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

Unlike 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.

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Publication Details

Journal
Current Biology
Published
2025-03-01
DOI
https://doi.org/10.1016/j.cub.2025.02.033
Citations
3
Primary Topic
Trypanosoma species research and implications
Type
article
Field-Weighted Citation Impact
4.06

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article

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

Corinne Blancard, David Moreira, Emmanuel Tétaud, Étienne Gontier et al.
3 citations
Current Biology
Trypanosoma species research and implications
4.06
article

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

Corinne Blancard, David Moreira, Emmanuel Tétaud, Étienne Gontier, Corinne Asencio, Manuel Rojo, Chloé Morel, Bénédicte Salin, Stéphane Duvezin‐Caubet, Frédéric Bringaud
article en
3 citations

Abstract

Unlike 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.

Current BiologyVol. 35(6)
Centre National de la Recherche Scientifique (FR), Université de Bordeaux (FR), Inserm (FR), AgroParisTech (FR), Université Paris-Saclay (FR), Ecologie, Société, Evolution (FR), Bordeaux Population Health (FR), Institut de Biochimie et Génétique Cellulaires (FR), Laboratoire de Microbiologie Fondamentale et Pathogénicité (FR)
University of Bern, Alliance Française contre les Maladies Parasitaires, Agence Nationale de la Recherche, Fondation pour la Recherche Médicale, Labex, Akademie Věd České Republiky, Centre National de la Recherche Scientifique, Université de Bordeaux, European Research Council, Biologické Centrum, Akademie Věd České Republiky, CHIST-ERA
Openalex Percentile: Top 7%
Trypanosoma species research and implications
4.06
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