ArticleThe Plant cell2012
Essential role of VIPP1 in chloroplast envelope maintenance in Arabidopsis.
Article in The Plant cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed, 135 citations in OpenAlex.
- 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
- 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
- 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
- Characterizing genome-wide changes associated with inbreeding tolerance in cranberry: insights into homozygosity and heterozygosity.Frontiers in plant science · 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
- Beyond rings and rods: In-situ imaging reveals the role of VIPP1 in chloroplast homeostasis in tobacco.Plant physiology · 2025Article
- 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
- Defining the heterogeneous composition of Arabidopsis thylakoid membrane.The Plant journal : for cell and molecular biology · 2025Article
- A comparative study on the distinct staygreen characteristics of two ecological types ofFrontiers in plant science · 2025Article
- 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
- CaProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Chlamydiae as symbionts of photosynthetic dinoflagellates.The ISME journal · 2024Article
- TurboID reveals the proxiomes of Chlamydomonas proteins involved in thylakoid biogenesis and stress response.Plant physiology · 2023Article
- Genetic dissection of maize (Zea mays L.) chlorophyll content using multi-locus genome-wide association studies.BMC genomics · 2023Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
VESICLE-INDUCING PROTEIN IN PLASTIDS1 (VIPP1), proposed to play a role in thylakoid biogenesis, is conserved in photosynthetic organisms and is closely related to Phage Shock Protein A (PspA), which is involved in plasma membrane integrity in Escherichia coli. This study showed that chloroplasts/plastids in Arabidopsis thaliana vipp1 knockdown and knockout mutants exhibit a unique morphology, forming balloon-like structures. This altered morphology, as well as lethality of vipp1, was complemented by expression of VIPP1 fused to green fluorescent protein (VIPP1-GFP). Several lines of evidence show that the balloon chloroplasts result from chloroplast swelling related to osmotic stress, implicating VIPP1 in the maintenance of plastid envelopes. In support of this, Arabidopsis VIPP1 rescued defective proton leakage in an E. coli pspA mutant. Microscopy observation of VIPP1-GFP in transgenic Arabidopsis revealed that VIPP1 forms large macrostructures that are integrated into various morphologies along the envelopes. Furthermore, live imaging revealed that VIPP1-GFP is highly mobile when chloroplasts are subjected to osmotic stress. VIPP1-GFP showed dynamic movement in the transparent area of spherical chloroplasts, as the fluorescent molecules formed filament-like structures likely derived from disassembly of the large VIPP1 complex. Collectively, our data demonstrate that VIPP1 is a multifunctional protein in chloroplasts that is critically important for envelope maintenance.
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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.