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Article

Positively charged amino acids at the SNAP-25 C terminus determine fusion rates, fusion pore properties, and energetics of tight SNARE complex zippering.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 18 Feb 2015

Fang Qinghua, Zhao Ying, Herbst Adam Drew, Kim Brian N, Lindau Manfred

Abstract excerpt

SNAP-25 is a Q-SNARE protein mediating exocytosis of neurosecretory vesicles including chromaffin granules. Previous results with a SNAP-25 construct lacking the nine C terminal residues (SNAP-25Δ9) showed changed fusion pore properties (Fang et al., 2008), suggesting a model for fusion pore mechanics that couple C terminal zipping of the SNARE complex to the opening of the fusion pore. The deleted fragment...

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Identifiers

PMID: 25698757
DOI: 10.1523/JNEUROSCI.2905-14.2015
PMCID: PMC4331636

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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