ArticleMolecular microbiology2014
Localisation and interactions of the Vipp1 protein in cyanobacteria.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Organ-on-a-Chip and Microfluidic Plant Cell Culture Systems: The Next Frontier for Controlled Secondary Metabolite Production and Real-Time Metabolomic Monitoring.Plants (Basel, Switzerland) · 2026Review
- 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
- 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 cyanobacterial protein VIPP1 forms ESCRT-III-like structures on lipid bilayers.Nature structural & molecular biology · 2025Article
- CyanoTag: Discovery of protein function facilitated by high-throughput endogenous tagging in a photosynthetic prokaryote.Science advances · 2025Article
- R-DeeP/TripepSVM identifies the RNA-binding OB-fold-like protein PatR as regulator of heterocyst patterning.Nucleic acids research · 2025Article
- Monomer unfolding of a bacterial ESCRT-III superfamily member is coupled to oligomer disassembly.Protein science : a publication of the Protein Society · 2024Article
- Dynamic Changes in the Thylakoid Proteome of Cyanobacteria during Light-Regulated Thylakoid Membrane Development.Plants (Basel, Switzerland) · 2023Article
- TurboID reveals the proxiomes of Chlamydomonas proteins involved in thylakoid biogenesis and stress response.Plant physiology · 2023Article
- Liquid-Liquid Phase Separation of the DEAD-Box Cyanobacterial RNA Helicase Redox (CrhR) into Dynamic Membraneless Organelles inApplied and environmental microbiology · 2023Article
- The increasing role of structural proteomics in cyanobacteria.Essays in biochemistry · 2023Review
- Asymmetric survival in single-cell lineages of cyanobacteria in response to photodamage.Photosynthesis research · 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
- Article
- A homolog of GuidedEntry of Tail-anchored proteins3 functions in membrane-specific protein targeting in chloroplasts of Arabidopsis.The Plant cell · 2021Article
- Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily.Cell · 2021Article
Corrections and comments
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Authors and funding
14 authors.
Funding
Abstract
The Vipp1 protein is essential in cyanobacteria and chloroplasts for the maintenance of photosynthetic function and thylakoid membrane architecture. To investigate its mode of action we generated strains of the cyanobacteria Synechocystis sp. PCC6803 and Synechococcus sp. PCC7942 in which Vipp1 was tagged with green fluorescent protein at the C-terminus and expressed from the native chromosomal locus. There was little perturbation of function. Live-cell fluorescence imaging shows dramatic relocalisation of Vipp1 under high light. Under low light, Vipp1 is predominantly dispersed in the cytoplasm with occasional concentrations at the outer periphery of the thylakoid membranes. High light induces Vipp1 coalescence into localised puncta within minutes, with net relocation of Vipp1 to the vicinity of the cytoplasmic membrane and the thylakoid membranes. Pull-downs and mass spectrometry identify an extensive collection of proteins that are directly or indirectly associated with Vipp1 only after high-light exposure. These include not only photosynthetic and stress-related proteins but also RNA-processing, translation and protein assembly factors. This suggests that the Vipp1 puncta could be involved in protein assembly. One possibility is that Vipp1 is involved in the formation of stress-induced localised protein assembly centres, enabling enhanced protein synthesis and delivery to membranes under stress conditions.
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