scholarly journals Lipid Rafts, Sphingolipids, and Ergosterol in Yeast Vacuole Fusion and Maturation

2020 ◽  
Vol 8 ◽  
Author(s):  
Logan R. Hurst ◽  
Rutilio A. Fratti
Keyword(s):  
Lipid Rafts ◽  
Yeast Vacuole ◽  
Vacuole Fusion

scholarly journals Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion

2007 ◽  
Vol 26 (24) ◽  
pp. 4935-4945 ◽  
Author(s):  
Youngsoo Jun ◽  
Hao Xu ◽  
Naomi Thorngren ◽  
William Wickner
Keyword(s):  
Yeast Vacuole ◽  
Vacuole Fusion

scholarly journals Copper blocks V‐ATPase activity and SNARE complex formation to inhibit yeast vacuole fusion

Traffic ◽  
2019 ◽  
Vol 20 (11) ◽  
pp. 841-850 ◽  
Author(s):  
Gregory E. Miner ◽  
Katherine D. Sullivan ◽  
Chi Zhang ◽  
Logan R. Hurst ◽  
Matthew L. Starr ◽  
...  
Keyword(s):  
Complex Formation ◽  
Atpase Activity ◽  
Snare Complex ◽  
Yeast Vacuole ◽  
Vacuole Fusion ◽  
Snare Complex Formation

Author response for "Copper blocks V‐ATPase activity and SNARE complex formation to inhibit yeast vacuole fusion"

2019 ◽  
Author(s):  
Gregory E. Miner ◽  
Katherine D. Sullivan ◽  
Chi Zhang ◽  
Logan R. Hurst ◽  
Matthew L. Starr ◽  
...  
Keyword(s):  
Complex Formation ◽  
Atpase Activity ◽  
Snare Complex ◽  
Author Response ◽  
Yeast Vacuole ◽  
Vacuole Fusion ◽  
Snare Complex Formation

Palmitoylation determines the function of Yeast vacuole fusion factor Vac8.

2007 ◽  
Vol 2007 (Spring) ◽  
Author(s):  
Kanagaraj Subramanian ◽  
Lars Dietrich ◽  
Haitong Hou ◽  
Christian Ungermann
Keyword(s):  
Yeast Vacuole ◽  
Vacuole Fusion

scholarly journals Improved reconstitution of yeast vacuole fusion with physiological SNARE concentrations reveals an asymmetric Rab(GTP) requirement

2016 ◽  
Vol 27 (16) ◽  
pp. 2590-2597 ◽  
Author(s):  
Michael Zick ◽  
William Wickner
Keyword(s):  
Acyl Chain ◽  
Fatty Acyl ◽  
Fatty Acyl Chain ◽  
Rab Gtpase ◽  
Lower Phase ◽  
Yeast Vacuole ◽  
Vacuole Fusion ◽  
In Vitro Reconstitution

In vitro reconstitution of homotypic yeast vacuole fusion from purified components enables detailed study of membrane fusion mechanisms. Current reconstitutions have yet to faithfully replicate the fusion process in at least three respects: 1) The density of SNARE proteins required for fusion in vitro is substantially higher than on the organelle. 2) Substantial lysis accompanies reconstituted fusion. 3) The Rab GTPase Ypt7 is essential in vivo but often dispensable in vitro. Here we report that changes in fatty acyl chain composition dramatically lower the density of SNAREs that are required for fusion. By providing more physiological lipids with a lower phase transition temperature, we achieved efficient fusion with SNARE concentrations as low as on the native organelle. Although fused proteoliposomes became unstable at elevated SNARE concentrations, releasing their content after fusion had occurred, reconstituted proteoliposomes with substantially reduced SNARE concentrations fused without concomitant lysis. The Rab GTPase Ypt7 is essential on both membranes for proteoliposome fusion to occur at these SNARE concentrations. Strikingly, it was only critical for Ypt7 to be GTP loaded on membranes bearing the R-SNARE Nyv1, whereas the bound nucleotide of Ypt7 was irrelevant on membranes bearing the Q-SNAREs Vam3 and Vti1.

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

2000 ◽  
Vol 148 (6) ◽  
pp. 1231-1238 ◽  
Author(s):  
Albert Price ◽  
Darren Seals ◽  
William Wickner ◽  
Christian Ungermann
Keyword(s):  
Binding Protein ◽  
Snare Complex ◽  
Guanosine Triphosphate ◽  
Yeast Vacuole ◽  
Vacuole Fusion ◽  
Direct Association ◽  
Rab Family

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.

scholarly journals A lifeline for lipid rafts?

2013 ◽  
Vol 202 (1) ◽  
pp. 3-3 ◽  
Author(s):  
Mitch Leslie
Keyword(s):  
Lipid Rafts ◽  
Vacuole Membrane ◽  
Yeast Vacuole

Study finds raft-like domains in yeast vacuole membrane.

Sign in / Sign up

Export Citation Format

Share Document