ArticleBiophysical journal2016
Assembly and Comparison of Plasma Membrane SNARE Acceptor Complexes.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 23 citations in OpenAlex.
- 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
- Multiple structural states in an intrinsically disordered protein, SNAP-25, using circular dichroism.Biophysical journal · 2025Article
- Synaptophysin accelerates synaptic vesicle fusion by expanding the membrane upon neurotransmitter loading.Science advances · 2025Article
- Functionally distinct SNARE motifs of SNAP25 cooperate in SNARE assembly and membrane fusion.Biophysical journal · 2025Article
- Membrane lipids couple synaptotagmin to SNARE-mediated granule fusion in insulin-secreting cells.Molecular biology of the cell · 2024Article
- Mass spectrometry uncovers intermediates and off-pathway complexes for SNARE complex assembly.Communications biology · 2023Article
- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- Drunken lipid membranes, not drunken SNARE proteins, promote fusion in a model of neurotransmitter release.Frontiers in molecular neuroscience · 2022Article
- In vitro single vesicle fusion assays based on pore-spanning membranes: merits and drawbacks.European biophysics journal : EBJ · 2021Review
- Synaptotagmin-1-, Munc18-1-, and Munc13-1-dependent liposome fusion with a few neuronal SNAREs.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Distinct insulin granule subpopulations implicated in the secretory pathology of diabetes types 1 and 2.eLife · 2020Article
- In vitro fusion of single synaptic and dense core vesicles reproduces key physiological properties.Nature communications · 2019Article
- Structural dynamics and transient lipid binding of synaptobrevin-2 tune SNARE assembly and membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A molecular mechanism for calcium-mediated synaptotagmin-triggered exocytosis.Nature structural & molecular biology · 2018Article
- Choice of reconstitution protocol modulates the aggregation state of full-length membrane-reconstituted synaptotagmin-1.Protein science : a publication of the Protein Society · 2018Article
- Solution NMR of SNAREs, complexin and α-synuclein in association with membrane-mimetics.Progress in nuclear magnetic resonance spectroscopy · 2018Review
- Asymmetric Phosphatidylethanolamine Distribution Controls Fusion Pore Lifetime and Probability.Biophysical journal · 2017Article
- Regulation of insulin exocytosis by calcium-dependent protein kinase C in beta cells.Cell calcium · 2017Review
- Complexin Binding to Membranes and Acceptor t-SNAREs Explains Its Clamping Effect on Fusion.Biophysical journal · 2017Article
- Reconstitution of calcium-mediated exocytosis of dense-core vesicles.Science advances · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Neuronal exocytotic membrane fusion occurs on a fast timescale and is dependent on interactions between the vesicle SNARE synaptobrevin-2 and the plasma membrane SNAREs syntaxin-1a and SNAP-25 with a 1:1:1 stoichiometry. Reproducing fast fusion rates as observed in cells by reconstitution in vitro has been hindered by the spontaneous assembly of a 2:1 syntaxin-1a:SNAP-25 complex on target membranes that kinetically alters the binding of synaptobrevin-2. Previously, an artificial SNARE acceptor complex consisting of 1:1:1 syntaxin-1a(residues 183-288):SNAP-25:syb(residues 49-96) was found to greatly accelerate the rates of lipid mixing of reconstituted target and vesicle SNARE proteoliposomes. Here we present two (to our knowledge) new procedures to assemble membrane-bound 1:1 SNARE acceptor complexes that produce fast and efficient fusion without the need of the syb(49-96) peptide. In the first procedure, syntaxin-1a is purified in a strictly monomeric form and subsequently assembled with SNAP-25 in detergent with the correct 1:1 stoichiometry. In the second procedure, monomeric syntaxin-1a and dodecylated (d-)SNAP-25 are separately reconstituted into proteoliposomes and subsequently assembled in the plane of merged target lipid bilayers. Examining single particle fusion between synaptobrevin-2 proteoliposomes and planar-supported bilayers containing the two different SNARE acceptor complexes revealed similar fast rates of fusion. Changing the stoichiometry of syntaxin-1a and d-SNAP-25 in the target bilayer had significant effects on docking, but little effect on the rates of synaptobrevin-2 proteoliposome fusion.
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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.