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Article

Syntaxin 1A drives fusion of large dense-core neurosecretory granules into a planar lipid bilayer.

Cell biochemistry and biophysics - 1 Jan 2004

McNally James M, Woodbury Dixon J, Lemos José R

Abstract excerpt

The SNARE complex, involved in vesicular trafficking and exocytosis, is composed of proteins in the vesicular membrane (v-SNAREs) that intertwine with proteins of the target membrane (t-SNAREs). Our results show that modified large dense-core neurosecretory granules (NSGs), isolated from the bovine neurohypophysis, spontaneously fuse with a planar lipid membrane containing only the t-SNARE syntaxin 1A. This...

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Source

Identifiers

PMID: 15371637
DOI: 10.1385/CBB:41:1:011

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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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Syntaxin 1A drives fusion of large dense-core neurosecretory granules into a planar lipid bilayer.PMID 15371637Read ↗

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

Syntaxin 1A regulation of weakly inactivating N-type Ca2+ channels.Semantic proximity Read ↗

Ca(2+)-independent syntaxin binding to the C(2)B effector region of synaptotagmin.Semantic proximity Read ↗

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Gβγ directly modulates vesicle fusion by competing with synaptotagmin for binding to neuronal SNARE proteins embedded in membranes.Semantic proximity Read ↗

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