Document Type

Article

Publication Date

5-22-2007

Publication Title

Proceedings of the National Academy of Sciences of the United States of America

Department

Geisel School of Medicine

Abstract

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.

DOI

10.1073/pnas.0702290104

Original Citation

Collins KM, Wickner WT. Trans-SNARE complex assembly and yeast vacuole membrane fusion. Proc Natl Acad Sci U S A. 2007 May 22;104(21):8755-60. doi: 10.1073/pnas.0702290104. Epub 2007 May 14. PMID: 17502611; PMCID: PMC1885575.

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