Capture and release of partially zipped trans-SNARE complexes on intact organelles.
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Molecular machines governing exocytosis of synaptic vesiclesThe V-ATPase proteolipid cylinder promotes the lipid-mixing stage of SNARE-dependent fusion of yeast vacuoles.HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusionMembranes 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.HOPS interacts with Apl5 at the vacuole membrane and is required for consumption of AP-3 transport vesicles.How and why intralumenal membrane fragments form during vacuolar lysosome fusion.Vps-C complexes: gatekeepers of endolysosomal traffic.SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18.Negative potentials across biological membranes promote fusion by class II and class III viral proteinsHOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly.The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulationCommon intermediates and kinetics, but different energetics, in the assembly of SNARE proteins.A lipid-anchored SNARE supports membrane fusionA distinct tethering step is vital for vacuole membrane fusion.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 vitroYeast vacuolar HOPS, regulated by its kinase, exploits affinities for acidic lipids and Rab:GTP for membrane binding and to catalyze tethering and fusion.Topological arrangement of the intracellular membrane fusion machinery.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.Vacuolar SNARE protein transmembrane domains serve as nonspecific membrane anchors with unequal roles in lipid mixing.Endosomal Na+ (K+)/H+ exchanger Nhx1/Vps44 functions independently and downstream of multivesicular body formation.Intrinsic tethering activity of endosomal Rab proteinsThe Energetics of Streptococcal Enolase Octamer Formation: The Quantitative Contributions of the Last Eight Amino Acids at the Carboxy-Terminus.Three steps forward, two steps back: mechanistic insights into the assembly and disassembly of the SNARE complex.N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assemblySec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.Munc18-1-regulated stage-wise SNARE assembly underlying synaptic exocytosis.Doc2b promotes GLUT4 exocytosis by activating the SNARE-mediated fusion reaction in a calcium- and membrane bending-dependent mannerMembrane fusion intermediates via directional and full assembly of the SNARE complex.Synip arrests soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-dependent membrane fusion as a selective target membrane SNARE-binding inhibitor.Improved reconstitution of yeast vacuole fusion with physiological SNARE concentrations reveals an asymmetric Rab(GTP) requirement.The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexes.Complex lipid requirements for SNARE- and SNARE chaperone-dependent membrane fusion.Components of the SNARE-containing regulon are co-regulated in root cells undergoing defense.HOPS catalyzes the interdependent assembly of each vacuolar SNARE into a SNARE complex.New links between vesicle coats and Rab-mediated vesicle targeting.The proteins of exocytosis: lessons from the sperm model.
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P2860
Capture and release of partially zipped trans-SNARE complexes on intact organelles.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Capture and release of partially zipped trans-SNARE complexes on intact organelles.
@en
Capture and release of partially zipped trans-SNARE complexes on intact organelles.
@nl
type
label
Capture and release of partially zipped trans-SNARE complexes on intact organelles.
@en
Capture and release of partially zipped trans-SNARE complexes on intact organelles.
@nl
prefLabel
Capture and release of partially zipped trans-SNARE complexes on intact organelles.
@en
Capture and release of partially zipped trans-SNARE complexes on intact organelles.
@nl
P2860
P356
P1476
Capture and release of partially zipped trans-SNARE complexes on intact organelles.
@en
P2093
Alexey J Merz
Matthew L Schwartz
P2860
P304
P356
10.1083/JCB.200811082
P407
P577
2009-05-01T00:00:00Z