ArticleJournal of the American Chemical Society2014
A half-zippered SNARE complex represents a functional intermediate in membrane fusion.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Munc18 reprograms the intrinsic neuronal SNARE complex assembly pathway.bioRxiv : the preprint server for biology · 2026Article
- Synaptic transmission: Munc13 assembles onto PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Synaptobrevin-2 disease variants reveal spatial constraints within the presynaptic active zone.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Quantitative single-molecule analysis of assembly and CaCommunications biology · 2024Article
- Exploring the Landscape of Pre- and Post-Synaptic Pediatric Disorders with Epilepsy: A Narrative Review on Molecular Mechanisms Involved.International journal of molecular sciences · 2024Review
- 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
- Diacylglycerol-dependent hexamers of the SNARE-assembling chaperone Munc13-1 cooperatively bind vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- Functional regulation of syntaxin-1: An underlying mechanism mediating exocytosis in neuroendocrine cells.Frontiers in endocrinology · 2023Review
- Neuronal SNARE complex assembly guided by Munc18-1 and Munc13-1.FEBS open bio · 2022Review
- Synaptotagmin rings as high-sensitivity regulators of synaptic vesicle docking and fusion.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Stability profile of the neuronal SNARE complex reflects its potency to drive fast membrane fusion.Biophysical journal · 2022Article
- Chaperoning SNARE Folding and Assembly.Annual review of biochemistry · 2021Review
- Membrane Binding and Homodimerization of Atg16 Via Two Distinct Protein Regions is Essential for Autophagy in Yeast.Journal of molecular biology · 2021Article
- In vitro single vesicle fusion assays based on pore-spanning membranes: merits and drawbacks.European biophysics journal : EBJ · 2021Review
- SNARE Zippering Is Suppressed by a Conformational Constraint that Is Removed by v-SNARE Splitting.Cell reports · 2021Article
- Mutations in the Neuronal Vesicular SNARE VAMP2 Affect Synaptic Membrane Fusion and Impair Human Neurodevelopment.American journal of human genetics · 2019Article
- SNARE machinery is optimized for ultrafast fusion.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
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Authors and funding
6 authors.
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Abstract
SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins mediate fusion by pulling biological membranes together via a zippering mechanism. Recent biophysical studies have shown that t- and v-SNAREs can assemble in multiple stages from the N-termini toward the C-termini. Here we show that functionally, membrane fusion requires a sequential, two-step folding pathway and assign specific and distinct functions for each step. First, the N-terminal domain (NTD) of the v-SNARE docks to the t-SNARE, which leads to a conformational rearrangement into an activated half-zippered SNARE complex. This partially assembled SNARE complex locks the C-terminal (CTD) portion of the t-SNARE into the same structure as in the postfusion 4-helix bundle, thereby creating the binding site for the CTD of the v-SNARE and enabling fusion. Then zippering of the remaining CTD, the membrane-proximal linker (LD), and transmembrane (TMD) domains is required and sufficient to trigger fusion. This intrinsic property of the SNAREs fits well with the action of physiologically vital regulators such as complexin. We also report that NTD assembly is the rate-limiting step. Our findings provide a refined framework for delineating the molecular mechanism of SNARE-mediated membrane fusion and action of regulatory proteins.
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