The Journal of Cell Biology
Geisel School of Medicine
Ca2+ transients trigger many SNARE-dependent membrane fusion events. The homotypic fusion of yeast vacuoles occurs after a release of lumenal Ca2+. Here, we show that trans-SNARE interactions promote the release of Ca2+ from the vacuole lumen. Ypt7p-GTP, the Sec1p/Munc18-protein Vps33p, and Rho GTPases, all of which function during docking, are required for Ca2+ release. Inhibitors of SNARE function prevent Ca2+ release. Recombinant Vam7p, a soluble Q-SNARE, stimulates Ca2+ release. Vacuoles lacking either of two complementary SNAREs, Vam3p or Nyv1p, fail to release Ca2+ upon tethering. Mixing these two vacuole populations together allows Vam3p and Nyv1p to interact in trans and rescues Ca2+ release. Sec17/18p promote sustained Ca2+ release by recycling SNAREs (and perhaps other limiting factors), but are not required at the release step itself. We conclude that trans-SNARE assembly events during docking promote Ca2+ release from the vacuole lumen.
Merz AJ, Wickner WT. Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen. J Cell Biol. 2004 Jan 19;164(2):195-206. doi: 10.1083/jcb.200310105. PMID: 14734531; PMCID: PMC2172329.
Dartmouth Digital Commons Citation
Merz, Alexey J. and Wickner, William T., "Trans-SNARE Interactions Elicit Ca2+ Efflux from the Yeast Vacuole Lumen" (2004). Dartmouth Scholarship. 1451.