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Article

Targeted mutations in the syntaxin H3 domain specifically disrupt SNARE complex function in synaptic transmission.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 1 Dec 2001

Fergestad T, Wu M N, Schulze K L, Lloyd T E, Bellen H J, Broadie K

Abstract excerpt

The cytoplasmic H3 helical domain of syntaxin is implicated in numerous protein-protein interactions required for the assembly and stability of the SNARE complex mediating vesicular fusion at the synapse. Two specific hydrophobic residues (Ala-240, Val-244) in H3 layers 4 and 5 of mammalian syntaxin1A have been suggested to be involved in SNARE complex stability and required for the inhibitory effects of syntaxin...

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Identifiers

PMID: 11717347
PMCID: PMC6763887

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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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Targeted mutations in the syntaxin H3 domain specifically disrupt SNARE complex function in synaptic transmission.PMID 11717347Read ↗

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