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A new member of the dynamin superfamily modulates mitochondrial membrane branching in Trypanosoma brucei.

dc.rights.licenseopenen_US
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorMOREL, Chloé Alexandra
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorASENCIO, Corinne
dc.contributor.authorMOREIRA, David
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorBLANCARD, Corinne
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorSALIN, Bénédicte
hal.structure.identifierBordeaux Imaging Center [BIC]
dc.contributor.authorGONTIER, Etienne
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorDUVEZIN-CAUBET, Stéphane
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorROJO, Manuel
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorBRINGAUD, Frédéric
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorTETAUD, Emmanuel
IDREF: 25436697X
dc.date.accessioned2025-03-18T14:15:32Z
dc.date.available2025-03-18T14:15:32Z
dc.date.issued2025-03-06
dc.identifier.issn1879-0445en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/205531
dc.description.abstractEnUnlike most other eukaryotes, where mitochondria continuously fuse and divide, the mitochondrion of trypanosome cells forms a single and continuously interconnected network that divides only during cytokinesis. However, the machinery governing mitochondrial remodeling and interconnection of trypanosome mitochondrion remain largely unknown. We functionally characterize a new member of the dynamin superfamily protein (DSP) from T. brucei (TbMfnL), which shares similarity with a family of homologs present in various eukaryotic and prokaryotic phyla but not in opisthokonts like mammals and budding yeast. The sequence and domain organization of TbMfnL is distinct, and it is phylogenetically very distant from the yeast and mammalian dynamin-related proteins involved in mitochondrial fusion/fission dynamics, such as optic atrophy 1 (Opa1) and mitofusin (Mfn). TbMfnL localizes to the inner mitochondrial membrane facing the matrix and, upon overexpression, induces a strong increase in the interconnection and branching of mitochondrial filaments in a GTPase-dependent manner. TbMfnL is a component of a novel membrane remodeling machinery with an unprecedented matrix-side localization that is able to modulate the degree of inter-mitochondrial connections.
dc.language.isoENen_US
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.title.enA new member of the dynamin superfamily modulates mitochondrial membrane branching in Trypanosoma brucei.
dc.title.alternativeCurr Biolen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.cub.2025.02.033en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed40081380en_US
bordeaux.journalCurrent Biologyen_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-04995799
hal.version1
hal.date.transferred2025-03-18T14:15:35Z
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exporttrue
workflow.import.sourcepubmed
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Current%20Biology&rft.date=2025-03-06&rft.eissn=1879-0445&rft.issn=1879-0445&rft.au=MOREL,%20Chlo%C3%A9%20Alexandra&ASENCIO,%20Corinne&MOREIRA,%20David&BLANCARD,%20Corinne&SALIN,%20B%C3%A9n%C3%A9dicte&rft.genre=article


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