The Journal of Cell Biology
Geisel School of Medicine
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.
Price A, Seals D, Wickner W, Ungermann C. The docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt protein. J Cell Biol. 2000 Mar 20;148(6):1231-8. doi: 10.1083/jcb.148.6.1231. PMID: 10725336; PMCID: PMC2174311.
Dartmouth Digital Commons Citation
Price, Albert; Seals, Darren; Wickner, William; and Ungermann, Christian, "The Docking Stage of Yeast Vacuole Fusion Requires the Transfer of Proteins from a Cis-Snare Complex to a Rab/Ypt Protein" (2000). Dartmouth Scholarship. 2329.