The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin
about
Purification and characterization of a novel 13 S hetero-oligomeric protein complex that stimulates in vitro Golgi transportIdentification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion proteinStimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosisOrdering the final events in yeast exocytosis.Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p.Mso1p: a yeast protein that functions in secretion and interacts physically and genetically with Sec1p.Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)Analysis of a yeast SNARE complex reveals remarkable similarity to the neuronal SNARE complex and a novel function for the C terminus of the SNAP-25 homolog, Sec9.Novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast.Sec1p binds to SNARE complexes and concentrates at sites of secretionA vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion.Identification of NSF as a beta-arrestin1-binding protein. Implications for beta2-adrenergic receptor regulationProtease resistance of syntaxin.SNAP-25.VAMP complexes. Implications for assembly and structureAn essential and NSF independent role for α-SNAP in store-operated calcium entryDisassembly of all SNARE complexes by N-ethylmaleimide-sensitive factor (NSF) is initiated by a conserved 1:1 interaction between α-soluble NSF attachment protein (SNAP) and SNARE complexSNAREs in native plasma membranes are active and readily form core complexes with endogenous and exogenous SNAREsSNAP-23 participates in SNARE complex assembly in rat adipose cellsThe V0 sector of the V-ATPase, synaptobrevin, and synaptophysin are associated on synaptic vesicles in a Triton X-100-resistant, freeze-thawing sensitive, complexThe gene for soluble N-ethylmaleimide sensitive factor attachment protein alpha is mutated in hydrocephaly with hop gait (hyh) miceAssembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesiclesFormation of a yeast SNARE complex is accompanied by significant structural changes-Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Is Expressed in Pancreatic Cells and Functions in Insulin but Not -Aminobutyric Acid SecretionSNAREs--engines for membrane fusionA molecular toggle after exocytosis sequesters the presynaptic syntaxin1a molecules involved in prior vesicle fusion.Distribution of synaptic vesicle proteins in the mammalian retina identifies obligatory and facultative components of ribbon synapses.Characterization of alpha-soluble N-ethylmaleimide-sensitive fusion attachment protein in alveolar type II cells: implications in lung surfactant secretion.Mapping of functional domains of gamma-SNAP.Formation and turnover of NSF- and SNAP-containing "fusion" complexes occur on undocked, clathrin-coated vesicle-derived membranes.Evaluation of the heterogeneous reactivity of the syntaxin molecules on the inner leaflet of the plasma membraneSec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion.Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes.The ionic layer is required for efficient dissociation of the SNARE complex by alpha-SNAP and NSF.Drosophila syntaxin is required for cell viability and may function in membrane formation and stabilization.α-SNAP prevents docking of the acrosome during sperm exocytosis because it sequesters monomeric syntaxin.Lysosomal fusion and SNARE function are impaired by cholesterol accumulation in lysosomal storage disorders.Biogenesis of the sorting endosome: the role of Rab5.Unraveling the mechanism of the vesicle transport ATPase NSF, the N-ethylmaleimide-sensitive factor.SNARE complex zero layer residues are not critical for N-ethylmaleimide-sensitive factor-mediated disassembly.Putative fusogenic activity of NSF is restricted to a lipid mixture whose coalescence is also triggered by other factorsA novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast.
P2860
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P2860
The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin
description
1995 nî lūn-bûn
@nan
1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
The N-ethylmaleimide-sensitive ...... formational change in syntaxin
@ast
The N-ethylmaleimide-sensitive ...... formational change in syntaxin
@en
The N-ethylmaleimide-sensitive ...... formational change in syntaxin
@nl
type
label
The N-ethylmaleimide-sensitive ...... formational change in syntaxin
@ast
The N-ethylmaleimide-sensitive ...... formational change in syntaxin
@en
The N-ethylmaleimide-sensitive ...... formational change in syntaxin
@nl
prefLabel
The N-ethylmaleimide-sensitive ...... formational change in syntaxin
@ast
The N-ethylmaleimide-sensitive ...... formational change in syntaxin
@en
The N-ethylmaleimide-sensitive ...... formational change in syntaxin
@nl
P2093
P2860
P356
P1476
The N-ethylmaleimide-sensitive ...... formational change in syntaxin
@en
P2093
P2860
P304
P356
10.1074/JBC.270.28.16955
P407
P577
1995-07-14T00:00:00Z