A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.
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Organelle acidification negatively regulates vacuole membrane fusion in vivo.The V-ATPase proteolipid cylinder promotes the lipid-mixing stage of SNARE-dependent fusion of yeast vacuoles.Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusionHOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusionPhosphatidic Acid Sequesters Sec18p from cis-SNARE Complexes to Inhibit PrimingHOPS proofreads the trans-SNARE complex for yeast vacuole fusionPurification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p.Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast.Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase.The yeast ATP-binding cassette (ABC) transporter Ycf1p enhances the recruitment of the soluble SNARE Vam7p to vacuoles for efficient membrane fusion.The Central Polybasic Region of the Soluble SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Vam7 Affects Binding to Phosphatidylinositol 3-Phosphate by the PX (Phox Homology) Domain.Yeast lipin 1 orthologue pah1p regulates vacuole homeostasis and membrane fusion.Diacylglycerol and its formation by phospholipase C regulate Rab- and SNARE-dependent yeast vacuole fusion.Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification.Differential Effects of Munc18s on Multiple Degranulation-Relevant Trans-SNARE ComplexesBem1p is a positive regulator of the homotypic fusion of yeast vacuoles.The yeast vacuolar Rab GTPase Ypt7p has an activity beyond membrane recruitment of the homotypic fusion and protein sorting-Class C Vps complexPhosphorylation of the effector complex HOPS by the vacuolar kinase Yck3p confers Rab nucleotide specificity for vacuole docking and fusion.Requirement for Golgi-localized PI(4)P in fusion of COPII vesicles with Golgi compartmentsHow and why intralumenal membrane fragments form during vacuolar lysosome fusion.Osmotic regulation of Rab-mediated organelle dockingDynamic association of the PI3P-interacting Mon1-Ccz1 GEF with vacuoles is controlled through its phosphorylation by the type 1 casein kinase Yck3.Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion.Sequential analysis of trans-SNARE formation in intracellular membrane fusionTracking of the dynamic localization of the Rab-specific HOPS subunits reveal their distinct interaction with Ypt7 and vacuoles.A lipid-anchored SNARE supports membrane fusionA distinct tethering step is vital for vacuole membrane fusion.The v-ATPase V0 subunit a1 is required for a late step in synaptic vesicle exocytosis in Drosophila.Homotypic fusion of early endosomes: SNAREs do not determine fusion specificityLegC3, an effector protein from Legionella pneumophila, inhibits homotypic yeast vacuole fusion in vivo and in vitroVibrio effector protein VopQ inhibits fusion of V-ATPase-containing membranes.Vacuolar SNARE protein transmembrane domains serve as nonspecific membrane anchors with unequal roles in lipid mixing.Trans-SNARE complex assembly and yeast vacuole membrane fusion.SNAREs support atlastin-mediated homotypic ER fusion in Saccharomyces cerevisiaeAssays of vacuole fusion resolve the stages of docking, lipid mixing, and content mixingExcess vacuolar SNAREs drive lysis and Rab bypass fusionRole of the V-ATPase in regulation of the vacuolar fission-fusion equilibriumSec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion.Transition from hemifusion to pore opening is rate limiting for vacuole membrane fusionThe vacuolar kinase Yck3 maintains organelle fragmentation by regulating the HOPS tethering complex.
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P2860
A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 08 July 2004
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.
@en
A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.
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A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.
@en
A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.
@nl
prefLabel
A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.
@en
A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.
@nl
P2093
P2860
P356
P1433
P1476
A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion
@en
P2093
Alexey J Merz
Naomi Thorngren
Rutilio A Fratti
William Wickner
P2860
P304
P356
10.1038/SJ.EMBOJ.7600286
P407
P577
2004-07-08T00:00:00Z