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Article

The trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosis.

Nature communications - 17 Nov 2015

Shen Chong, Rathore Shailendra S, Yu Haijia, Gulbranson Daniel R, Hua Rui, Zhang Chen, Schoppa Nathan E, Shen Jingshi

Abstract excerpt

The fusion of neurotransmitter-filled synaptic vesicles with the plasma membrane requires two classes of molecules-SNAP receptor (SNARE) and Sec1/Munc18 (SM) protein. Reconstitution studies suggest that the SM protein Munc18-1 promotes the zippering of trans-SNARE complexes and accelerates the kinetics of SNARE-dependent membrane fusion. However, the physiological role of this trans-SNARE-regulating function in...

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Source

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Identifiers

PMID: 26572858
DOI: 10.1038/ncomms9852
PMCID: PMC4668942

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosis.PMID 26572858Read ↗

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Munc18-1 regulates early and late stages of exocytosis via syntaxin-independent protein interactions.Semantic proximity Read ↗

The functions of Munc18-1 in regulated exocytosis.Semantic proximity Read ↗

Control of fusion pore dynamics during exocytosis by Munc18.Semantic proximity Read ↗

Munc18-1 tuning of vesicle merger and fusion pore properties.Semantic proximity Read ↗

Conformational switch of syntaxin-1 controls synaptic vesicle fusion.Semantic proximity Read ↗

Mso1p regulates membrane fusion through interactions with the putative N-peptide-binding area in Sec1p domain 1.Semantic proximity Read ↗

Syntaxin N-terminal peptide motif is an initiation factor for the assembly of the SNARE-Sec1/Munc18 membrane fusion complex.Semantic proximity Read ↗

Binding of UNC-18 to the N-terminus of syntaxin is essential for neurotransmission in Caenorhabditis elegans.Semantic proximity Read ↗

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