Journal
JOURNAL OF CELL BIOLOGY
Volume 186, Issue 6, Pages 793-803Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200906098
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Funding
- National Institutes of Health (NIH) [R01GM062942, U54GM074929, 1F32GM078749]
- Howard Hughes Medical Institute [SHHMI01 GSRRD]
- American Heart Preodoctoral Award [0715023Y]
- Pew Latin American Fellow Program [MCA4934SC]
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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.
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