ArticleScientific reports2019
VIPP1 rods engulf membranes containing phosphatidylinositol phosphates.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 63 citations in OpenAlex.
- Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins.The Plant journal : for cell and molecular 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
- 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 FIBRILLIN multigene family in tomato, their roles in plastoglobuli structure and metabolism.The Plant journal : for cell and molecular biology · 2025Article
- 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
- Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies.Nature structural & molecular biology · 2025Article
- The cyanobacterial protein VIPP1 forms ESCRT-III-like structures on lipid bilayers.Nature structural & molecular biology · 2025Article
- Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair.Nature structural & molecular biology · 2025Article
- Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies.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
- The phage shock protein (PSP) envelope stress response: discovery of novel partners and evolutionary history.mSystems · 2024Article
- TurboID reveals the proxiomes of Chlamydomonas proteins involved in thylakoid biogenesis and stress response.Plant physiology · 2023Article
- Cyanobacterial membrane dynamics in the light of eukaryotic principles.Bioscience reports · 2023Article
- Membrane destabilization and pore formation induced by the Synechocystis IM30 protein.Biophysical journal · 2022Article
- Chloroplast-localized PITP7 is essential for plant growth and photosynthetic function in Arabidopsis.Physiologia plantarum · 2022Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In cyanobacteria and plants, VIPP1 plays crucial roles in the biogenesis and repair of thylakoid membrane protein complexes and in coping with chloroplast membrane stress. In chloroplasts, VIPP1 localizes in distinct patterns at or close to envelope and thylakoid membranes. In vitro, VIPP1 forms higher-order oligomers of >1 MDa that organize into rings and rods. However, it remains unknown how VIPP1 oligomerization is related to function. Using time-resolved fluorescence anisotropy and sucrose density gradient centrifugation, we show here that Chlamydomonas reinhardtii VIPP1 binds strongly to liposomal membranes containing phosphatidylinositol-4-phosphate (PI4P). Cryo-electron tomography reveals that VIPP1 oligomerizes into rods that can engulf liposomal membranes containing PI4P. These findings place VIPP1 into a group of membrane-shaping proteins including epsin and BAR domain proteins. Moreover, they point to a potential role of phosphatidylinositols in directing the shaping of chloroplast membranes.
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Registered trials
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