Journal
FEBS LETTERS
Volume 583, Issue 13, Pages 2237-2243Publisher
WILEY
DOI: 10.1016/j.febslet.2009.05.053
Keywords
Mitochondria; Membrane fusion; Mitochondrial DNA; Mgm1; Genetic analysis; Dynamin-like GTPase
Funding
- University of Munich FFoLe program
- Deutsche Forschungsgemeinschaft [SFB 594]
- Center for Integrated Protein Science Munich
- Goethe University Frankfurt DFG [EXC 115]
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The mitochondrial dynamin-like GTPase Mgm1 exists as a long (l-Mgm1) and a short isoform (s-Mgm1). They both are essential for mitochondrial fusion. Here we show that the isoforms interact in a homotypic and heterotypic manner. Their submitochondrial distribution between inner boundary membrane and cristae was markedly different. Overexpression of l-Mgm1 exerts a dominant negative effect on mitochondrial fusion. A functional GTPase domain is required only in s-Mgm1 but not in l-Mgm1. We propose that l-Mgm1 acts primarily as an anchor in the inner membrane that in concert with the GTPase activity of s-Mgm1 mediates the fusion of inner membranes. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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