ArticleMolecular biology of the cell2003
Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.
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Who cites it
123 citing papers in PubMed.
- Cristae: bridging bioenergetic hubs and compartmental barriers in mitochondrial homeostasis.Cell death & disease · 2026Review
- Structural and Metabolic Remodeling of Skeletal Muscle in Heart Failure with Reduced Ejection Fraction: A Review: Beyond the Failing Heart.International journal of molecular sciences · 2026Review
- A special latch in yeast mitofusin guarantees mitochondrial fusion by stabilizing self-assembly.Nature communications · 2025Article
- Molecular machineries shaping the mitochondrial inner membrane.Nature reviews. Molecular cell biology · 2025Review
- Deficits in mitochondrial dynamics and iron balance result in templated insertions.Nature communications · 2025Article
- Bringing together but staying apart: decisive differences in animal and fungal mitochondrial inner membrane fusion.Biological reviews of the Cambridge Philosophical Society · 2025Review
- A quantitative ultrastructural timeline of nuclear autophagy reveals a role for dynamin-like protein 1 at the nuclear envelope.Nature cell biology · 2025Article
- De NovoInternational journal of molecular sciences · 2025Review
- OPA1 and disease-causing mutants perturb mitochondrial nucleoid distribution.Cell death & disease · 2024Article
- A quantitative ultrastructural timeline of nuclear autophagy reveals a role for dynamin-like protein 1 at the nuclear envelope.bioRxiv : the preprint server for biology · 2024Article
- Chemical inhibition of phosphatidylcholine biogenesis reveals its role in mitochondrial division.iScience · 2024Article
- Cristae formation is a mechanical buckling event controlled by the inner mitochondrial membrane lipidome.The EMBO journal · 2023Article
- Biased placement of Mitochondria fission facilitates asymmetric inheritance of protein aggregates during yeast cell division.PLoS computational biology · 2023Article
- Mitophagy in yeast: known unknowns and unknown unknowns.The Biochemical journal · 2023Review
- OPA1, a molecular regulator of dilated cardiomyopathy.Journal of cellular and molecular medicine · 2023Review
- Cristae formation is a mechanical buckling event controlled by the inner membrane lipidome.bioRxiv : the preprint server for biology · 2023Article
- Mitochondrial networks through the lens of mathematics.Physical biology · 2023Review
- Drug Drop Test: How to Quickly Identify Potential Therapeutic Compounds for Mitochondrial Diseases Using YeastInternational journal of molecular sciences · 2023Review
- The mitochondrial intermembrane space protein mitofissin drives mitochondrial fission required for mitophagy.Molecular cell · 2023Article
- Mitochondria as central hubs in synaptic modulation.Cellular and molecular life sciences : CMLS · 2023Review
63 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
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Abstract
In Saccharomyces cerevisiae, mitochondrial fusion requires at least two outer membrane proteins, Fzo1p and Ugo1p. We provide direct evidence that the dynamin-related Mgm1 protein is also required for mitochondrial fusion. Like fzo1 and ugo1 mutants, cells disrupted for the MGM1 gene contain numerous mitochondrial fragments instead of the few long, tubular organelles seen in wild-type cells. Fragmentation of mitochondria in mgm1 mutants is rescued by disrupting DNM1, a gene required for mitochondrial division. In zygotes formed by mating mgm1 mutants, mitochondria do not fuse and mix their contents. Introducing mutations in the GTPase domain of Mgm1p completely block mitochondrial fusion. Furthermore, we show that mgm1 mutants fail to fuse both their mitochondrial outer and inner membranes. Electron microscopy demonstrates that although mgm1 mutants display aberrant mitochondrial inner membrane cristae, mgm1 dnm1 double mutants restore normal inner membrane structures. However, mgm1 dnm1 mutants remain defective in mitochondrial fusion, indicating that mitochondrial fusion requires Mgm1p regardless of the morphology of mitochondria. Finally, we find that Mgm1p, Fzo1p, and Ugo1p physically interact in the mitochondrial outer membrane. Our results raise the possibility that Mgm1p regulates fusion of the mitochondrial outer membrane through its interactions with Fzo1p and Ugo1p.
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