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Nuclear poly(A)-binding protein 1 is an ATM target and essential for DNA double-strand break repair
dc.creator | Prados Carvajal, Rosario | es |
dc.creator | Huertas Sánchez, Pablo | es |
dc.creator | Gavish Izakson, Michal | es |
dc.creator | Bhavana Velpula, Bhagya | es |
dc.creator | Elkon, Ran | es |
dc.date.accessioned | 2018-05-16T12:05:39Z | |
dc.date.available | 2018-05-16T12:05:39Z | |
dc.date.issued | 2018 | |
dc.identifier.citation | Prados Carvajal, R., Huertas Sánchez, P., Gavish Izakson, M., Bhavana Velpula, . y Elkon, R. (2018). Nuclear poly(A)-binding protein 1 is an ATM target and essential for DNA double-strand break repair. Nucleic Acids Research, 46 (2), 730-747. | |
dc.identifier.issn | 1362-4962 | es |
dc.identifier.uri | https://hdl.handle.net/11441/74699 | |
dc.description.abstract | The DNA damage response (DDR) is an extensive signaling network that is robustly mobilized by DNA double-strand breaks (DSBs). The primary transducer of the DSB response is the protein kinase, ataxia-telangiectasia, mutated (ATM). Here, we establish nuclear poly(A)-binding protein 1 (PABPN1) as a novel target of ATM and a crucial player in the DSB response. PABPN1 usually functions in regulation of RNA processing and stability. We establish that PABPN1 is recruited to the DDR as a critical regulator of DSB repair. A portion of PABPN1 relocalizes to DSB sites and is phosphorylated on Ser95 in an ATM-dependent manner. PABPN1 depletion sensitizes cells to DSB-inducing agents and prolongs the DSB-induced G2/M cell-cycle arrest, and DSB repair is hampered by PABPN1 depletion or elimination of its phosphorylation site. PABPN1 is required for optimal DSB repair via both nonhomologous end-joining (NHEJ) and homologous recombination repair (HRR), and specifically is essential for efficient DNA-end resection, an initial, key step in HRR. Using mass spectrometry analysis, we capture DNA damage-induced interactions of phospho-PABPN1, including well-established DDR players as well as other RNA metabolizing proteins. Our results uncover a novel ATM-dependent axis in the rapidly growing interface between RNA metabolism and the DDR. | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Oxford University Press | es |
dc.relation.ispartof | Nucleic Acids Research, 46 (2), 730-747. | |
dc.rights | Atribución-NoComercial-SinDerivadas 3.0 Estados Unidos de América | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | Nuclear poly(A)-binding protein 1 is an ATM target and essential for DNA double-strand break repair | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Genética | es |
dc.relation.publisherversion | http://dx.doi.org/10.1093/nar/gkx1240 | es |
dc.identifier.doi | 10.1093/nar/gkx1240 | es |
idus.format.extent | 17 p. | es |
dc.journaltitle | Nucleic Acids Research | es |
dc.publication.volumen | 46 | es |
dc.publication.issue | 2 | es |
dc.publication.initialPage | 730 | es |
dc.publication.endPage | 747 | es |
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