ArticleMolecular biology of the cell2018
Syntaxin clusters at secretory granules in a munc18-bound conformation.
Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 14 citations in OpenAlex.
- Functional differences of Munc18 isoforms reflect their affinities for the exocytosis site.Cellular and molecular life sciences : CMLS · 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
- 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
- Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission.Nature communications · 2025Article
- Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission.bioRxiv : the preprint server for biology · 2025Article
- Neuronal Network Inactivity Potentiates Neuropeptide Release from Mouse Cortical Neurons.eNeuro · 2025Article
- Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022Review
- Secretory granule exocytosis and its amplification by cAMP in pancreatic β-cells.Diabetology international · 2022Review
- VAMP2 and synaptotagmin mobility in chromaffin granule membranes: implications for regulated exocytosis.Molecular biology of the cell · 2022Article
- SNARE proteins: zip codes in vesicle targeting?The Biochemical journal · 2022Review
- Munc18-dependent and -independent clustering of syntaxin in the plasma membrane of cultured endocrine cells.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Isolation and Proteomics of the Insulin Secretory Granule.Metabolites · 2021Review
- Conventional and Unconventional Mechanisms by which Exocytosis Proteins Oversee β-cell Function and Protection.International journal of molecular sciences · 2021Review
- Molecular Evolution and Characterization of Fish Stathmin Genes.Animals : an open access journal from MDPI · 2020Article
- Simultaneous Release of Multiple Vesicles from Rods Involves Synaptic Ribbons and Syntaxin 3B.Biophysical journal · 2020Article
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Syntaxin (stx)-1 is an integral plasma membrane protein that is crucial for two distinct steps of regulated exocytosis, docking of secretory granules at the plasma membrane and membrane fusion. During docking, stx1 clusters at the granule docking site, together with the S/M protein munc18. Here we determined features of stx1 that contribute to its clustering at granules. In live insulin-secreting cells, stx1 and stx3 (but not stx4 or stx11) accumulated at docked granules, and stx1 (but not stx4) rescued docking in cells expressing botulinum neurotoxin-C. Using a series of stx1 deletion mutants and stx1/4 chimeras, we found that all four helical domains (Ha, Hb, Hc, SNARE) and the short N-terminal peptide contribute to recruitment to granules. However, only the Hc domain confers specificity, and it must be derived from stx1 for recruitment to occur. Point mutations in the Hc or the N-terminal peptide designed to interfere with binding to munc18-1 prevent stx1 from clustering at granules, and a mutant munc18 deficient in binding to stx1 does not cluster at granules. We conclude that stx1 is recruited to the docking site in a munc18-1-bound conformation, providing a rationale for the requirement for both proteins for granule docking.
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