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dc.contributor.authorVilar, Marçal 
dc.contributor.authorSung, Tsung-Chang
dc.contributor.authorChen, Zhijiang
dc.contributor.authorGarcia-Carpio, Irmina 
dc.contributor.authorFernandez, Eva M 
dc.contributor.authorXu, Jiqing
dc.contributor.authorRiek, Roland
dc.contributor.authorLee, Kuo-Fen
dc.date.accessioned2019-12-02T09:28:09Z
dc.date.available2019-12-02T09:28:09Z
dc.date.issued2014-08
dc.identifier.citationPLoS Biol. 2014 Aug 5;12(8):e1001918.es_ES
dc.identifier.issn1545-7885es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/8725
dc.description.abstractThe p75 neurotrophin receptor, a member of the tumor necrosis factor receptor superfamily, is required as a co-receptor for the Nogo receptor (NgR) to mediate the activity of myelin-associated inhibitors such as Nogo, MAG, and OMgp. p45/NRH2/PLAIDD is a p75 homologue and contains a death domain (DD). Here we report that p45 markedly interferes with the function of p75 as a co-receptor for NgR. P45 forms heterodimers with p75 and thereby blocks RhoA activation and inhibition of neurite outgrowth induced by myelin-associated inhibitors. p45 binds p75 through both its transmembrane (TM) domain and DD. To understand the underlying mechanisms, we have determined the three-dimensional NMR solution structure of the intracellular domain of p45 and characterized its interaction with p75. We have identified the residues involved in such interaction by NMR and co-immunoprecipitation. The DD of p45 binds the DD of p75 by electrostatic interactions. In addition, previous reports suggested that Cys257 in the p75 TM domain is required for signaling. We found that the interaction of the cysteine 58 of p45 with the cysteine 257 of p75 within the TM domain is necessary for p45-p75 heterodimerization. These results suggest a mechanism involving both the TM domain and the DD of p45 to regulate p75-mediated signaling.es_ES
dc.description.sponsorshipThis research was supported by grants from the National Institute of Health HD034534, NS060833, NS072031, AG010435, CA014195, AG042985 (KFL), Muscular Dystrophy Association (KFL), the Clayton Medical Research Foundation, Inc. (KFL), and the Spanish Ministry of Economy and Competitiveness (BFU2010-15276) to MV. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.es_ES
dc.language.isoenges_ES
dc.publisherPublic Library of Science (PLOS) es_ES
dc.type.hasVersionVoRes_ES
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subject.meshAmino Acid Sequence es_ES
dc.subject.meshAnimals es_ES
dc.subject.meshCysteine es_ES
dc.subject.meshHEK293 Cells es_ES
dc.subject.meshHumans es_ES
dc.subject.meshMagnetic Resonance Spectroscopy es_ES
dc.subject.meshMice es_ES
dc.subject.meshModels, Biological es_ES
dc.subject.meshModels, Molecular es_ES
dc.subject.meshMolecular Sequence Data es_ES
dc.subject.meshProtein Binding es_ES
dc.subject.meshProtein Interaction Mapping es_ES
dc.subject.meshProtein Stability es_ES
dc.subject.meshReceptor, Nerve Growth Factor es_ES
dc.subject.meshReceptors, Cell Surface es_ES
dc.subject.meshReceptors, Nerve Growth Factor es_ES
dc.subject.meshSciatic Nerve es_ES
dc.subject.meshSolutions es_ES
dc.subject.meshStructure-Activity Relationship es_ES
dc.subject.meshUp-Regulation es_ES
dc.subject.meshProtein Multimerization es_ES
dc.subject.meshSignal Transduction es_ES
dc.titleHeterodimerization of p45-p75 modulates p75 signaling: structural basis and mechanism of actiones_ES
dc.typejournal articlees_ES
dc.rights.licenseAtribución 4.0 Internacional*
dc.identifier.pubmedID25093680es_ES
dc.format.volume12es_ES
dc.format.number8es_ES
dc.format.pagee1001918es_ES
dc.identifier.doi10.1371/journal.pbio.1001918es_ES
dc.contributor.funderInstituto de Salud Carlos III 
dc.contributor.funderMinisterio de Economía y Competitividad (España) 
dc.description.peerreviewedes_ES
dc.identifier.e-issn1545-7885es_ES
dc.relation.publisherversionhttps://doi.org/10.1371/journal.pbio.1001918es_ES
dc.identifier.journalPLoS biologyes_ES
dc.repisalud.centroISCIII::Unidad Funcional de Investigación de Enfermedades Crónicas (UFIEC)::Unidad de Neurodegeneraciónes_ES
dc.repisalud.institucionISCIIIes_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/HD034534es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/NS060833es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/NS072031es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/AG010435es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/CA014195es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/AG042985es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/BFU2010-15276es_ES
dc.rights.accessRightsopen accesses_ES


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