ArticleProceedings of the National Academy of Sciences of the United States of America2001
VIPP1, a nuclear gene of Arabidopsis thaliana essential for thylakoid membrane formation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 135 papers.
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135 citing papers in PubMed, 330 citations in OpenAlex.
- OsVIPP1 Supports Rice Leaf Chloroplast Development and Is Associated with Seed Metabolic Changes and Yield-Related Traits.Plants (Basel, Switzerland) · 2026Article
- VIA1 is a conserved regulator of thylakoid membrane integrity that acts through VIPP1.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
- 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 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
- 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 basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies.Nature structural & molecular biology · 2025Article
- Chloroplast Vesiculation and InducedPlant direct · 2025Article
- The clues offered by SNAREs on the vacuoles of plants and animals.Frontiers in plant science · 2025Review
- 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
- Exploring the Origins and Evolution of Oxygenic and Anoxygenic Photosynthesis in Deeply Branched Cyanobacteriota.Molecular biology and evolution · 2024Article
- TurboID reveals the proxiomes of Chlamydomonas proteins involved in thylakoid biogenesis and stress response.Plant physiology · 2023Article
- Characterization of thylakoid division using chloroplast dividing mutants in Arabidopsis.Photosynthesis research · 2023Article
- Absolute quantification of cellular levels of photosynthesis-related proteins in Synechocystis sp. PCC 6803.Photosynthesis research · 2023Article
75 more citing papers are in PubMed but not listed here.
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8 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The conversion of light to chemical energy by the process of photosynthesis is localized to the thylakoid membrane network in plant chloroplasts. Although several pathways have been described that target proteins into and across the thylakoids, little is known about the origin of this membrane system or how the lipid backbone of the thylakoids is transported and fused with the target membrane. Thylakoid biogenesis and maintenance seem to involve the flow of membrane elements via vesicular transport. Here we show by mutational analysis that deletion of a single gene called VIPP1 (vesicle-inducing protein in plastids 1) is deleterious to thylakoid membrane formation. Although VIPP1 is a hydrophilic protein it is found in both the inner envelope and the thylakoid membranes. In VIPP1 deletion mutants vesicle formation is abolished. We propose that VIPP1 is essential for the maintenance of thylakoids by a transport pathway not previously recognized.
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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.