Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p

Christopher Stroupe, Kevin M. Collins, Rutilio A. Fratti, William Wickner

Research output: Contribution to journalArticle

171 Scopus citations


Coupling of Rab GTPase activation and SNARE complex assembly during membrane fusion is poorly understood. The homotypic fusion and vacuole protein sorting (HOPS) complex links these two processes: it is an effector for the vacuolar Rab GTPase Ypt7p and is required for vacuolar SNARE complex assembly. We now report that pure, active HOPS complex binds phosphoinositides and the PX domain of the vacuolar SNARE protein Vam7p. These binding interactions support HOPS complex association with the vacuole and explain its enrichment at the same microdomains on docked vacuoles as phosphoinositides, Ypt7p, Vam7p, and the other SNARE proteins. Concentration of the HOPS complex at these microdomains may be a key factor for coupling Rab GTPase activation to SNARE complex assembly.

Original languageEnglish (US)
Pages (from-to)1579-1589
Number of pages11
JournalEMBO Journal
Issue number8
StatePublished - Apr 19 2006
Externally publishedYes



  • HOPS
  • PX
  • Phosphoinositide
  • Rab

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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