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The ubiquitin E3/E4 ligase, UBE4A, fine-tunes protein ubiquitylation and accumulation at sites of DNA damage facilitating double-strand break repair
dc.creator | Soria Bretones, Isabel | es |
dc.creator | Baranes Bachar, Keren | es |
dc.creator | Huertas Sánchez, Pablo | es |
dc.creator | Levy Barda, Adva | es |
dc.creator | Oehler, Judith | es |
dc.date.accessioned | 2019-03-20T11:21:21Z | |
dc.date.available | 2019-03-20T11:21:21Z | |
dc.date.issued | 2018 | |
dc.identifier.citation | Soria Bretones, I., Baranes Bachar, K., Huertas Sánchez, P., Levy Barda, A. y Oehler, J. (2018). The ubiquitin E3/E4 ligase, UBE4A, fine-tunes protein ubiquitylation and accumulation at sites of DNA damage facilitating double-strand break repair. Molecular Cell, 69 (5), 866-878. | |
dc.identifier.issn | 1097-4164 | es |
dc.identifier.uri | https://hdl.handle.net/11441/84468 | |
dc.description.abstract | Double-strand breaks (DSBs) are critical DNA lesions that robustly activate the elaborate DNA damage response (DDR) network. We identified a critical player in DDR fine-tuning - the E3/E4 ubiquitin ligase, UBE4A. UBE4A’s recruitment to sites of DNA damage is dependent on primary E3 ligases in the DDR and promotes enhancement and sustainment of K48- and K63-linked ubiquitin chains at these sites. This step is required for timely recruitment of the RAP80 and BRCA1 proteins and proper organization of RAP80- and BRCA1-associated protein complexes at DSB sites. This pathway is essential for optimal end-resection at DSBs, and its abrogation leads to up-regulation of the highly mutagenic alternative end-joining repair at the expense of error-free homologous recombination repair. Our data uncover a critical regulatory level in the DSB response and underscore the importance of fine-tuning of the complex DDR network for accurate and balanced execution of DSB repair | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Elsevier | es |
dc.relation.ispartof | Molecular Cell, 69 (5), 866-878. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | genome stability | es |
dc.subject | DNA damage | es |
dc.subject | double-strand breaks | es |
dc.subject | ubiquitin | es |
dc.subject | UBE4A | es |
dc.title | The ubiquitin E3/E4 ligase, UBE4A, fine-tunes protein ubiquitylation and accumulation at sites of DNA damage facilitating 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/acceptedVersion | 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/10.1016/j.molcel.2018.02.002 | es |
dc.identifier.doi | 10.1016/j.molcel.2018.02.002 | es |
idus.format.extent | 11 p. | es |
dc.journaltitle | Molecular Cell | es |
dc.publication.volumen | 69 | es |
dc.publication.issue | 5 | es |
dc.publication.initialPage | 866 | es |
dc.publication.endPage | 878 | es |
Ficheros | Tamaño | Formato | Ver | Descripción |
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pubnihms-983807.pdf | 1.323Mb | [PDF] | Ver/ | |