SNARE interactions are not selective. Implications for membrane fusion specificity.
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Munc18-bound syntaxin readily forms SNARE complexes with synaptobrevin in native plasma membranesVAMP-7 mediates vesicular transport from endosomes to lysosomesAczonin, a 550-kD putative scaffolding protein of presynaptic active zones, shares homology regions with Rim and Bassoon and binds profilinDifferential roles of syntaxin 7 and syntaxin 8 in endosomal traffickingSyntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle traffickingDirect interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagminAmisyn, a novel syntaxin-binding protein that may regulate SNARE complex assemblyMolecular basis for the sorting of the SNARE VAMP7 into endocytic clathrin-coated vesicles by the ArfGAP HrbIdentification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosisThe UT-A1 urea transporter interacts with snapin, a SNARE-associated proteinSyntaxin 7 is localized to late endosome compartments, associates with Vamp 8, and Is required for late endosome-lysosome fusionThe R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomesSNAP-29: a general SNARE protein that inhibits SNARE disassembly and is implicated in synaptic transmissionA SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and functionSNARE proteins mediate lipid bilayer fusionSec34p, a protein required for vesicle tethering to the yeast Golgi apparatus, is in a complex with Sec35pLTP requires a unique postsynaptic SNARE fusion machinerySynaptic vesicle exocytosisThe Secret Life of Tethers: The Role of Tethering Factors in SNARE Complex RegulationDistinct initial SNARE configurations underlying the diversity of exocytosisMolecular characterisation of transport mechanisms at the developing mouse blood-CSF interface: a transcriptome approachA novel snare N-terminal domain revealed by the crystal structure of Sec22bHomotetrameric structure of the SNAP-23 N-terminal coiled-coil domainEarly endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologiesOrdering the final events in yeast exocytosis.Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes.Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late GolgiThe Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE ComplexesGenetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6.Analysis of Sec22p in endoplasmic reticulum/Golgi transport reveals cellular redundancy in SNARE protein function.The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast.Identification of domains required for developmentally regulated SNARE function in Saccharomyces cerevisiaeSec1p binds to SNARE complexes and concentrates at sites of secretionSyntaxin 13 is a developmentally regulated SNARE involved in neurite outgrowth and endosomal traffickingThree-dimensional structure of the neuronal-Sec1-syntaxin 1a complexMixed and non-cognate SNARE complexes. Characterization of assembly and biophysical propertiesThe N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assemblyCysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targetingThe identification of a novel endoplasmic reticulum to Golgi SNARE complex used by the prechylomicron transport vesicleDirect interaction of Rab4 with syntaxin 4
P2860
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P2860
SNARE interactions are not selective. Implications for membrane fusion specificity.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
SNARE interactions are not selective. Implications for membrane fusion specificity.
@en
type
label
SNARE interactions are not selective. Implications for membrane fusion specificity.
@en
prefLabel
SNARE interactions are not selective. Implications for membrane fusion specificity.
@en
P2093
P2860
P356
P1476
SNARE interactions are not selective. Implications for membrane fusion specificity.
@en
P2093
Gonzalez L Jr
Prekeris R
Scheller RH
Steegmaier M
P2860
P304
P356
10.1074/JBC.274.9.5649
P407
P577
1999-02-01T00:00:00Z