Regulation of mitochondrial inner membrane fusion: divergent evolution with similar solutions?

2015 ◽  
Vol 62 (2) ◽  
pp. 291-294 ◽  
Author(s):  
Johannes Wagener
2009 ◽  
Vol 186 (6) ◽  
pp. 793-803 ◽  
Author(s):  
Rachel M. DeVay ◽  
Lenin Dominguez-Ramirez ◽  
Laura L. Lackner ◽  
Suzanne Hoppins ◽  
Henning Stahlberg ◽  
...  

Two dynamin-related protein (DRP) families are essential for fusion of the outer and inner mitochondrial membranes, Fzo1 (yeast)/Mfn1/Mfn2 (mammals) and Mgm1 (yeast)/Opa1 (mammals), respectively. Fzo1/Mfns possess two medial transmembrane domains, which place their critical GTPase and coiled-coil domains in the cytosol. In contrast, Mgm1/Opa1 are present in cells as long (l) isoforms that are anchored via the N terminus to the inner membrane, and short (s) isoforms were predicted to be soluble in the intermembrane space. We addressed the roles of Mgm1 isoforms and how DRPs function in membrane fusion. Our analysis indicates that in the absence of a membrane, l- and s-Mgm1 both exist as inactive GTPase monomers, but that together in trans they form a functional dimer in a cardiolipin-dependent manner that is the building block for higher-order assemblies.


PLoS ONE ◽  
2012 ◽  
Vol 7 (11) ◽  
pp. e49639 ◽  
Author(s):  
Cécile Sauvanet ◽  
Stéphane Duvezin-Caubet ◽  
Bénédicte Salin ◽  
Claudine David ◽  
Aurélie Massoni-Laporte ◽  
...  

2018 ◽  
Vol 1859 (9) ◽  
pp. 951-957 ◽  
Author(s):  
Tadato Ban ◽  
Hiroto Kohno ◽  
Takaya Ishihara ◽  
Naotada Ishihara

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Danyang Zhang ◽  
Yan Zhang ◽  
Jun Ma ◽  
Chunmei Zhu ◽  
Tongxin Niu ◽  
...  

Mammalian mitochondrial inner membrane fusion is mediated by optic atrophy 1 (OPA1). Under physiological conditions, OPA1 undergoes proteolytic processing to form a membrane-anchored long isoform (L-OPA1) and a soluble short isoform (S-OPA1). A combination of L-OPA1 and S-OPA1 is essential for efficient membrane fusion; however, the relevant mechanism is not well understood. In this study, we investigate the cryo-electron microscopic structures of S-OPA1–coated liposomes in nucleotide-free and GTPγS-bound states. S-OPA1 exhibits a general dynamin-like structure and can assemble onto membranes in a helical array with a dimer building block. We reveal that hydrophobic residues in its extended membrane-binding domain are critical for its tubulation activity. The binding of GTPγS triggers a conformational change and results in a rearrangement of the helical lattice and tube expansion similar to that of S-Mgm1. These observations indicate that S-OPA1 adopts a dynamin-like power stroke membrane remodeling mechanism during mitochondrial inner membrane fusion.


Cell ◽  
2006 ◽  
Vol 127 (2) ◽  
pp. 383-395 ◽  
Author(s):  
Shelly Meeusen ◽  
Rachel DeVay ◽  
Jennifer Block ◽  
Ann Cassidy-Stone ◽  
Sarah Wayson ◽  
...  

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