ArticleNature communications2021
CryoEM structure of the super-constricted two-start dynamin 1 filament.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Membrane Constriction by Dynamin through GTP-Driven Conformational Changes from Coarse-Grained Molecular Dynamics Simulations.The journal of physical chemistry letters · 2025Article
- Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- The Structure of the Drp1 Lattice on Membrane.Journal of molecular biology · 2025Article
- Expanding the phenotypic spectrum of DNM1-related disorders: novel GTPase domain variants and their diverse neurological outcomes.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2025Article
- Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies.Nature structural & molecular biology · 2025Article
- Nanoscale dynamics of Dynamin 1 helices reveals squeeze-twist deformation mode critical for membrane fission.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cryo-EM structures of membrane-bound dynamin in a post-hydrolysis state primed for membrane fission.Developmental cell · 2024Article
- Mesoscopic elasticity controls dynamin-driven fission of lipid tubules.Scientific reports · 2024Article
- Brominated lipid probes expose structural asymmetries in constricted membranes.Nature structural & molecular biology · 2023Article
- Cryo-electron tomography reveals structural insights into the membrane remodeling mode of dynamin-like EHD filaments.Nature communications · 2022Article
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Authors and funding
5 authors.
Funding
Abstract
Dynamin belongs to the large GTPase superfamily, and mediates the fission of vesicles during endocytosis. Dynamin molecules are recruited to the neck of budding vesicles to assemble into a helical collar and to constrict the underlying membrane. Two helical forms were observed: the one-start helix in the constricted state and the two-start helix in the super-constricted state. Here we report the cryoEM structure of a super-constricted two-start dynamin 1 filament at 3.74 Å resolution. The two strands are joined by the conserved GTPase dimeric interface. In comparison with the one-start structure, a rotation around Hinge 1 is observed, essential for communicating the chemical power of the GTPase domain and the mechanical force of the Stalk and PH domain onto the underlying membrane. The Stalk interfaces are well conserved and serve as fulcrums for adapting to changing curvatures. Relative to one-start, small rotations per interface accumulate to bring a drastic change in the helical pitch. Elasticity theory rationalizes the diversity of dynamin helical symmetries and suggests corresponding functional significance.
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