ArticleNature communications2024
Differential SNARE chaperoning by Munc13-1 and Munc18-1 dictates fusion pore fate at the release site.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Selective, genetically induced increase in synaptic vesicle priming.Science advances · 2026Article
- Integrated multiomics profiling of amniotic fluid exosomes reveals dysregulated lipid and protein signatures in fetal 22q11.2 deletion syndrome.Human genomics · 2026Article
- The MO25 protein Pmo25 functions in contractile ring stability and Sid2 localization during cytokinesis.iScience · 2026Article
- The activation of glial cells in the medulla visceral zone impairs synaptic plasticity and promotes inflammation and immune disorders in sepsis.Translational neuroscience · 2026Article
- Spatiotemporal patterns of gene expression changes in the mouse dentate gyrus following entorhinal denervation.Frontiers in molecular neuroscience · 2026Article
- Fusion Pores as Regulators of Quantal Size and Cellular Physiology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- The Ync13-Rga7-Rng10 complex selectively coordinates secretory vesicle trafficking and secondary septum formation during cytokinesis.PLoS biology · 2025Article
- Roles of the MO25 protein Pmo25 in contractile-ring stability and localization of the NDR kinase Sid2 during cytokinesis.bioRxiv : the preprint server for biology · 2025Article
- Two successive oligomeric Munc13 assemblies scaffold vesicle docking and SNARE assembly to support neurotransmitter release.Nature communications · 2025Article
- Spatial control of secretory vesicle targeting by the Ync13-Rga7-Rng10 complex during cytokinesis.bioRxiv : the preprint server for biology · 2025Article
- PROTON ATPASE TRANSLOCATION CONTROL 1-mediated HPNAS nexus · 2025Article
- Neural Excitatory/Inhibitory Imbalance in Motor Aging: From Genetic Mechanisms to Therapeutic Challenges.Biology · 2025Review
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Authors and funding
8 authors.
Funding
Abstract
The regulated release of chemical messengers is crucial for cell-to-cell communication; abnormalities in which impact coordinated human body function. During vesicular secretion, multiple SNARE complexes assemble at the release site, leading to fusion pore opening. How membrane fusion regulators act on heterogeneous SNARE populations to assemble fusion pores in a timely and synchronized manner, is unknown. Here, we demonstrate the role of SNARE chaperones Munc13-1 and Munc18-1 in rescuing individual nascent fusion pores from their diacylglycerol lipid-mediated inhibitory states. At the onset of membrane fusion, Munc13-1 clusters multiple SNARE complexes at the release site and synchronizes release events, while Munc18-1 stoichiometrically interacts with trans-SNARE complexes to enhance N- to C-terminal zippering. When both Munc proteins are present simultaneously, they differentially access dynamic trans-SNARE complexes to regulate pore properties. Overall, Munc proteins' direct action on fusion pore assembly indicates their role in controlling quantal size during vesicular secretion.
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