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• W2003265295 startingPage "1774" @default.
• W2003265295 abstract "Mitochondrial dynamics resulting from competing membrane fusion and fission reactions are required for normal cellular function in eukaryotes. Mgm1p, a dynamin-related protein, is a key component in yeast mitochondrial fusion and is evolutionarily conserved. Previous studies suggest that Mgm1p mediates mitochondrial inner membrane fusion in a manner similar to that of other dynamin proteins that use GTP hydrolysis and oligomerization to induce structural changes in lipid bilayers; however, a direct demonstration of these activities has yet to be presented. Here we show that purified Mgm1p forms low-order oligomers that are dependent on protein concentration, suggesting a dynamic and reversible interaction. We further demonstrate that Mgm1p has GTPase activity and kinetic properties consistent with a mechanoenzyme and with a role in inner membrane mitochondrial fusion. Mutations of key residues in conserved motifs of the GTPase domain show markedly reduced or diminished GTPase activity. A mutation in the GTPase effector domain, involved in assembly and assembly-stimulated GTP hydrolysis, has basal GTPase activity similar to that of wild-type Mgm1p but has a weaker propensity to form oligomers. Finally, our data indicate that Mgm1p interacts specifically with negatively charged phospholipids found in mitochondrial membranes, and point mutations in the predicted lipid-binding domain abrogate these interactions. These findings suggest the presence of a putative lipid-binding domain, providing insight into how this protein mediates inner membrane fusion. Together, these data indicate that Mgm1p mediates fusion through oligomerization, GTP hydrolysis, and lipid binding in a manner similar to those of other dynamin mechanoenzymes." @default.
• W2003265295 created "2016-06-24" @default.
• W2003265295 creator A5016601719 @default.
• W2003265295 creator A5022408568 @default.
• W2003265295 date "2009-02-10" @default.
• W2003265295 modified "2023-09-26" @default.
• W2003265295 title "The Dynamin-Related Protein Mgm1p Assembles into Oligomers and Hydrolyzes GTP To Function in Mitochondrial Membrane Fusion" @default.
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• W2003265295 doi "https://doi.org/10.1021/bi801723d" @default.
• W2003265295 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19236101" @default.
• W2003265295 hasPublicationYear "2009" @default.
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