Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1

Mitochondrial outer- and inner-membrane fusion events are coupled in vivo but separable and mechanistically distinct in vitro, indicating that separate fusion machines exist in each membrane. Outer-membrane fusion requires trans interactions of the dynamin-related GTPase Fzo1, GTP hydrolysis, and an intact inner-membrane proton gradient. Innermembrane fusion also requires GTP hydrolysis but distinctly requires an innermembrane electrical potential. The protein machinery responsible for innermembrane fusion is unknown. Here, we show that the conserved intermembrane-space dynamin-related GTPase Mgm1 is required to tether and fuse mitochondrial inner membranes. We observe an additional role of Mgm1 in innermembrane dynamics, specifically in the maintenance of crista structures. We present evidence that trans Mgm1 interactions on opposing inner membranes function similarly to tether and fuse innermembranes as well as maintain crista structures and propose a model for how the mitochondrial dynamins function to facilitate fusion.