Munc13 mediates the transition from the closed syntaxin–Munc18 complex to the SNARE complex
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During the priming step that leaves synaptic vesicles ready for neurotransmitter release, the SNARE syntaxin-1 transitions from a closed conformation that binds Munc18-1 tightly to an open conformation within the highly stable SNARE complex. Control of this conformational transition is important for brain function, but the underlying mechanism is unknown. NMR and fluorescence experiments now show that the Munc13-1 MUN domain, which plays a central role in vesicle priming, markedly accelerates the transition from the syntaxin-1-Munc18-1 complex to the SNARE complex. This activity depends on weak interactions of the MUN domain with the syntaxin-1 SNARE motif, and probably with Munc18-1. Together with available physiological data, these results provide a defined molecular basis for synaptic vesicle priming, and they illustrate how weak protein-protein interactions can play crucial biological roles by promoting transitions between high-affinity macromolecular assemblies.
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Munc13 opens syntaxin-1, allowing trans-zippering of SNAREs from the N- to C-terminals and formation of a 4-helix trans-complex or ternary complex.
“Munc13 opens syntaxin-1 (407), allowing the trans-zippering of the SNAREs in the plasma and granular membranes from the N- to the C-terminals (which are anchored to the membrane). This leads to the formation of a 4-helix trans-complex, also referred to as the ‘ternary complex’ (100) (Figure 16B, step ii).”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [407]
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“…- SNAP - resistant mechanism ( 3 , 17 ) in which Munc18 - 1 binds first to a closed conformation of syntaxin - 1 ( 18 , 19 ) and later binds to synaptobrevin, forming a template complex ( 20 – 22 ) for SNARE assembly while Munc13 bridges the two membranes ( 4 , 23 ) and opens syntaxin - 1 ( 24 ).”
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- Authors
- Ma, C., Li, W., Xu, Y., & Rizo, J.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Corresponding author
- Rizo, Josep
- Venue
- Nature Structural & Molecular Biology
- Published
- 2011-04-17
- Volume
- 18
- Issue
- 5
- Pages
- 542-549
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC3087822
- OpenAlex
- W2086919645
- Cited by
- 363
- References
- 60
- Citations by year
- 2026: 15 · 2025: 21 · 2024: 17 · 2023: 27 · 2022: 36 · 2021: 27 · 2020: 21 · 2019: 16 · 2018: 24 · 2017: 35 · 2016: 20 · 2015: 21 · 2014: 24 · 2013: 25 · 2012: 24
- FWCI
- 12.74
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (NS 37200, R01NS037200)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- Munc13-1, syntaxin-1, Munc18-1, SNARE complex, synaptic vesicle priming, protein-protein interaction, conformational change, neurotransmitter release, weak interaction, synaptic vesicle exocytosis
- MeSH terms
- Animals, Binding Sites, Humans, Nerve Tissue Proteins, Protein Structure, Tertiary, Nuclear Magnetic Resonance, Biomolecular, Amino Acid Motifs, Fluorescence Resonance Energy Transfer, SNARE Proteins, Synaptosomal-Associated Protein 25, Syntaxin 1, Vesicle-Associated Membrane Protein 2, Rats, Munc18 Proteins
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