trans-SNARE complex assembly and yeast vacuole membrane fusion

Kevin M. Collins, William T. Wickner

Research output: Contribution to journalArticle

65 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)8755-8760
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume104
Issue number21
DOIs
StatePublished - May 22 2007

Keywords

  • Homotypic fusion and vacuole protein sorting
  • Rab/Ypt

ASJC Scopus subject areas

  • General

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