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Article

Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly.

Neuron - 1 Aug 1998

Littleton J T, Chapman E R, Kreber R, Garment M B, Carlson S D, Ganetzky B

Abstract excerpt

The neuronal SNARE complex is formed via the interaction of synaptobrevin with syntaxin and SNAP-25. Purified SNARE proteins assemble spontaneously, while disassembly requires the ATPase NSF. Cycles of assembly and disassembly have been proposed to drive lipid bilayer fusion. However, this hypothesis remains to be tested in vivo. We have isolated a Drosophila temperature-sensitive paralytic mutation in syntaxin...

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Source

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PMID: 9728921
DOI: 10.1016/s0896-6273(00)80549-8

Genes

NSF

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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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Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly.PMID 9728921Read ↗

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The sodium leak channel NALCN is regulated by neuronal SNARE complex proteinsSemantic proximity Read ↗

NSF-mediated disassembly of on- and off-pathway SNARE complexes and inhibition by complexin.Semantic proximity Read ↗

Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis.Semantic proximity Read ↗

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

Synaptic physiology and ultrastructure in comatose mutants define an in vivo role for NSF in neurotransmitter release.Semantic proximity Read ↗

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