ArticlePloS one2015
Differential Effects of Munc18s on Multiple Degranulation-Relevant Trans-SNARE Complexes.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Dissecting SNARE-Mediated Exocytosis in RBL-2H3 Mast Cells.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Exocytic machineries differentially control mediator release from allergen-triggered RBL-2H3 cells.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2023Article
- SNARE Proteins Mediate α-Synuclein Secretion via Multiple Vesicular Pathways.Molecular neurobiology · 2022Article
- TNF Production in Activated RBL-2H3 Cells Requires Munc13-4.Inflammation · 2020Article
- Review
- Diverse exocytic pathways for mast cell mediators.Biochemical Society transactions · 2018Review
- PKC-dependent phosphorylation of Munc18a at Ser313 in activated RBL-2H3 cells.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2018Article
- Munc18a clusters SNARE-bearing liposomes prior toThe Biochemical journal · 2017Article
- Opposing roles for SNAP23 in secretion in exocrine and endocrine pancreatic cells.The Journal of cell biology · 2016Article
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Authors and funding
3 authors.
Funding
Abstract
Mast cell exocytosis, which includes compound degranulation and vesicle-associated piecemeal degranulation, requires multiple Q- and R- SNAREs. It is not clear how these SNAREs pair to form functional trans-SNARE complexes and how these trans-SNARE complexes are selectively regulated for fusion. Here we undertake a comprehensive examination of the capacity of two Q-SNARE subcomplexes (syntaxin3/SNAP-23 and syntaxin4/SNAP-23) to form fusogenic trans-SNARE complexes with each of the four granule-borne R-SNAREs (VAMP2, 3, 7, 8). We report the identification of at least six distinct trans-SNARE complexes under enhanced tethering conditions: i) VAMP2/syntaxin3/SNAP-23, ii) VAMP2/syntaxin4/SNAP-23, iii) VAMP3/syntaxin3/SNAP-23, iv) VAMP3/syntaxin4/SNAP-23, v) VAMP8/syntaxin3/SNAP-23, and vi) VAMP8/syntaxin4/SNAP-23. We show for the first time that Munc18a operates synergistically with SNAP-23-based non-neuronal SNARE complexes (i to iv) in lipid mixing, in contrast to Munc18b and c, which exhibit no positive effect on any SNARE combination tested. Pre-incubation with Munc18a renders the SNARE-dependent fusion reactions insensitive to the otherwise inhibitory R-SNARE cytoplasmic domains, suggesting a protective role of Munc18a for its cognate SNAREs. Our findings substantiate the recently discovered but unexpected requirement for Munc18a in mast cell exocytosis, and implicate post-translational modifications in Munc18b/c activation.
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