ReviewProtein science : a publication of the Protein Society2017
Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers.
Review in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 57 citations in OpenAlex.
- Turbocharging synaptic transmission: 12 SNAREpins are required for rapid release of reconstituted synaptic vesicles.Science advances · 2026Article
- Functionally distinct SNARE motifs of SNAP25 cooperate in SNARE assembly and membrane fusion.Biophysical journal · 2025Article
- Exocyst stimulates multiple steps of exocytic SNARE complex assembly and vesicle fusion.Nature structural & molecular biology · 2025Article
- Dual-Ring SNAREpin Machinery Tuning for Fast Synaptic Vesicle Fusion.Biomolecules · 2024Article
- Tomosyns attenuate SNARE assembly and synaptic depression by binding to VAMP2-containing template complexes.Nature communications · 2024Article
- Article
- Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024Review
- Synaptophysin chaperones the assembly of 12 SNAREpins under each ready-release vesicle.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Complexin-1 regulated assembly of single neuronal SNARE complex revealed by single-molecule optical tweezers.Communications biology · 2023Article
- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- A dynamic template complex mediates Munc18-chaperoned SNARE assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The beginning and the end of SNARE-induced membrane fusion.FEBS open bio · 2022Review
- Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022Review
- Article
- Nano-Precision Tweezers for Mechanosensitive Proteins and Beyond.Molecules and cells · 2022Review
- Chaperoning SNARE Folding and Assembly.Annual review of biochemistry · 2021Review
- Sec17/Sec18 can support membrane fusion without help from completion of SNARE zippering.eLife · 2021Article
- Effects of Ligand Binding on the Energy Landscape of Acyl-CoA-Binding Protein.Biophysical journal · 2020Article
- Munc13-1 MUN domain and Munc18-1 cooperatively chaperone SNARE assembly through a tetrameric complex.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) are universal molecular engines that drive membrane fusion. Particularly, synaptic SNAREs mediate fast calcium-triggered fusion of neurotransmitter-containing vesicles with plasma membranes for synaptic transmission, the basis of all thought and action. During membrane fusion, complementary SNAREs located on two apposed membranes (often called t- and v-SNAREs) join together to assemble into a parallel four-helix bundle, releasing the energy to overcome the energy barrier for fusion. A long-standing hypothesis suggests that SNAREs act like a zipper to draw the two membranes into proximity and thereby force them to fuse. However, a quantitative test of this SNARE zippering hypothesis was hindered by difficulties to determine the energetics and kinetics of SNARE assembly and to identify the relevant folding intermediates. Here, we first review different approaches that have been applied to study SNARE assembly and then focus on high-resolution optical tweezers. We summarize the folding energies, kinetics, and pathways of both wild-type and mutant SNARE complexes derived from this new approach. These results show that synaptic SNAREs assemble in four distinct stages with different functions: slow N-terminal domain association initiates SNARE assembly; a middle domain suspends and controls SNARE assembly; and rapid sequential zippering of the C-terminal domain and the linker domain directly drive membrane fusion. In addition, the kinetics and pathway of the stagewise assembly are shared by other SNARE complexes. These measurements prove the SNARE zippering hypothesis and suggest new mechanisms for SNARE assembly regulated by other proteins.
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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.