ArticleNature structural & molecular biology2025
Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Self-supervised image denoising and restoration method for atomic force microscopy.Nature communications · 2026Article
- Bottom-up reconstitution of model membrane systems: a mini-review.Biochemical Society transactions · 2026Review
- Phosphatidylinositol diphosphate binding by ESCRT-III filaments.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins.The Plant journal : for cell and molecular biology · 2026Review
- ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026Review
- The cyanobacterial ESCRT-III protein IM30 forms biomolecular condensates at physiologically relevant conditions.Biophysical journal · 2026Article
- Chloroplast heat shock protein cpHsc70-1 interacts with thylakoid membrane remodeling protein VIPP1 C-terminal tail and controls VIPP1 oligomer assembly.PNAS nexus · 2026Article
- Membrane binding of a cyanobacterial ESCRT-III protein crucially involves the helix α1-3 hairpin conserved in all superfamily members.Protein science : a publication of the Protein Society · 2025Article
- Thylakostasis: key factors in thylakoid membrane organization with emphasis on biogenesis and remodeling proteins in vascular plants.Plant & cell physiology · 2025Review
- The evolution and mechanism of bacterial and archaeal ESCRT-III-like systems.Current opinion in structural biology · 2025Review
- The green ESCRTs: Newly defined roles for ESCRT proteins in plants.The Journal of biological chemistry · 2025Review
- The thylakoid membrane remodeling protein VIPP1 forms bundled oligomers in tobacco chloroplasts.Plant physiology · 2025Article
- Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair.Nature structural & molecular biology · 2025Article
- Monomer unfolding of a bacterial ESCRT-III superfamily member is coupled to oligomer disassembly.Protein science : a publication of the Protein Society · 2024Article
- Structure, biogenesis, and evolution of thylakoid membranes.The Plant cell · 2024Review
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Authors and funding
7 authors.
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Abstract
The ESCRT-III-like protein Vipp1 couples filament polymerization with membrane remodeling. It assembles planar sheets as well as 3D rings and helical polymers, all implicated in mitigating plastid-associated membrane stress. The architecture of Vipp1 planar sheets and helical polymers remains unknown, as do the geometric changes required to transition between polymeric forms. Here we show how cyanobacterial Vipp1 assembles into morphologically-related sheets and spirals on membranes in vitro. The spirals converge to form a central ring similar to those described in membrane budding. Cryo-EM structures of helical filaments reveal a close geometric relationship between Vipp1 helical and planar lattices. Moreover, the helical structures reveal how filaments twist-a process required for Vipp1, and likely other ESCRT-III filaments, to transition between planar and 3D architectures. Overall, our results provide a molecular model for Vipp1 ring biogenesis and a mechanism for Vipp1 membrane stabilization and repair, with implications for other ESCRT-III systems.
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