Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen.
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Yeast translation elongation factor-1A binds vacuole-localized Rho1p to facilitate membrane integrity through F-actin remodeling.Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p.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.Membranes linked by trans-SNARE complexes require lipids prone to non-bilayer structure for progression to fusion.How and why intralumenal membrane fragments form during vacuolar lysosome fusion.Glutamate-induced exocytosis of glutamate from astrocytes.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.Mitofusins and the mitochondrial permeability transition: the potential downside of mitochondrial fusionAcidocalcisomes and the contractile vacuole complex are involved in osmoregulation in Trypanosoma cruzi.LegC3, an effector protein from Legionella pneumophila, inhibits homotypic yeast vacuole fusion in vivo and in vitroWhat are the roles of V-ATPases in membrane fusion?Vibrio effector protein VopQ inhibits fusion of V-ATPase-containing membranes.Acidic calcium stores of Saccharomyces cerevisiae.Membrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to small molecules and by lysis.Calcium: a fundamental regulator of intracellular membrane fusion?Assays 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 yeast vacuolar ABC transporter Ybt1p regulates membrane fusion through Ca2+ transport modulationThe lipid composition and physical properties of the yeast vacuole affect the hemifusion-fusion transition.Fusion proteins and select lipids cooperate as membrane receptors for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vam7p.Capture and release of partially zipped trans-SNARE complexes on intact organelles.The yeast lysosome-like vacuole: endpoint and crossroadsResolution of organelle docking and fusion kinetics in a cell-free assay.A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.Pairing phosphoinositides with calcium ions in endolysosomal dynamics: phosphoinositides control the direction and specificity of membrane trafficking by regulating the activity of calcium channels in the endolysosomes.The Golgin protein Coy1 functions in intra-Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs.Deleting the DAG kinase Dgk1 augments yeast vacuole fusion through increased Ypt7 activity and altered membrane fluidity.Reversible, cooperative reactions of yeast vacuole dockingThe coxsackievirus 2B protein increases efflux of ions from the endoplasmic reticulum and Golgi, thereby inhibiting protein trafficking through the Golgi.Analysis of a novel calcium auxotrophy in Aspergillus nidulans.Vps41 phosphorylation and the Rab Ypt7 control the targeting of the HOPS complex to endosome-vacuole fusion sites.
P2860
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P2860
Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
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2004年学术文章
@zh-sg
2004年學術文章
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2004年學術文章
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name
Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen.
@ast
Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen.
@en
type
label
Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen.
@ast
Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen.
@en
prefLabel
Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen.
@ast
Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen.
@en
P2860
P356
P1476
Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen.
@en
P2093
Alexey J Merz
William T Wickner
P2860
P304
P356
10.1083/JCB.200310105
P407
P577
2004-01-01T00:00:00Z