ArticleThe EMBO journal2017
An activated Q-SNARE/SM protein complex as a possible intermediate in SNARE assembly.
Article in The EMBO journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 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
- A PIP2-stabilized syntaxin-1a structure mapped with transition metal ion FRET and unnatural fluorescent amino acids at the plasma membrane.Structure (London, England : 1993) · 2026Article
- Complexin regulation of synaptic vesicle release: mechanisms in the central nervous system and specialized retinal ribbon synapses.Cell communication and signaling : CCS · 2024Review
- Intermediate steps in the formation of neuronal SNARE complexes.The Journal of biological chemistry · 2024Article
- Article
- Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024Review
- 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
- Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022Review
- The Effect of Sleep Deprivation and Subsequent Recovery Period on the Synaptic Proteome of Rat Cerebral Cortex.Molecular neurobiology · 2022Article
- Reexamination of N-terminal domains of syntaxin-1 in vesicle fusion from central murine synapses.eLife · 2021Article
- Chaperoning SNARE Folding and Assembly.Annual review of biochemistry · 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
- Structural Roles for the Juxtamembrane Linker Region and Transmembrane Region of Synaptobrevin 2 in Membrane Fusion.Frontiers in cell and developmental biology · 2020Article
- Unc13: a multifunctional synaptic marvel.Current opinion in neurobiology · 2019Review
- Phosphatidylinositol 4,5 Bisphosphate Controls the cis and trans Interactions of Synaptotagmin 1.Biophysical journal · 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
- Article
- Syntaxin clusters at secretory granules in a munc18-bound conformation.Molecular biology of the cell · 2018Article
- SNARE zippering requires activation by SNARE-like peptides in Sec1/Munc18 proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
4 authors.
Funding
Abstract
Assembly of the SNARE proteins syntaxin1, SNAP25, and synaptobrevin into a SNARE complex is essential for exocytosis in neurons. For efficient assembly, SNAREs interact with additional proteins but neither the nature of the intermediates nor the sequence of protein assembly is known. Here, we have characterized a ternary complex between syntaxin1, SNAP25, and the SM protein Munc18-1 as a possible acceptor complex for the R-SNARE synaptobrevin. The ternary complex binds synaptobrevin with fast kinetics, resulting in the rapid formation of a fully zippered SNARE complex to which Munc18-1 remains tethered by the N-terminal domain of syntaxin1. Intriguingly, only one of the synaptobrevin truncation mutants (Syb1-65) was able to bind to the syntaxin1:SNAP25:Munc18-1 complex, suggesting either a cooperative zippering mechanism that proceeds bidirectionally or the progressive R-SNARE binding via an SM template. Moreover, the complex is resistant to disassembly by NSF Based on these findings, we consider the ternary complex as a strong candidate for a physiological intermediate in SNARE assembly.
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