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.
Highlights
Mitochondria are delimited by an outer membrane and include an inner membrane that separates a matrix and an intermembrane space
The ubiquitin–proteasome system was recently shown to modulate mitochondrial fusion by coordinating an intricate balance between the turnover of Fuzzy Onion (Fzo)[1] and the desaturation of fatty acids[100]. These results suggest that the last steps of mitochondrial fusion might be regulated by specific lipids that modify the structure of bilayers so as to facilitate their interaction with key protein sequences and/or their transition to non-bilayer fusion intermediate structures
We are just beginning to understand the mode of action of Mitofusins in mitochondrial fusion
Summary
Faculty Reviews are review articles written by the prestigious Members of Faculty Opinions. The articles are commissioned and peer reviewed before publication to ensure that the final, published version is comprehensive and accessible. The reviewers who approved the final version are listed with their names and affiliations
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