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dc.contributor.authorMoubarak, Rana S.
dc.contributor.authorPlanells Ferrer, Laura
dc.contributor.authorUrresti, Jorge
dc.contributor.authorReix, Stéphanie
dc.contributor.authorSegura Ginard, Miguel Francisco
dc.contributor.authorCarriba, Paulina
dc.contributor.authorMarqués Fernàndez, Fernando
dc.contributor.authorSolé Serra, Carme
dc.contributor.authorLlecha Cano, Núria
dc.contributor.authorLópez Soriano, Joaquin
dc.contributor.authorSanchis, Daniel
dc.contributor.authorYuste Mateos, Víctor J. (Víctor José)
dc.contributor.authorComella i Carnicé, Joan Xavier
dc.date.accessioned2016-11-14T10:38:32Z
dc.date.issued2013
dc.identifier.issn0270-6474
dc.identifier.urihttp://hdl.handle.net/10459.1/58487
dc.description.abstractThe neuronal long isoform of Fas Apoptotic Inhibitory Molecule (FAIM-L) protects from death receptor (DR)-induced apoptosis, yet its mechanism of protection remains unknown. Here, we show that FAIM-L protects rat neuronal Type II cells from Fas-induced apoptosis. XIAP has previously emerged as a molecular discriminator that is upregulated in Type II and downregulated in Type I apoptotic signaling. We demonstrate that FAIM-L requires sustained endogenous levels of XIAP to protect Type II cells as well as murine cortical neurons from Fas-induced apoptosis. FAIM-L interacts with the BIR2 domain of XIAP through an IAP-binding motif, the mutation of which impairs the antiapoptotic function of FAIM-L. Finally, we report that FAIM-L inhibits XIAP auto-ubiquitinylation and maintains its stability, thus conferring protection from apoptosis. Our results bring new understanding of the regulation of endogenous XIAP by a DR antagonist, pointing out at FAIM-L as a promising therapeutic tool for protection from apoptosis in pathological situations where XIAP levels are decreased.ca_ES
dc.description.sponsorshipThis work was funded by the Spanish Government Ministerio de Sanidad y Consumo (Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas, CB06/05/1104 to J.X.C.), Ministerio de Economía y Competitividad (SAF2010–19953 to J.X.C.; SAF2012–31485 to V.J.Y.), Instituto de Salud Carlos III (CP11/00052 to M.F.S.), and the Generalitat de Catalunya (Suport als Grups de Recerca Consolidats 2009SGR346). F.M.-F. and L.P.-F. are supported by postgraduate fellowships from the Spanish Government Ministerio de Educación y Ciencia. J.U. is supported by a postgraduate fellowship from the Generalitat de Catalunya. R.S.M. and V.J.Y. were under the Juan de la Cierva and the Ramon y Cajal programs, respectively, from the Ministerio de Educación y Ciencia (Spain), cofinanced by the European Social Fund. M.F.S. is under the Miguel Servet program from the Instituto de Salud Carlos III and cofinanced by the European Regional Development Fund.ca_ES
dc.language.isoengca_ES
dc.publisherSociety for Neuroscienceca_ES
dc.relationMICINN/PN2008-2011/SAF2010-19953
dc.relationMICINN/PN2008-2011/SAF2012-31485
dc.relation.isformatofReproducció del document publicat a https://doi.org/10.1523/JNEUROSCI.2479-13.2013ca_ES
dc.relation.ispartofThe Journal of Neuroscience, 2013, vol. 33, núm. 49, p 19262-19275ca_ES
dc.rightscc-by (c) Moubarak et al., 2013ca_ES
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/es/
dc.titleFAIM-L Is an IAP-Binding Protein That Inhibits XIAP Ubiquitinylation and Protects from Fas-Induced Apoptosisca_ES
dc.typearticleca_ES
dc.identifier.idgrec021615
dc.type.versionpublishedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_ES
dc.identifier.doihttps://doi.org/10.1523/JNEUROSCI.2479-13.2013


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