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Article

Conformational regulation of SNARE assembly and disassembly in vivo.

The Journal of biological chemistry - 15 Mar 2002

Munson Mary, Hughson Frederick M

Abstract excerpt

SNAP receptor (SNARE) proteins function in intracellular trafficking by forming complexes that bridge vesicle and target membranes prior to fusion. Biochemical studies indicate that the entry of certain SNARE proteins into complexes is inhibited by intramolecular interactions that generate a closed conformation. For example, an essential N-terminal regulatory domain of the yeast plasma membrane SNARE Sso1p...

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Identifiers

PMID: 11777922
DOI: 10.1074/jbc.M111729200

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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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Conformational regulation of SNARE assembly and disassembly in vivo.PMID 11777922Read ↗

Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion.Semantic proximity Read ↗

Binding interactions control SNARE specificity in vivo.Semantic proximity Read ↗

Characterization of temperature-sensitive mutations in the yeast syntaxin 1 homologues Sso1p and Sso2p, and evidence of a distinct function for Sso1p in sporulation.Semantic proximity Read ↗

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

The conserved C-terminus of Sss1p is required to maintain the endoplasmic reticulum permeability barrier.Semantic proximity Read ↗

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

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

Functional analysis of phosphorylation on Saccharomyces cerevisiae syntaxin 1 homologues Sso1p and Sso2p.Semantic proximity Read ↗

A random mutagenesis approach to isolate dominant-negative yeast sec1 mutants reveals a functional role for domain 3a in yeast and mammalian Sec1/Munc18 proteins.Semantic proximity Read ↗

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

Exocytosis requires asymmetry in the central layer of the SNARE complex.Semantic proximity Read ↗

Analysis of SEC9 suppression reveals a relationship of SNARE function to cell physiology.Semantic proximity Read ↗

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