ArticleBiophysical journal2013
Allosteric control of syntaxin 1a by Munc18-1: characterization of the open and closed conformations of syntaxin.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Syntaxin-3 Regulates Tight Junction Assembly in Human Retinal Pigment Epithelium.Cell biochemistry and function · 2026Article
- 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
- Syntaxin 3B Mediates Light-Dependent Interactions with STXBP1 and Arrestin 4: Distinct Roles in Rods and Cones.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission.Nature communications · 2025Article
- Insight into molecular and neural mechanisms of general anesthesia from the invertebrate modelZoological research · 2025Review
- Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission.bioRxiv : the preprint server for biology · 2025Article
- Review
- The role of syntaxins in retinal function and health.Frontiers in cellular neuroscience · 2024Review
- Investigating Native Metal Ion Binding Sites in Mammalian Histidine-Rich Glycoprotein.Journal of the American Chemical Society · 2023Article
- Presynaptic Short-Term Plasticity Persists in the Absence of PKC Phosphorylation of Munc18-1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Reexamination of N-terminal domains of syntaxin-1 in vesicle fusion from central murine synapses.eLife · 2021Article
- Viewing rare conformations of the βProceedings of the National Academy of Sciences of the United States of America · 2020Article
- KPlant physiology · 2019Article
- Hybrid Refinement of Heterogeneous Conformational Ensembles Using Spectroscopic Data.The journal of physical chemistry letters · 2019Article
- Syntaxin clusters at secretory granules in a munc18-bound conformation.Molecular biology of the cell · 2018Article
- A molecular mechanism for calcium-mediated synaptotagmin-triggered exocytosis.Nature structural & molecular biology · 2018Article
- Solution NMR of SNAREs, complexin and α-synuclein in association with membrane-mimetics.Progress in nuclear magnetic resonance spectroscopy · 2018Review
- Sparse Labeling PELDOR Spectroscopy on Multimeric Mechanosensitive Membrane Channels.Biophysical journal · 2017Article
- Asymmetric Phosphatidylethanolamine Distribution Controls Fusion Pore Lifetime and Probability.Biophysical journal · 2017Article
- TRIM5α SPRY/coiled-coil interactions optimize avid retroviral capsid recognition.PLoS pathogens · 2017Article
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Authors and funding
2 authors.
Funding
Abstract
Syntaxin 1a is a plasma membrane soluble N-ethylmaleimide-sensitive factor attachment receptor protein (SNARE) that contains an H3 domain (SNARE motif) and a regulatory Habc domain. These regions associate to produce a closed state, which is generally thought to suppress assembly of syntaxin into the SNARE complex. However, the molecular nature of the closed and open states of syntaxin is not well defined. Here, we use electron paramagnetic resonance spectroscopy to characterize conformational exchange in syntaxin. The data indicate that the H3 segment is in equilibrium between ordered and disordered states that have significant populations. In solution, the central region of the H3 segment is positioned close to the Habc domain and the configuration of syntaxin 1a is dominated by a closed state. However, an open state is enhanced in full-length membrane reconstituted syntaxin. Munc18-1 binding alters the equilibrium along H3 to favor the ordered, folded state. Munc18 also suppresses the minor open population and narrows the distance distributions between H3 and Habc. The allosteric control exhibited by Munc18 on the H3 segment and the suppression of the minor open component may both play a role in regulating membrane fusion by controlling the assembly of syntaxin into the SNARE complex.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.