ArticleNature structural & molecular biology2018
Structure of a mitochondrial fission dynamin in the closed conformation.
Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 23 citations in OpenAlex.
- Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Dynamin-like Proteins Combine Mechano-constriction and Membrane Remodeling to Enable Two-Step Mitochondrial Fission via a "Snap-through" Instability.Journal of the American Chemical Society · 2025Article
- Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025Review
- Structural basis for regulated assembly of the mitochondrial fission GTPase Drp1.Nature communications · 2024Article
- A Novel Group of Dynamin-Related Proteins Shared by Eukaryotes and Giant Viruses Is Able to Remodel Mitochondria From Within the Matrix.Molecular biology and evolution · 2023Article
- SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features.Nature communications · 2023Article
- Measuring Membrane Penetration Depths and Conformational Changes in Membrane Peptides and Proteins.The Journal of membrane biology · 2022Review
- The Unicellular Red Alga Cyanidioschyzon merolae-The Simplest Model of a Photosynthetic Eukaryote.Plant & cell physiology · 2021Review
- Review
- Molecular Basis of Mitochondrial and Peroxisomal Division Machineries.International journal of molecular sciences · 2020Review
- The cell biology of mitochondrial membrane dynamics.Nature reviews. Molecular cell biology · 2020Review
- The structural biology of the dynamin-related proteins: New insights into a diverse, multitalented family.Traffic (Copenhagen, Denmark) · 2019Review
- Open and cut: allosteric motion and membrane fission by dynamin superfamily proteins.Molecular biology of the cell · 2019Review
- Sirt1 inhibits HG-induced endothelial injury: Role of Mff-based mitochondrial fission and F‑actin homeostasis-mediated cellular migration.International journal of molecular medicine · 2019Article
- Structural Insights into the Mechanism of Dynamin Superfamily Proteins.Trends in cell biology · 2019Review
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Onsite GTP fuelling via DYNAMO1 drives division of mitochondria and peroxisomes.Nature communications · 2018Article
- Bacterial dynamin-like proteins reveal mechanism for membrane fusion.Nature communications · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Dynamin 1-like proteins (DNM1-L) are mechanochemical GTPases that induce membrane fission in mitochondria and peroxisomes. Their mechanism depends on conformational changes driven by nucleotide and lipid cycling. Here we show the crystal structure of a mitochondrial fission dynamin (CmDnm1) from the algae Cyanidioschyzon merolae. Unlike other eukaryotic dynamin structures, CmDnm1 is in a hinge 1 closed conformation, with the GTPase domain compacted against the stalk. Within the crystal, CmDnm1 packs as a diamond-shaped tetramer that is consistent with an inactive off-membrane state. Crosslinking, photoinduced electron transfer assays, and electron microscopy verify these structures. In vitro, CmDnm1 forms concentration-dependent rings and protein-lipid tubes reminiscent of DNM1-L and classical dynamin with hinge 1 open. Our data provides a mechanism for filament collapse and membrane release that may extend to other dynamin family members. Additionally, hinge 1 closing may represent a key conformational change that contributes to membrane fission.
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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.