ArticleBiochimica et biophysica acta. Bioenergetics2017
The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion.
Article in Biochimica et biophysica acta. Bioenergetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 36 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
- 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
- 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 evolution and mechanism of bacterial and archaeal ESCRT-III-like systems.Current opinion in structural biology · 2025Review
- 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
- Monomer unfolding of a bacterial ESCRT-III superfamily member is coupled to oligomer disassembly.Protein science : a publication of the Protein Society · 2024Article
- Exploring the Origins and Evolution of Oxygenic and Anoxygenic Photosynthesis in Deeply Branched Cyanobacteriota.Molecular biology and evolution · 2024Article
- Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily.Cell · 2021Article
- Orchestral manoeuvres in the light: crosstalk needed for regulation of the Chlamydomonas carbon concentration mechanism.Journal of experimental botany · 2021Review
- IM30 IDPs form a membrane-protective carpet upon super-complex disassembly.Communications biology · 2020Article
- Proton Leakage Is Sensed by IM30 and Activates IM30-Triggered Membrane Fusion.International journal of molecular sciences · 2020Article
- GTP hydrolysis by Synechocystis IM30 does not decisively affect its membrane remodeling activity.Scientific reports · 2020Article
- The TomatoFrontiers in plant science · 2020Article
- The Fusion Activity of IM30 Rings Involves Controlled Unmasking of the Fusogenic Core.Frontiers in plant science · 2019Article
- Functional Implications of Multiple IM30 Oligomeric States.Frontiers in plant science · 2019Review
- MgThe Journal of biological chemistry · 2018Article
- VIPP1 Involved in Chloroplast Membrane Integrity Has GTPase Activity in Vitro.Plant physiology · 2018Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
IM30/Vipp1 proteins are crucial for thylakoid membrane biogenesis in chloroplasts and cyanobacteria. A characteristic C-terminal extension distinguishes these proteins from the homologous bacterial PspA proteins, and this extension has been discussed to be key for the IM30/Vipp1 activity. Here we report that the extension of the Synechocystis IM30 protein is indispensable, and argue that both, the N-terminal PspA-domain as well as the C-terminal extension are needed in order for the IM30 protein to conduct its in vivo function. In vitro, we show that the PspA-domain of IM30 is vital for stability/folding and oligomer formation of IM30 as well as for IM30-triggered membrane fusion. In contrast, the IM30 C-terminal domain is involved in and necessary to stabilize defined contacts to negatively charged membrane surfaces, and to modulate the IM30-induced membrane fusion activity. Although the two IM30 protein domains have distinct functional roles, only together they enable IM30 to work properly.
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Registered trials
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.