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Conformational Switch of Syntaxin-1 Controls Synaptic Vesicle Fusion
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During synaptic vesicle fusion, the soluble N -ethylmaleimide-sensitive factor–attachment protein receptor (SNARE) protein syntaxin-1 exhibits two conformations that both bind to Munc18-1: a “closed” conformation outside the SNARE complex and an “open” conformation in the SNARE complex. Although SNARE complexes containing open syntaxin-1 and Munc18-1 are essential for exocytosis, the function of closed syntaxin-1 is unknown. We generated knockin/knockout mice that expressed only open syntaxin-1B. Syntaxin-1B Open mice were viable but succumbed to generalized seizures at 2 to 3 months of age. Binding of Munc18-1 to syntaxin-1 was impaired in syntaxin-1B Open synapses, and the size of the readily releasable vesicle pool was decreased; however, the rate of synaptic vesicle fusion was dramatically enhanced. Thus, the closed conformation of syntaxin-1 gates the initiation of the synaptic vesicle fusion reaction, which is then mediated by SNARE-complex/Munc18-1 assemblies.
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“The MUN domain may act to open the ‘closed’ form of the SNARE protein syntaxin-1 (Gerber et al., 2008), thereby enabling syntaxin-1 to form SNARE complexes (Richmond et al., 2001; Ma et al., 2011).”
From The Presynaptic Active Zone (2012) · cites this paper as Gerber et al., 2008
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Metadata
- Authors
- Gerber, S. H., Rah, J.-C., Min, S.-W., Liu, X., de Wit, H., Dulubova, I., Meyer, A. C., Rizo, J., Arancillo, M., Hammer, R. E., Verhage, M., Rosenmund, C., & Südhof, T. C.
- Affiliations
- Baylor College of Medicine (US)
- Department of Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75390–9111, USA.
- Corresponding author
- Gerber, Stefan H.
- Rah, Jong-Cheol
- Min, Sang-Won
- Rosenmund, Christian
- ORCID
- Venue
- Science
- Published
- 2008-09-12
- Volume
- 321
- Issue
- 5895
- Pages
- 1507-1510
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3235364
- OpenAlex
- W2006897184
- Cited by
- 294
- References
- 23
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 7 · 2023: 15 · 2022: 9 · 2021: 13 · 2020: 16 · 2019: 12 · 2018: 15 · 2017: 15 · 2016: 15 · 2015: 18 · 2014: 28 · 2013: 22 · 2012: 24
- FWCI
- 10.95
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Amsterdam UMC (VU Amsterdam) - Institutional Repository (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Pure Amsterdam UMC (submittedVersion)
- VU Research Portal (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of Neurological Disorders and Stroke (NS 37200, R01NS037200, R01NS051262, NS051262)
- 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 › Extracellular vesicles in disease
- Keywords
- syntaxin-1, Munc18-1, SNARE complex, synaptic vesicle fusion, conformational switching, exocytosis, seizures, synaptic transmission
- MeSH terms
- Animals, Calcium, Epilepsy, Membrane Fusion, Mutation, Protein Conformation, Sucrose, Synapses, Synaptic Vesicles, Protein Structure, Tertiary, Mice, Knockout, Excitatory Postsynaptic Potentials, SNARE Proteins, Syntaxin 1, Mice, Munc18 Proteins
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