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dc.contributor.authorBustillo Zabalbeitia, Itsasne
dc.contributor.authorMontessuit, Sylvie
dc.contributor.authorRaemy, Etienne
dc.contributor.authorBasáñez Asúa, Gorka
dc.contributor.authorTerrones Urio, Oihana ORCID
dc.contributor.authorMartinou, Jean-Claude
dc.date.accessioned2015-12-09T17:00:12Z
dc.date.available2015-12-09T17:00:12Z
dc.date.issued2014-07-18
dc.identifier.citationPLOS ONE 9 (7) : (2014) // Article ID e102738es
dc.identifier.issn1932-6203
dc.identifier.urihttp://hdl.handle.net/10810/16405
dc.description.abstractDynamin-Related Protein 1 (Drp1), a large GTPase of the dynamin superfamily, is required for mitochondrial fission in healthy and apoptotic cells. Drp1 activation is a complex process that involves translocation from the cytosol to the mitochondrial outer membrane (MOM) and assembly into rings/spirals at the MOM, leading to membrane constriction/division. Similar to dynamins, Drp1 contains GTPase (G), bundle signaling element (BSE) and stalk domains. However, instead of the lipid-interacting Pleckstrin Homology (PH) domain present in the dynamins, Drp1 contains the so-called B insert or variable domain that has been suggested to play an important role in Drp1 regulation. Different proteins have been implicated in Drp1 recruitment to the MOM, although how MOM-localized Drp1 acquires its fully functional status remains poorly understood. We found that Drp1 can interact with pure lipid bilayers enriched in the mitochondrion-specific phospholipid cardiolipin (CL). Building on our previous study, we now explore the specificity and functional consequences of this interaction. We show that a four lysine module located within the B insert of Drp1 interacts preferentially with CL over other anionic lipids. This interaction dramatically enhances Drp1 oligomerization and assembly-stimulated GTP hydrolysis. Our results add significantly to a growing body of evidence indicating that CL is an important regulator of many essential mitochondrial functions.es
dc.description.sponsorshipThis work was funded by the Swiss National Science Foundation (31993A-141068/1), IGE3 and the State of Geneva (J.-C.M.), the Spanish Ministerio de Ciencia e Innovacion grant BFU2011-28566 and the Basque Government grant IT838-13 (G.B., O.T.). O.T. was supported by a postdoctoral Juan de la Cierva fellow, Spanish Government, and by a FEBS Short-Term fellowship. I.B.-Z. was supported by a predoctoral fellowship from the Basque Government. 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.relationinfo:eu-repo/grantAgreement/MINECO/BFU2011-28566
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.subjectdominant optic atrophyes
dc.subjectmitochondrial fissiones
dc.subjectoxidative-phosphorylationes
dc.subjectconformational-changeses
dc.subjectmenbrane-bindinges
dc.subjectmammalian cellses
dc.subjectDRP1es
dc.subjectGTPasees
dc.subjectfusiones
dc.subjectdomaines
dc.titleSpecific Interaction with Cardiolipin Triggers Functional Activation of Dynamin-Related Protein 1es
dc.typeinfo:eu-repo/semantics/articlees
dc.rights.holder2014 Bustillo-Zabalbeitia 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 credited.es
dc.relation.publisherversionhttp://journals.plos.org/plosone/article?id=10.1371/journal.pone.0102738#abstract0es
dc.identifier.doi10.1371/journal.pone.0102738
dc.departamentoesBioquímica y biología moleculares_ES
dc.departamentoeuBiokimika eta biologia molekularraes_ES
dc.subject.categoriaAGRICULTURAL AND BIOLOGICAL SCIENCES
dc.subject.categoriaMEDICINE
dc.subject.categoriaBIOCHEMISTRY AND MOLECULAR BIOLOGY


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