ArticleScience (New York, N.Y.)2015
A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly.
Article in Science (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 200 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
200 citing papers in PubMed.
- Munc18 binds to and organizes membrane-bound acceptor Q-SNARE complexes in a fashion that depends on the membrane's lipid composition.bioRxiv : the preprint server for biology · 2026Article
- Munc18-1 is crucial for photoreceptor function, survival and regulation of syntaxin-3 localization and expression.Scientific reports · 2026Article
- Endosomes as central hubs of interorganellar communication and cellular homeostasis.Protein & cell · 2026Review
- VPS33B regulates MHC class II antigen presentation in dendritic cells to drive CD4 T cell immunity.iScience · 2026Article
- Guiding AlphaFold to predict how Munc13-1 opens Syntaxin-1.FEBS open bio · 2026Article
- SNAP-25 disease variants affect synaptic transmission by destabilizing SNARE complexes within a multimeric SNARE ring.Cell reports · 2026Article
- Membrane Merger Dynamics in Exocytosis and Endocytosis.Advances in experimental medicine and biology · 2026Review
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- Two successive oligomeric Munc13 assemblies scaffold vesicle docking and SNARE assembly to support neurotransmitter release.Nature communications · 2025Article
- Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025Article
- Evaluation of synaptotagmin-1 action models by all-atom molecular dynamics simulations.FEBS open bio · 2025Article
- VPS41 recruits biosynthetic LAMP-positive vesicles through interaction with Arl8b.The Journal of cell biology · 2025Article
- Deacetylated SNAP47 recruits HOPS to facilitate autophagosome-lysosome fusion independent of STX17.Nature communications · 2025Article
- A lever hypothesis for Synaptotagmin-1 action in neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Exocyst stimulates multiple steps of exocytic SNARE complex assembly and vesicle fusion.Nature structural & molecular biology · 2025Article
- After their membrane assembly, Sec18 (NSF) and Sec17 (SNAP) promote membrane fusion.Molecular biology of the cell · 2024Article
- Membrane fusion reactions limited by defective SNARE zippering or stiff lipid fatty acyl composition have distinct requirements for Sec17, Sec18, and adenine nucleotide.bioRxiv : the preprint server for biology · 2024Article
- Genome-Scale Screening ofJournal of fungi (Basel, Switzerland) · 2024Article
- Article
- Structure of the endosomal CORVET tethering complex.Nature communications · 2024Article
140 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Fusion of intracellular transport vesicles requires soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) and Sec1/Munc18-family (SM) proteins. Membrane-bridging SNARE complexes are critical for fusion, but their spontaneous assembly is inefficient and may require SM proteins in vivo. We report x-ray structures of Vps33, the SM subunit of the yeast homotypic fusion and vacuole protein-sorting (HOPS) complex, bound to two individual SNAREs. The two SNAREs, one from each membrane, are held in the correct orientation and register for subsequent complex assembly. Vps33 and potentially other SM proteins could thus act as templates for generating partially zipped SNARE assembly intermediates. HOPS was essential to mediate SNARE complex assembly at physiological SNARE concentrations. Thus, Vps33 appears to catalyze SNARE complex assembly through specific SNARE motif recognition.
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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.