Cohen Mickael M, Tareste David
Sorbonne Université, CNRS UMR8226, Institut de Biologie Physico-Chimique, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Paris, France.
Université Paris Descartes, Sorbonne Paris Cité, INSERM ERL U950, Trafic Membranaire dans le Cerveau Normal et Pathologique, Paris, France.
F1000Res. 2018 Dec 28;7. doi: 10.12688/f1000research.16629.1. eCollection 2018.
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.
线粒体频繁经历融合和裂变事件，以使其形态适应细胞需求。线粒体外膜的同型对接和融合由线粒体融合蛋白调控，线粒体融合蛋白是一组属于发动蛋白超家族的大型膜锚定GTP酶蛋白。线粒体融合蛋白除了其GTP酶和跨膜结构域外，还包括两个七肽重复结构域，即HR1和HR2。所有这四个区域对线粒体融合蛋白的功能都至关重要，但直到最近，它们对线粒体对接和融合事件的确切贡献仍不清楚。在这篇评论中，我们首先概述了不同于线粒体融合蛋白的各种蛋白质机制用于介导膜融合的既定策略。然后，我们展示了关于线粒体融合蛋白的最新结构-功能数据，这些数据为其在线粒体融合中的作用模式提供了重要的新见解。
