Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components. - Wikidata - awgldk - TriplyDB

Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components.

Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components.

http://www.wikidata.org/entity/Q37394517

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Structural basis of Vps33A recruitment to the human HOPS complex by Vps16 The Secret Life of Tethers: The Role of Tethering Factors in SNARE Complex Regulation Exorcising the exocyst complex Function and regulation of the endosomal fusion and fission machineries Organelle acidification negatively regulates vacuole membrane fusion in vivo.HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion The HOPS/class C Vps complex tethers membranes by binding to one Rab GTPase in each apposed membrane.In vitro assay using engineered yeast vacuoles for neuronal SNARE-mediated membrane fusion.Membranes linked by trans-SNARE complexes require lipids prone to non-bilayer structure for progression to fusion.The yeast vacuolar Rab GTPase Ypt7p has an activity beyond membrane recruitment of the homotypic fusion and protein sorting-Class C Vps complex Phosphorylation of the effector complex HOPS by the vacuolar kinase Yck3p confers Rab nucleotide specificity for vacuole docking and fusion.Molecular architecture of the multisubunit homotypic fusion and vacuole protein sorting (HOPS) tethering complex.Live-cell imaging of exocyst links its spatiotemporal dynamics to various stages of vesicle fusion.SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18.HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly.Key role of polyphosphoinositides in dynamics of fusogenic nuclear membrane vesicles.An update on transport vesicle tethering.At the junction of SNARE and SM protein function.Sequential analysis of trans-SNARE formation in intracellular membrane fusion Membrane tethering Phosphorylation of a membrane curvature-sensing motif switches function of the HOPS subunit Vps41 in membrane tethering.Phosphoinositides function asymmetrically for membrane fusion, promoting tethering and 3Q-SNARE subcomplex assembly.LegC3, an effector protein from Legionella pneumophila, inhibits homotypic yeast vacuole fusion in vivo and in vitro Yeast vacuolar HOPS, regulated by its kinase, exploits affinities for acidic lipids and Rab:GTP for membrane binding and to catalyze tethering and fusion.The Vps39-like TRAP1 is an effector of Rab5 and likely the missing Vps3 subunit of human CORVET Munc18a does not alter fusion rates mediated by neuronal SNAREs, synaptotagmin, and complexin Rab proteins and the compartmentalization of the endosomal system Membrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to small molecules and by lysis.Sec17 can trigger fusion of trans-SNARE paired membranes without Sec18.Intrinsic tethering activity of endosomal Rab proteins Vacuolar ATPase in phagosome-lysosome fusion.N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release.Fusion proteins and select lipids cooperate as membrane receptors for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vam7p.The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexes.Organelle docking: R-SNAREs are late.HOPS catalyzes the interdependent assembly of each vacuolar SNARE into a SNARE complex.New links between vesicle coats and Rab-mediated vesicle targeting.Principle of duality in phospholipids: regulators of membrane morphology and dynamics.

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Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components.

http://www.wikidata.org/entity/Q37394517

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

@tr

scientific article published on 13 October 2009

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

Minimal membrane docking requi ...... sion from purified components.

@en

Minimal membrane docking requi ...... sion from purified components.

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type

label

Minimal membrane docking requi ...... sion from purified components.

@en

Minimal membrane docking requi ...... sion from purified components.

@nl

prefLabel

Minimal membrane docking requi ...... sion from purified components.

@en

Minimal membrane docking requi ...... sion from purified components.

@nl

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PNAS.0903801106

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Proceedings of the National Academy of Sciences of the United States of America

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Minimal membrane docking requi ...... sion from purified components.

@en

P2093

Amy S Burfeind

http://www.w3.org/2001/XMLSchema#string

Christopher M Hickey

http://www.w3.org/2001/XMLSchema#string

Christopher Stroupe

http://www.w3.org/2001/XMLSchema#string

Joji Mima

http://www.w3.org/2001/XMLSchema#string

William Wickner

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P2860

Rab27a: A key to melanosome transport in human melanocytes

A conformational switch in syntaxin during exocytosis: role of munc18.

Membrane fusion and the lamellar-to-inverted-hexagonal phase transition in cardiolipin vesicle systems induced by divalent cations

Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs

Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis

Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae

Complexin controls the force transfer from SNARE complexes to membranes in fusion

Open syntaxin docks synaptic vesicles

New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion.

Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins

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17626-17633

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scholarly article

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10.1073/PNAS.0903801106

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42

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106

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2009-10-13T00:00:00Z

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26891701

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19826089

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2764952

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