ArticleNature structural & molecular biology2025
Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies.
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 17 papers.
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Who cites it
17 citing papers in PubMed.
- Self-supervised image denoising and restoration method for atomic force microscopy.Nature communications · 2026Article
- Phosphatidylinositol diphosphate binding by ESCRT-III filaments.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Lipid metabolism and contact site homologs are present at the chloroplast envelope-thylakoid interface.Nature communications · 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
- ETSAM: Effectively Segmenting Cell Membranes in cryo-Electron Tomograms.Research square · 2026Article
- The cyanobacterial ESCRT-III protein IM30 forms biomolecular condensates at physiologically relevant conditions.Biophysical journal · 2026Article
- Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery.Proceedings of the National Academy of Sciences of the United States of America · 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
- Functional reconstitution of bacterial ESCRT-III protein PspA identifies key regions in membrane binding and remodeling.Protein science : a publication of the Protein Society · 2025Article
- The bacterial ESCRT-III PspA rods thin lipid tubules and increase membrane curvature through helix α0 interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- 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
- Monomer unfolding of a bacterial ESCRT-III superfamily member is coupled to oligomer disassembly.Protein science : a publication of the Protein Society · 2024Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vesicle-inducing protein in plastids 1 (Vipp1) is critical for thylakoid membrane biogenesis and maintenance. Although Vipp1 has recently been identified as a member of the endosomal sorting complexes required for transport III superfamily, it is still unknown how Vipp1 remodels membranes. Here, we present cryo-electron microscopy structures of Synechocystis Vipp1 interacting with membranes: seven structures of helical and stacked-ring assemblies at 5-7-Å resolution engulfing membranes and three carpet structures covering lipid vesicles at ~20-Å resolution using subtomogram averaging. By analyzing ten structures of N-terminally truncated Vipp1, we show that helix α0 is essential for membrane tubulation and forms the membrane-anchoring domain of Vipp1. Lastly, using a conformation-restrained Vipp1 mutant, we reduced the structural plasticity of Vipp1 and determined two structures of Vipp1 at 3.0-Å resolution, resolving the molecular details of membrane-anchoring and intersubunit contacts of helix α0. Our data reveal membrane curvature-dependent structural transitions from carpets to rings and rods, some of which are capable of inducing and/or stabilizing high local membrane curvature triggering membrane fusion.
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