Results 21 to 30 of about 72,246 (300)
SNARE complex‐mediated degranulation in mast cells [PDF]
Introduction SNARE function in membrane fusion events Expression of SNAREs and SNARE complexes in mast cells Functional studies implicating specific SNAREs or SNARE complexes in mast cell degranulation RNA interference studies, SNARES and mast cells Regulation of mast cell SNAREs Conclusions Mast cell function and dysregulation is important in the ...
Woska, Joseph R, Gillespie, Marc E
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Epigallocatechin gallate inhibits SNARE‐dependent membrane fusion by blocking trans‐SNARE assembly
Insulin secretion is a signal‐triggered process that requires membrane fusion between the secretory granules and plasma membrane in pancreatic β cells. The exocytosis of insulin is mediated by target‐soluble N‐ethylmaleimide sensitive factor attachment ...
Min Zhu +4 more
doaj +1 more source
Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion [PDF]
SNARE functions during membrane docking and fusion are regulated by Sec1/Munc18 (SM) chaperones and Rab/Ypt GTPase effectors. These functions for yeast vacuole fusion are combined in the six-subunit HOPS complex. HOPS facilitates Ypt7p nucleotide exchange, is a Ypt7p effector, and contains an SM protein.
Kevin M, Collins +3 more
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Summary: The AAA+ NSF complex is responsible for SNARE complex disassembly both before and after membrane fusion. Loss of NSF function results in pronounced developmental and degenerative defects. In a genetic screen for sensory deficits in zebrafish, we
Yan Gao +8 more
doaj +1 more source
The COG complex interacts with multiple Golgi SNAREs and enhances fusogenic SNARE complexes assembly [PDF]
Multisubunit tethering complexes (MTCs) positively regulate vesicular fusion by as yet unclear mechanism. In this study we provide evidence that the MTC COG enhances the assembly of fusogenic Golgi SNARE complexes and concomitantly prevents nonfusogenic tSNARE interactions.
Orly Laufman, WanJin Hong, Sima Lev
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COG complexes form spatial landmarks for distinct SNARE complexes [PDF]
Vesicular tethers and SNAREs (soluble N-ethylmalemide-sensitive fusion attachment protein receptors) are two key protein components of the intracellular membrane-trafficking machinery. The conserved oligomeric Golgi (COG) complex has been implicated in the tethering of retrograde intra-Golgi vesicles.
Willett, Rose +6 more
openaire +2 more sources
Amyloid-β Oligomers May Impair SNARE-Mediated Exocytosis by Direct Binding to Syntaxin 1a
Alzheimer’s disease (AD) is closely associated with synaptic dysfunction, and thus current treatments often aim to stimulate neurotransmission to improve cognitive impairment.
Yoosoo Yang +7 more
doaj +1 more source
ATP-independent Control of Vac8 Palmitoylation by a SNARE Subcomplex on Yeast Vacuoles [PDF]
Yeast vacuole fusion requires palmitoylated Vac8. We previously showed that Vac8 acylation occurs early in the fusion reaction, is blocked by antibodies against Sec18 (yeast N-ethylmaleimide-sensitive fusion protein (NSF)), and is mediated by the R-SNARE
Cristodero, Marina +5 more
core +1 more source
Summary: Exocytosis of synaptic vesicles and dense-core vesicles requires both the Munc13 and CAPS (Ca2+-dependent activator proteins for secretion) proteins.
Hao Zhou +5 more
doaj +1 more source
VAMP721 conformations unmask an extended motif for K+ channel binding and gating control [PDF]
Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins play a major role in membrane fusion and contribute to cell expansion, signaling, and polar growth in plants.
Blatt, Mike R. +4 more
core +2 more sources

