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dc.contributor.authorRamírez Sánchez, Juan Manuel ORCID
dc.contributor.authorMartínez Zárate, Aitor
dc.contributor.authorLectez, Benoit
dc.contributor.authorLee, So Young
dc.contributor.authorFranco, Maribel
dc.contributor.authorBarrio Olano, María Rosa
dc.contributor.authorDittmar, Gunnar
dc.contributor.authorMayor Martínez, Ugo ORCID
dc.date.accessioned2016-05-11T10:15:51Z
dc.date.available2016-05-11T10:15:51Z
dc.date.issued2015-10-13
dc.identifier.citationPlos One 10(10) : (2015) // Article ID e0139083es
dc.identifier.issn1932-6203
dc.identifier.urihttp://hdl.handle.net/10810/18220
dc.description.abstractBackground Ubiquitination is known to regulate physiological neuronal functions as well as to be involved in a number of neuronal diseases. Several ubiquitin proteomic approaches have been developed during the last decade but, as they have been mostly applied to non-neuronal cell culture, very little is yet known about neuronal ubiquitination pathways in vivo. Methodology/Principal Findings Using an in vivo biotinylation strategy we have isolated and identified the ubiquitinated proteome in neurons both for the developing embryonic brain and for the adult eye of Drosophila melanogaster. Bioinformatic comparison of both datasets indicates a significant difference on the ubiquitin substrates, which logically correlates with the processes that are most active at each of the developmental stages. Detection within the isolated material of two ubiquitin E3 ligases, Parkin and Ube3a, indicates their ubiquitinating activity on the studied tissues. Further identification of the proteins that do accumulate upon interference with the proteasomal degradative pathway provides an indication of the proteins that are targeted for clearance in neurons. Last, we report the proof-of-principle validation of two lysine residues required for nSyb ubiquitination. Conclusions/Significance These data cast light on the differential and common ubiquitination pathways between the embryonic and adult neurons, and hence will contribute to the understanding of the mechanisms by which neuronal function is regulated. The in vivo biotinylation methodology described here complements other approaches for ubiquitome study and offers unique advantages, and is poised to provide further insight into disease mechanisms related to the ubiquitin proteasome system.es
dc.description.sponsorshipUM was supported by the Basque Government research grant (PI2011-24), the Asociacion Sindrome de Angelman, and the March of Dimes Basil O'Connor Award (5-FY12-16). JR was supported by the CIC bioGUNE PhD fellowship. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.es
dc.language.isoenges
dc.publisherPublic Library Sciencees
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.subjectangelman-syndromees
dc.subjectmass-spectrometryes
dc.subjectbiotinylated ubiquitines
dc.subjectprotein ubiquitinationes
dc.subjectneuromuscular-junctiones
dc.subjectsynapse developmentes
dc.subjectbinding entitieses
dc.subjectligasees
dc.subjectdegradationes
dc.subjecthomeostasises
dc.titleProteomic Analysis of the Ubiquitin Landscape in the Drosophila Embryonic Nervous System and the Adult Photoreceptor Cellses
dc.typeinfo:eu-repo/semantics/articlees
dc.rights.holder© 2015 Ramirez et al. This is an open access article distributed under the terms of the Creative Commons Attribution License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are creditedes
dc.relation.publisherversionhttp://journals.plos.org/plosone/article?id=10.1371/journal.pone.0139083#abstract0es
dc.identifier.doi10.1371/journal.pone.0139083
dc.departamentoesBioquímica y biología moleculares_ES
dc.departamentoeuBiokimika eta biologia molekularraes_ES
dc.subject.categoriaAGRICULTURAL AND BIOLOGICAL SCIENCES
dc.subject.categoriaBIOCHEMISTRY AND MOLECULAR BIOLOGY
dc.subject.categoriaMEDICINE


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