ArticleeLife2015
Structural basis for activation, assembly and membrane binding of ESCRT-III Snf7 filaments.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.
What it found
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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
92 citing papers in PubMed.
- Characterization of the Mos10 (Vps60) ESCRT-III complex.Bioscience reports · 2026Article
- Large eukaryotic DNA viruses encode ESCRT machinery for membrane remodelling.Nature microbiology · 2026Article
- Molecular Mechanism of the SepF N‑Terminal Conformational Switch in Ring Assembly and Membrane Anchoring.JACS Au · 2026Article
- Targeted disruption of vacuolar-sorting protein and inhibitor of apoptosis genes via virus-induced gene silencing alters survival and reproduction of Diaphorina citri.Pest management science · 2026Article
- Phosphatidylinositol diphosphate binding by ESCRT-III filaments.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The role of extracellular vesicles-associated proteins markers in prostate cancer: a review.Discover oncology · 2026Review
- Exosomes in Amyloid Propagation-Roles in Neurodegeneration.Molecular neurobiology · 2026Review
- ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 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
- The soluble state of the HIV-1 Vpu protein forms a complex with CaProtein science : a publication of the Protein Society · 2026Article
- Wbm0152, an outer membrane lipoprotein of the Wolbachia endosymbiont of Brugia malayi, inhibits yeast ESCRT complex activity.PLoS pathogens · 2025Article
- 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
- Analysis of native Ist1 dynamics reveals multiple pools of ESCRT-III on endosomes.The Journal of cell biology · 2025Article
- Temporal dissection of the roles of Atg4 and ESCRT in autophagosome formation in yeast.Cell death and differentiation · 2025Article
- Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair.Nature structural & molecular biology · 2025Article
- The cyanobacterial protein VIPP1 forms ESCRT-III-like structures on lipid bilayers.Nature structural & molecular biology · 2025Article
- Asgard archaea reveal the conserved principles of ESCRT-III membrane remodeling.Science advances · 2025Article
- Mechanism of Centrosomal Protein 55 (CEP55) Loading Into Exosomes.Journal of extracellular vesicles · 2025Article
- Nuclear and degradative functions of the ESCRT-III pathway: implications for neurodegenerative disease.Nucleus (Austin, Tex.) · 2024Review
32 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The endosomal sorting complexes required for transport (ESCRTs) constitute hetero-oligomeric machines that catalyze multiple topologically similar membrane-remodeling processes. Although ESCRT-III subunits polymerize into spirals, how individual ESCRT-III subunits are activated and assembled together into a membrane-deforming filament remains unknown. Here, we determine X-ray crystal structures of the most abundant ESCRT-III subunit Snf7 in its active conformation. Using pulsed dipolar electron spin resonance spectroscopy (PDS), we show that Snf7 activation requires a prominent conformational rearrangement to expose protein-membrane and protein-protein interfaces. This promotes the assembly of Snf7 arrays with ~30 Å periodicity into a membrane-sculpting filament. Using a combination of biochemical and genetic approaches, both in vitro and in vivo, we demonstrate that mutations on these protein interfaces halt Snf7 assembly and block ESCRT function. The architecture of the activated and membrane-bound Snf7 polymer provides crucial insights into the spatially unique ESCRT-III-mediated membrane remodeling.
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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.