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TitleCoassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion.
Journal, issue, pagesJ Cell Biol, Vol. 186, Issue 6, Page 793-803, Year 2009
Publish dateSep 21, 2009
AuthorsRachel M DeVay / Lenin Dominguez-Ramirez / Laura L Lackner / Suzanne Hoppins / Henning Stahlberg / Jodi Nunnari /
PubMed AbstractTwo 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. ...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.
External linksJ Cell Biol / PubMed:19752025 / PubMed Central
MethodsEM (electron crystallography)
Resolution24.0 Å
Structure data

EMDB-5644:
Two-dimensional crystals of sMgm1 over a monolayer with a lipid composition identical to that of the mitochondrial inner membrane
Method: EM (electron crystallography) / Resolution: 24.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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