The major role of the Rab Ypt7p in vacuole fusion is supporting HOPS membrane association.
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The HOPS proteins hVps41 and hVps39 are required for homotypic and heterotypic late endosome fusionCoat/Tether Interactions-Exception or Rule?Membrane trafficking and phagosome maturation during the clearance of apoptotic cellsStructures and mechanisms of vesicle coat components and multisubunit tethering complexesPhosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusionThe HOPS/Class C Vps Complex Tethers High-Curvature Membranes via a Direct Protein-Membrane Interaction.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 complexPhosphorylation 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.Vps-C complexes: gatekeepers of endolysosomal traffic.Dynamic association of the PI3P-interacting Mon1-Ccz1 GEF with vacuoles is controlled through its phosphorylation by the type 1 casein kinase Yck3.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.Membrane tetheringPhosphorylation 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.Yeast vacuolar HOPS, regulated by its kinase, exploits affinities for acidic lipids and Rab:GTP for membrane binding and to catalyze tethering and fusion.Metazoan cell biology of the HOPS tethering complexMembrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to small molecules and by lysis.Intrinsic tethering activity of endosomal Rab proteinsThe toxicity of an "artificial" amyloid is related to how it interacts with membranes.Bioengineered yeast-derived vacuoles with enhanced tissue-penetrating ability for targeted cancer therapyImproved reconstitution of yeast vacuole fusion with physiological SNARE concentrations reveals an asymmetric Rab(GTP) requirement.Fusion proteins and select lipids cooperate as membrane receptors for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vam7p.Neo1 and phosphatidylethanolamine contribute to vacuole membrane fusion in Saccharomyces cerevisiae.The Ccz1-Mon1-Rab7 module and Rab5 control distinct steps of autophagy.The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexes.Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components.Endolysosomal membrane trafficking complexes drive nutrient-dependent TORC1 signaling to control cell growth in Saccharomyces cerevisiaeNew links between vesicle coats and Rab-mediated vesicle targeting.Functional homologies in vesicle tethering.Deleting the DAG kinase Dgk1 augments yeast vacuole fusion through increased Ypt7 activity and altered membrane fluidity.Rab7 may be a novel therapeutic target for neurologic diseases as a key regulator in autophagy.The small GTPase Arl8b regulates assembly of the mammalian HOPS complex on lysosomes.Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion-to-fusion transition.A short region upstream of the yeast vacuolar Qa-SNARE heptad-repeats promotes membrane fusion through enhanced SNARE complex assembly.hVps41 and VAMP7 function in direct TGN to late endosome transport of lysosomal membrane proteins.
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The major role of the Rab Ypt7p in vacuole fusion is supporting HOPS membrane association.
description
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 21 April 2009
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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
The major role of the Rab Ypt7 ...... ing HOPS membrane association.
@en
The major role of the Rab Ypt7 ...... ing HOPS membrane association.
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type
label
The major role of the Rab Ypt7 ...... ing HOPS membrane association.
@en
The major role of the Rab Ypt7 ...... ing HOPS membrane association.
@nl
prefLabel
The major role of the Rab Ypt7 ...... ing HOPS membrane association.
@en
The major role of the Rab Ypt7 ...... ing HOPS membrane association.
@nl
P2093
P2860
P356
P1476
The major role of the Rab Ypt7 ...... ing HOPS membrane association.
@en
P2093
Christopher M Hickey
Christopher Stroupe
William Wickner
P2860
P304
16118-16125
P356
10.1074/JBC.M109.000737
P407
P577
2009-04-21T00:00:00Z