ArticleMolecular biology of the cell2005
Munc18-1 regulates early and late stages of exocytosis via syntaxin-independent protein interactions.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 66 citations in OpenAlex.
- Fusion Pores as Regulators of Quantal Size and Cellular Physiology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- The trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosis.Nature communications · 2015Article
- Asynchronous GABA Release Is a Key Determinant of Tonic Inhibition and Controls Neuronal Excitability: A Study in the Synapsin II-/- Mouse.Cerebral cortex (New York, N.Y. : 1991) · 2015Article
- Differential interaction of tomosyn with syntaxin and SNAP25 depends on domains in the WD40 β-propeller core and determines its inhibitory activity.The Journal of biological chemistry · 2014Article
- Rab-3 and unc-18 interactions in alcohol sensitivity are distinct from synaptic transmission.PloS one · 2013Article
- Syntaxin binding protein 1 is not required for allergic inflammation via IgE-mediated mast cell activation.PloS one · 2013Article
- Munc18-1, exocytotic fusion pore regulation and local membrane anisotropy.Communicative & integrative biology · 2012Article
- A computational analysis framework for molecular cell dynamics: case-study of exocytosis.PloS one · 2012Article
- Copy number variants and infantile spasms: evidence for abnormalities in ventral forebrain development and pathways of synaptic function.European journal of human genetics : EJHG · 2011Article
- Munc18-1 tuning of vesicle merger and fusion pore properties.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Structure-function study of mammalian Munc18-1 and C. elegans UNC-18 implicates domain 3b in the regulation of exocytosis.PloS one · 2011Article
- Syntaxin N-terminal peptide motif is an initiation factor for the assembly of the SNARE-Sec1/Munc18 membrane fusion complex.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Yeast Sec1p functions before and after vesicle docking.Molecular biology of the cell · 2009Article
- UNC-18 modulates ethanol sensitivity in Caenorhabditis elegans.Molecular biology of the cell · 2009Article
- X11 proteins regulate the translocation of amyloid beta-protein precursor (APP) into detergent-resistant membrane and suppress the amyloidogenic cleavage of APP by beta-site-cleaving enzyme in brain.The Journal of biological chemistry · 2008Article
- Munc18a scaffolds SNARE assembly to promote membrane fusion.Molecular biology of the cell · 2008Article
- Article
- UNC-18 promotes both the anterograde trafficking and synaptic function of syntaxin.Molecular biology of the cell · 2008Article
- Munc-18-1 regulates the initial release rate of exocytosis.Biophysical journal · 2008Article
- Munc18-1: sequential interactions with the fusion machinery stimulate vesicle docking and priming.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sec1/Munc18 (SM) proteins are involved in various intracellular membrane trafficking steps. Many SM proteins bind to appropriate syntaxin homologues involved in these steps, suggesting that SM proteins function as syntaxin chaperones. Organisms with mutations in SM genes, however, exhibit defects in either early (docking) or late (fusion) stages of exocytosis, implying that SM proteins may have multiple functions. To gain insight into the role of SM proteins, we introduced mutations modeled on those identified in Caenorhabditis elegans, Drosophila melanogaster, and Saccharomyces cerevisiae into mammalian Munc18-1. As expected, several mutants exhibited reduced binding to syntaxin1A. However, three mutants displayed wild-type syntaxin binding affinities, indicating syntaxin-independent defects. Expression of these mutants in chromaffin cells either increased the rate and extent of exocytosis or altered the kinetics of individual release events. This latter effect was associated with a reduced Mint binding affinity in one mutant, implying a potential mechanism for the observed alteration in release kinetics. Furthermore, this phenotype persisted when the mutation was combined with a second mutation that greatly reduced syntaxin binding affinity. These results clarify the data on the function of SM proteins in mutant organisms and indicate that Munc18-1 controls multiple stages of exocytosis via both syntaxin-dependent and -independent protein interactions.
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