trans-SNARE complex assembly and yeast vacuole membrane fusion

cis-SNARE complexes (anchored in one membrane) are disassembled by Sec17p (α-SNAP) and Sec18p (NSF), permitting the unpaired SNAREs to assemble in trans. We now report a direct assay of trans-SNARE complex formation during yeast vacuole docking. SNARE complex assembly and fusion is promoted by high...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2007-05, Vol.104 (21), p.8755-8760
Main Authors: Collins, Kevin M, Wickner, William T
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antibodies
Biochemistry
Biological Sciences
Cellular biology
cis-SNARE proteins
cytochemistry
Error rates
fungal proteins
Intracellular Membranes - metabolism
Kinases
Ligands
Lipid Metabolism
Lipids
Membrane Fusion
Membranes
Molecular Sequence Data
Phosphatidylinositols
Protein Binding
protein sorting
Proteins
Qa-SNARE Proteins - chemistry
Qa-SNARE Proteins - genetics
Qa-SNARE Proteins - metabolism
R SNARE proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
SNARE proteins
SNARE Proteins - genetics
SNARE Proteins - metabolism
tonoplast
trans-SNARE proteins
Vacuoles
Vacuoles - metabolism
Yeast
Yeasts
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Summary:cis-SNARE complexes (anchored in one membrane) are disassembled by Sec17p (α-SNAP) and Sec18p (NSF), permitting the unpaired SNAREs to assemble in trans. We now report a direct assay of trans-SNARE complex formation during yeast vacuole docking. SNARE complex assembly and fusion is promoted by high concentrations of the SNARE Vam7p or Nyv1p or by addition of HOPS (homotypic fusion and vacuole protein sorting), a Ypt7p (Rab)-effector complex with a Sec1/Munc18-family subunit. Inhibitors that target Ypt7p, HOPS, or key regulatory lipids prevent trans-SNARE complex assembly and ensuing fusion. Strikingly, the lipid ligand MED (myristoylated alanine-rich C kinase substrate effector domain) or elevated concentrations of Sec17p, which can displace HOPS from SNARE complexes, permit full trans-SNARE pairing but block fusion. These findings suggest that efficient fusion requires trans-SNARE complex associations with factors such as HOPS and subsequent regulated lipid rearrangements.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0702290104