ArticleMolecular biology of the cell2008
Munc18a scaffolds SNARE assembly to promote membrane fusion.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Syntaxin 3B Mediates Light-Dependent Interactions with STXBP1 and Arrestin 4: Distinct Roles in Rods and Cones.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Light-dependent regulation of neurotransmitter release from rod photoreceptor ribbon synapses involves an interplay of Complexin 4 and Transducin with the SNARE complex.Frontiers in molecular neuroscience · 2024Article
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- The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022Review
- STXBP1 encephalopathies: Clinical spectrum, disease mechanisms, and therapeutic strategies.Journal of neurochemistry · 2021Review
- Munc13 activates the Munc18-1/syntaxin-1 complex and enables Munc18-1 to prime SNARE assembly.The EMBO journal · 2020Article
- The N-peptide-binding mode is critical to Munc18-1 function in synaptic exocytosis.The Journal of biological chemistry · 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
- Tyrosine phosphorylation of Munc18-1 inhibits synaptic transmission by preventing SNARE assembly.The EMBO journal · 2018Article
- Munc18a clusters SNARE-bearing liposomes prior toThe Biochemical journal · 2017Article
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- Munc18-1 and the Syntaxin-1 N Terminus Regulate Open-Closed States in a t-SNARE Complex.Structure (London, England : 1993) · 2016Article
- The trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosis.Nature communications · 2015Article
- Reconstituting Intracellular Vesicle Fusion Reactions: The Essential Role of Macromolecular Crowding.Journal of the American Chemical Society · 2015Article
- Munc18a does not alter fusion rates mediated by neuronal SNAREs, synaptotagmin, and complexin.The Journal of biological chemistry · 2015Article
- Reconstituting SNARE-mediated membrane fusion at the single liposome level.Methods in cell biology · 2015Article
- A pivotal role for pro-335 in balancing the dual functions of Munc18-1 domain-3a in regulated exocytosis.The Journal of biological chemistry · 2014Article
- Review
- In vitro assay using engineered yeast vacuoles for neuronal SNARE-mediated membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Munc18a is an SM protein required for SNARE-mediated fusion. The molecular details of how Munc18a acts to enhance neurosecretion have remained elusive. Here, we use in vitro fusion assays to characterize how specific interactions between Munc18a and the neuronal SNAREs enhance the rate and extent of fusion. We show that Munc18a interacts directly and functionally with the preassembled t-SNARE complex. Analysis of Munc18a point mutations indicates that Munc18a interacts with helix C of the Syntaxin1a NRD in the t-SNARE complex. Replacement of the t-SNARE SNAP25b with yeast Sec9c had little effect, suggesting that Munc18a has minimal contact with SNAP25b within the t-SNARE complex. A chimeric Syntaxin built of the Syntaxin1a NRD and the H3 domain of yeast Sso1p and paired with Sec9c eliminated stimulation of fusion, suggesting that Munc18a/Syntaxin1a H3 domain contacts are important. Additionally, a Syntaxin1A mutant lacking a flexible linker region that allows NRD movement abolished stimulation of fusion. These experiments suggest that Munc18a binds to the Syntaxin1a NRD and H3 domain within the assembled t-SNARE complex, positioning them for productive VAMP2 binding. In this capacity, Munc18a serves as a platform for trans-SNARE complex assembly that facilitates efficient SNARE-mediated membrane fusion.
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Registered trials
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