature cell biology | es_ES |
dc.repisalud.institucion | CNIO | es_ES |
dc.repisalud.orgCNIO | CNIO::Grupos de investigación::Grupo de Inestabilidad Genómica | es_ES |
dc.rights.accessRights | open access | es_ES |
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