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© The Rockefeller University Press, 0021-9525/2000//1231 $5.00
The Journal of Cell Biology, Volume 148, Number 6, , 2000 1231-1238

Original Article

The Docking Stage of Yeast Vacuole Fusion Requires the Transfer of Proteins from a Cis-Snare Complex to a Rab/Ypt Protein



Albert Pricea, Darren Sealsa, William Wicknera, and Christian Ungermanna

a Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755-3844
Department of Biochemistry, Dartmouth Medical School, 7200 Vail Building, Hanover, NH 03755-3844.(603) 650-1353(603) 650-1701

The homotypic fusion of yeast vacuoles requires Sec18p (NSF)-driven priming to allow vacuole docking, but the mechanism that links priming and docking is unknown. We find that a large multisubunit protein called the Vam2/6p complex is bound to cis-paired SNAP receptors (SNAREs) on isolated vacuoles. This association of the Vam2/6p complex with the cis-SNARE complex is disrupted during priming. The Vam2/6p complex then binds to Ypt7p, a guanosine triphosphate binding protein of the Rab family, to initiate productive contact between vacuoles. Thus, cis-SNARE complexes can contain Rab/Ypt effectors, and these effectors can be mobilized by NSF/Sec18p-driven priming, allowing their direct association with a Rab/Ypt protein to activate docking.

Key Words: Vps39/Vam6p • Vps41/Vam2p • Ypt7p • priming • Rab/Ypt effector

© 2000 The Rockefeller University Press

A. Price's present address is Department of Cell Biology, Sterling Hall of Medicine, C441, Yale University School of Medicine, 333 Cedar Street, P.O. Box 208002, New Haven, CT 06520-8002.

C. Ungermann's present address is Biochemie-Zentrum Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.

The website for this laboratory is located at http://www.dartmouth.edu/~wickner

Abbreviations used in this paper: GST, glutathione S-transferase; HA, hemagglutinin; LMA1, low molecular weight activity #1; NSF, N-ethylmaleimide sensitive factor; SNARE, SNAP receptor; TRAPP, transport protein particle.


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J. Cell Biol. 2000 148: 1-2. [Full Text] [PDF]





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