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The small GTPase Rab11 co-localizes with α-synuclein in intracellular inclusions and modulates its aggregation, secretion and toxicity

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dc.contributor.authorChutna, Oldriska
dc.contributor.authorGoncalves, Susana
dc.contributor.authorVillar-Pique, Anna
dc.contributor.authorGuerreiro, Patrícia
dc.contributor.authorMarijanovic, Zrinka
dc.contributor.authorMendes, Tiago
dc.contributor.authorRamalho, José
dc.contributor.authorEmmanouilidou, Evangelia
dc.contributor.authorVentura, Salvador
dc.contributor.authorKlucken, Jochen
dc.contributor.authorBarral, Duarte C.
dc.contributor.authorGiorgini, Flaviano
dc.contributor.authorVekrellis, Kostas
dc.contributor.authorOuteiro, Tiago
dc.date.accessioned2022-03-21T17:49:20Z
dc.date.available2022-03-21T17:49:20Z
dc.date.issued2014
dc.description© The Author 2014. Published by Oxford University Press. All rights reserved.pt_PT
dc.description.abstractAlpha-synuclein (aSyn) misfolding and aggregation are pathological features common to several neurodegenerative diseases, including Parkinson's disease (PD). Mounting evidence suggests that aSyn can be secreted and transferred from cell to cell, participating in the propagation and spreading of pathological events. Rab11, a small GTPase, is an important regulator in both endocytic and secretory pathways. Here, we show that Rab11 is involved in regulating aSyn secretion. Rab11 knockdown or overexpression of either Rab11a wild-type (Rab11a WT) or Rab11a GDP-bound mutant (Rab11a S25N) increased secretion of aSyn. Furthermore, we demonstrate that Rab11 interacts with aSyn and is present in intracellular inclusions together with aSyn. Moreover, Rab11 reduces aSyn aggregation and toxicity. Our results suggest that Rab11 is involved in modulating the processes of aSyn secretion and aggregation, both of which are important mechanisms in the progression of aSyn pathology in PD and other synucleinopathies.pt_PT
dc.description.sponsorshipO.C. was supported by Fundação para a Ciência e Tecnologia, Portugal (SFRH/BD/44446/2008). T.F.O. was supported by an EMBO Installation Grant, a Marie Curie International Reintegration Grant (Neurofold), and is currently supported by the DFG Center for Nanoscale Microscopy and Molecular Physiology of the Brain. F.G. and T.F.O. have been supported by research funding from Parkinson's UK (G-1203).pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationHum Mol Genet. 2014 Dec 20;23(25):6732-6745pt_PT
dc.identifier.doi10.1093/hmg/ddu391pt_PT
dc.identifier.eissn1460-2083
dc.identifier.issn0964-6906
dc.identifier.urihttp://hdl.handle.net/10451/51869
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherOxford University Presspt_PT
dc.relation.publisherversionhttps://academic.oup.com/hmgpt_PT
dc.subjectBodily secretionspt_PT
dc.subjectGuanosine triphosphate phosphohydrolasespt_PT
dc.subjectTransfection toxic effectpt_PT
dc.titleThe small GTPase Rab11 co-localizes with α-synuclein in intracellular inclusions and modulates its aggregation, secretion and toxicitypt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardNumberSFRH/BD/44446/2008
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBD%2F44446%2F2008/PT
oaire.citation.endPage6745pt_PT
oaire.citation.issue25pt_PT
oaire.citation.startPage6732pt_PT
oaire.citation.titleHuman Molecular Geneticspt_PT
oaire.citation.volume23pt_PT
oaire.fundingStreamSFRH
person.familyNameGuerreiro
person.familyNameMendes
person.familyNameOuteiro
person.givenNamePatrícia
person.givenNameTiago
person.givenNameTiago
person.identifier1489171
person.identifier.ciencia-idBC14-20AB-8D68
person.identifier.orcid0000-0002-0948-043X
person.identifier.orcid0000-0002-6194-7295
person.identifier.orcid0000-0003-1679-1727
person.identifier.scopus-author-id55200776400
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsrestrictedAccesspt_PT
rcaap.typearticlept_PT
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relation.isAuthorOfPublication8d484933-f4ef-4678-92f5-6ccc3cffe6fd
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