Article
- The EMBO Journal (2006) 25, 1579 - 1589
- doi:10.1038/sj.emboj.7601051
Published online: 6 April 2006
Subject Category:
Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p
Christopher Stroupe, Kevin M Collins, Rutilio A Fratti and William Wickner
- Department of Biochemistry, Dartmouth Medical School, Hanover, NH, USA
Correspondence to:
William Wickner, Department of Biochemistry, Dartmouth Medical School, 7200 Vail Building, Room 425 Remsen, Hanover, NH 03755-3844, USA. Tel.: +1 603 650 1701; Fax: +1 603 650 1353; E-mail: william.wickner@dartmouth.edu, URL: http://www.dartmouth.edu/~wickner
Received 26 July 2005; Accepted 27 February 2006
Abstract
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.
Keywords:
- HOPS,
- phosphoinositide,
- PX,
- Rab,
- SNARE
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