Recent insights into the structure and function of Mitofusins in mitochondrial fusion

Mickaël Cohen 1, * David Tareste 2, 3, *
* Corresponding author
2 Trafic Membranaire et Morphogenèse Neuronale & Epithéliale
IJM (UMR_7592) - Institut Jacques Monod, UPD7 - Université Paris Diderot - Paris 7, INSERM - Institut National de la Santé et de la Recherche Médicale : U950
Abstract : Mitochondria undergo frequent fusion and fission events to adapt their morphology to cellular needs. Homotypic docking and fusion of outer mitochondrial membranes are controlled by Mitofusins, a set of large membrane-anchored GTPase proteins belonging to the dynamin superfamily. Mitofusins include, in addition to their GTPase and transmembrane domains, two heptad repeat domains, HR1 and HR2. All four regions are crucial for Mitofusin function, but their precise contribution to mitochondrial docking and fusion events has remained elusive until very recently. In this commentary, we first give an overview of the established strategies employed by various protein machineries distinct from Mitofusins to mediate membrane fusion. We then present recent structure-function data on Mitofusins that provide important novel insights into their mode of action in mitochondrial fusion.
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Mickaël Cohen, David Tareste. Recent insights into the structure and function of Mitofusins in mitochondrial fusion. F1000Research, Faculty of 1000, 2018, 7, pp.1983. ⟨10.12688/f1000research.16629.1⟩. ⟨inserm-02290020⟩

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