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Article

Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification.

The Journal of biological chemistry - 18 May 2007

Fratti Rutilio A, Collins Kevin M, Hickey Christopher M, Wickner William

Abstract excerpt

SNARE proteins form bundles of four alpha-helical SNARE domains with conserved polar amino acids, 3Q and 1R, at the "0-layer" of the bundle. Previous studies have confirmed the importance of 3Q.1R for fusion but have not shown whether it regulates SNARE complex assembly or the downstream functions of assembled SNAREs. Yeast vacuole fusion requires regulatory lipids (ergosterol, phosphoinositides, and...

Topics

Chlorpromazine
Dopamine Antagonists
Estrenes
Lipid Bilayers
Membrane Fusion
Multiprotein Complexes
Mutation
Phosphodiesterase Inhibitors
Pyrrolidinones
SNARE Proteins
Saccharomyces cerevisiae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Saccharomyces cerevisiae Proteins

Type C Phospholipases

Vacuoles

Source

Identifiers

PMID: 17400548
DOI: 10.1074/jbc.M700971200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification.PMID 17400548Read ↗

Ykt6 functionally overlaps with vacuolar and exocytic R-SNAREs in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

Testing the 3Q:1R “Rule”: Mutational Analysis of the Ionic “Zero” Layer in the Yeast Exocytic SNARE Complex Reveals No Requirement for ArginineSemantic proximity Read ↗

The lipid composition and physical properties of the yeast vacuole affect the hemifusion-fusion transition.Semantic proximity Read ↗

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

Functional analysis of conserved structural elements in yeast syntaxin Vam3p.Semantic proximity Read ↗

Identification of functionally interacting SNAREs by using complementary substitutions in the conserved '0' layer.Semantic proximity Read ↗

Self-interaction of a SNARE transmembrane domain promotes the hemifusion-to-fusion transition.Semantic proximity Read ↗

The v-ATPase V0 subunit a1 is required for a late step in synaptic vesicle exocytosis in Drosophila.Semantic proximity Read ↗

SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions.Semantic proximity Read ↗

The SM protein Vps33 and the t-SNARE H(abc) domain promote fusion pore opening.Semantic proximity Read ↗

Double-Transmembrane Domain of SNAREs Decelerates the Fusion by Increasing the Protein-Lipid Mismatch.Semantic proximity Read ↗

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

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