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dc.contributor.authorElu Arantzamendi, Nagore ORCID
dc.contributor.authorOsinalde Moraleja, Nerea ORCID
dc.contributor.authorBeaskoetxea Lejarzegi, Javier
dc.contributor.authorRamírez Sánchez, Juan Manuel ORCID
dc.contributor.authorLectez, Benoît
dc.contributor.authorAloria Escolastico, Kerman
dc.contributor.authorRodríguez Pérez, José Antonio ORCID
dc.contributor.authorArizmendi Bastarrika, Jesús María ORCID
dc.contributor.authorMayor Martínez, Ugo ORCID
dc.date.accessioned2024-06-12T16:20:08Z
dc.date.available2024-06-12T16:20:08Z
dc.date.issued2019-05-03
dc.identifier.citationFrontiers in Physiology 10 : (2019) // Article ID 534es_ES
dc.identifier.issn1664-042X
dc.identifier.urihttp://hdl.handle.net/10810/68414
dc.description.abstractThe ubiquitin E3 ligase UBE3A has been widely reported to interact with the proteasome, but it is still unclear how this enzyme regulates by ubiquitination the different proteasomal subunits. The proteasome receptor DDI1 has been identified both in Drosophila photoreceptor neurons and in human neuroblastoma cells in culture as a direct substrate of UBE3A. Here, we further characterize this regulation, by identifying the UBE3A-dependent ubiquitination sites and ubiquitin chains formed on DDI1. Additionally, we found one deubiquitinating enzyme that is capable of reversing the action of UBE3A on DDI1. The complete characterization of the ubiquitination pathway of an UBE3A substrate is important due to the role of this E3 ligase in rare neurological disorders as Angelman syndrome.es_ES
dc.description.sponsorshipThis work was supported by March of Dimes (Research Grant 1-FY15-339); Spanish MINECO (grant SAF2016-76898-P) cofinanced with FEDER funds, and grant PRB3 (IPT17/0019 - ISCIII-SGEFI / ERDF). UM is also part of COST action Proteostasis. This work was also partially supported by Fondation Jérôme Lejeune grant 1381-MU2015A.es_ES
dc.language.isoenges_ES
dc.publisherFrontierses_ES
dc.relationinfo:eu-repo/grantAgreement/MINECO/SAF2016-76898-Pes_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.titleDetailed dissection of UBE3A-mediated DDI1 ubiquitination.es_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.rights.holder© 2019 The authors. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY).es_ES
dc.relation.publisherversionhttps://www.frontiersin.org/journals/physiology/articles/10.3389/fphys.2019.00534es_ES
dc.identifier.doi10.3389/fphys.2019.00534
dc.departamentoesGenética, antropología física y fisiología animales_ES
dc.departamentoeuGenetika,antropologia fisikoa eta animalien fisiologiaes_ES


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© 2019 The authors. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY).
Except where otherwise noted, this item's license is described as © 2019 The authors. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY).