Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
about
Vps33b pathogenic mutations preferentially affect VIPAS39/SPE-39-positive endosomesMunc18/Syntaxin interaction kinetics control secretory vesicle dynamics.Identification of the neuroblastoma-amplified gene product as a component of the syntaxin 18 complex implicated in Golgi-to-endoplasmic reticulum retrograde transportSingle-Vesicle Fusion Assay Reveals Munc18-1 Binding to the SNARE Core Is Sufficient for Stimulating Membrane FusionRegulation of intracellular membrane trafficking and cell dynamics by syntaxin-6Ultrahigh-resolution imaging reveals formation of neuronal SNARE/Munc18 complexes in situMunc18-1 binding to the neuronal SNARE complex controls synaptic vesicle primingReconciling the regulatory role of Munc18 proteins in SNARE-complex assemblyMolecular machines governing exocytosis of synaptic vesiclesDistinct initial SNARE configurations underlying the diversity of exocytosisConformational states of syntaxin-1 govern the necessity of N-peptide binding in exocytosis of PC12 cells and Caenorhabditis elegansDynamic conformational changes in munc18 prevent syntaxin bindingPossible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formationPrimordial neurosecretory apparatus identified in the choanoflagellate Monosiga brevicollisThe binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically inactive conformationCrystal Structures of the Sec1/Munc18 (SM) Protein Vps33, Alone and Bound to the Homotypic Fusion and Vacuolar Protein Sorting (HOPS) Subunit Vps16*Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformationSyntaxin binding mechanism and disease-causing mutations in Munc18-2Prefusion structure of syntaxin-1A suggests pathway for folding into neuronal trans-SNARE complex fusion intermediate.Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1.Negative regulation of syntaxin4/SNAP-23/VAMP2-mediated membrane fusion by Munc18c in vitroMunc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complexVesicle fusion probability is determined by the specific interactions of munc18An extended helical conformation in domain 3a of Munc18-1 provides a template for SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complex assembly.SNAREpin assembly by Munc18-1 requires previous vesicle docking by synaptotagmin 1.Crucial role of the hydrophobic pocket region of Munc18 protein in mast cell degranulation.Munc18-1 and the Syntaxin-1 N Terminus Regulate Open-Closed States in a t-SNARE Complex.Reconstituting SNARE-mediated membrane fusion at the single liposome level.Identifying and quantitating conformational exchange in membrane proteins using site-directed spin labeling.Yeast Sec1p functions before and after vesicle docking.Allosteric control of syntaxin 1a by Munc18-1: characterization of the open and closed conformations of syntaxin.Novel 9q34.11 gene deletions encompassing combinations of four Mendelian disease genes: STXBP1, SPTAN1, ENG, and TOR1A.Analysis of familial hemophagocytic lymphohistiocytosis type 4 (FHL-4) mutant proteins reveals that S-acylation is required for the function of syntaxin 11 in natural killer cellsDifferential interaction of tomosyn with syntaxin and SNAP25 depends on domains in the WD40 β-propeller core and determines its inhibitory activity.Single-molecule studies of the neuronal SNARE fusion machinery.The longin SNARE VAMP7/TI-VAMP adopts a closed conformation.Membrane bridging and hemifusion by denaturated Munc18.SNARE bundle and syntaxin N-peptide constitute a minimal complement for Munc18-1 activation of membrane fusion.At the junction of SNARE and SM protein function.Autoinhibition of SNARE complex assembly by a conformational switch represents a conserved feature of syntaxins.
P2860
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P2860
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
description
2008 nî lūn-bûn
@nan
2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
@ast
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
@en
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
@nl
type
label
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
@ast
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
@en
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
@nl
prefLabel
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
@ast
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
@en
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
@nl
P2860
P50
P356
P1433
P1476
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
@en
P2093
Douglas A Hattendorf
P2860
P304
P356
10.1038/EMBOJ.2008.37
P407
P577
2008-04-09T00:00:00Z