ArticleThe Journal of biological chemistry2009
Phospholipid association is essential for dynamin-related protein Mgm1 to function in mitochondrial membrane fusion.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed, 76 citations in OpenAlex.
- Article
- Loss and recovery of myocardial mitochondria in mice under different tail suspension time: Apoptosis and mitochondrial fission, fusion and autophagy.Experimental physiology · 2023Article
- The role of the mitochondrial outer membrane protein SLC25A46 in mitochondrial fission and fusion.Life science alliance · 2023Article
- Impact of Selected Small-Molecule Kinase Inhibitors on Lipid Membranes.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Article
- Mitoprotective Effects of a Synergistic Nutraceutical Combination: Basis for a Prevention Strategy Against Alzheimer's Disease.Frontiers in aging neuroscience · 2021Article
- Dominant Optic Atrophy (DOA): Modeling the Kaleidoscopic Roles of OPA1 in Mitochondrial Homeostasis.Frontiers in neurology · 2021Review
- Cardiolipin, the Mitochondrial Signature Lipid: Implication in Cancer.International journal of molecular sciences · 2020Review
- Phospholipid ebb and flow makes mitochondria go.The Journal of cell biology · 2020Review
- Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Effects of Regulatory Lipids on Intracellular Membrane Fusion Mediated by Dynamin-Like GTPases.Frontiers in cell and developmental biology · 2020Review
- Proteolytic regulation of mitochondrial dynamics.Mitochondrion · 2019Review
- A Molecular Perspective on Mitochondrial Membrane Fusion: From the Key Players to Oligomerization and Tethering of Mitofusin.The Journal of membrane biology · 2019Review
- The Metabolomic Signature of Opa1 Deficiency in Rat Primary Cortical Neurons Shows Aspartate/Glutamate Depletion and Phospholipids Remodeling.Scientific reports · 2019Article
- Mitochondrial Membrane Dynamics-Functional Positioning of OPA1.Antioxidants (Basel, Switzerland) · 2018Article
- Mitochondrial dynamics: overview of molecular mechanisms.Essays in biochemistry · 2018Review
- Mitochondrial dynamics: The dynamin superfamily and execution by collusion.Seminars in cell & developmental biology · 2018Review
- Phosphatidic Acid and Cardiolipin Coordinate Mitochondrial Dynamics.Trends in cell biology · 2018Review
- Recent insights into the structure and function of Mitofusins in mitochondrial fusion.F1000Research · 2018Review
- Specific degradation of phosphatidylglycerol is necessary for proper mitochondrial morphology and function.Biochimica et biophysica acta · 2016Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mgm1, the yeast ortholog of mammalian OPA1, is a key component in mitochondrial membrane fusion and is required for maintaining mitochondrial dynamics and morphology. We showed recently that the purified short isoform of Mgm1 (s-Mgm1) possesses GTPase activity, self-assembles into low order oligomers, and interacts specifically with negatively charged phospholipids (Meglei, G., and McQuibban, G. A. (2009) Biochemistry 48, 1774-1784). Here, we demonstrate that s-Mgm1 binds to a mixture of phospholipids characteristic of the mitochondrial inner membrane. Binding to physiologically representative lipids results in approximately 50-fold stimulation of s-Mgm1 GTPase activity. s-Mgm1 point mutants that are defective in oligomerization and lipid binding do not exhibit such stimulation and do not function in vivo. Electron microscopy and lipid turbidity assays demonstrate that s-Mgm1 promotes liposome interaction. Furthermore, s-Mgm1 assembles onto liposomes as oligomeric rings with 3-fold symmetry. The projection map of negatively stained s-Mgm1 shows six monomers, consistent with two stacked trimers. Taken together, our data identify a lipid-binding domain in Mgm1, and the structural analysis suggests a model of how Mgm1 promotes the fusion of opposing mitochondrial inner membranes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.