Functionally and spatially distinct modes of munc18-syntaxin 1 interaction
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Munc18/Syntaxin interaction kinetics control secretory vesicle dynamics.Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptideSyntaxin-1 N-peptide and Habc-domain perform distinct essential functions in synaptic vesicle fusionReconciling the regulatory role of Munc18 proteins in SNARE-complex assemblyDistinct initial SNARE configurations underlying the diversity of exocytosisDynamic conformational changes in munc18 prevent syntaxin bindingPossible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formationSynaptic vesicle docking: sphingosine regulates syntaxin1 interaction with Munc18Vesicle 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.A molecular toggle after exocytosis sequesters the presynaptic syntaxin1a molecules involved in prior vesicle fusion.SNAREpin/Munc18 promotes adhesion and fusion of large vesicles to giant membranest-SNARE protein conformations patterned by the lipid microenvironment.Membrane trafficking of large conductance calcium-activated potassium channels is regulated by alternative splicing of a transplantable, acidic trafficking motif in the RCK1-RCK2 linker.SNARE bundle and syntaxin N-peptide constitute a minimal complement for Munc18-1 activation of membrane fusion.Autoinhibition of SNARE complex assembly by a conformational switch represents a conserved feature of syntaxins.Rapid disruption of axon-glial integrity in response to mild cerebral hypoperfusionDual roles of Munc18-1 rely on distinct binding modes of the central cavity with Stx1A and SNARE complexLow-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide.Syntaxin N-terminal peptide motif is an initiation factor for the assembly of the SNARE-Sec1/Munc18 membrane fusion complexThe WNKs: atypical protein kinases with pleiotropic actions.Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide binding mode of Sec1/Munc18 proteins.Differential Regulation of Synaptic Vesicle Tethering and Docking by UNC-18 and TOM-1.Structure-function study of mammalian Munc18-1 and C. elegans UNC-18 implicates domain 3b in the regulation of exocytosis.De novo mutations in the gene encoding STXBP1 (MUNC18-1) cause early infantile epileptic encephalopathy.The functions of Munc18-1 in regulated exocytosis.Munc18-1 and Munc18-2 proteins modulate beta-cell Ca2+ sensitivity and kinetics of insulin exocytosis differently.Resolving the function of distinct Munc18-1/SNARE protein interaction modes in a reconstituted membrane fusion assay.Munc18-1 domain-1 controls vesicle docking and secretion by interacting with syntaxin-1 and chaperoning it to the plasma membraneEndoplasmic reticulum localization of DHHC palmitoyltransferases mediated by lysine-based sorting signalsDynamical Organization of Syntaxin-1A at the Presynaptic Active ZoneMunc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission.FRAP to Characterize Molecular Diffusion and Interaction in Various Membrane Environments.WNK1 is a novel regulator of Munc18c-syntaxin 4 complex formation in soluble NSF attachment protein receptor (SNARE)-mediated vesicle exocytosis.UNC-18 promotes both the anterograde trafficking and synaptic function of syntaxin.UNC-18 modulates ethanol sensitivity in Caenorhabditis elegans.The Munc18-1 domain 3a hinge-loop controls syntaxin-1A nanodomain assembly and engagement with the SNARE complex during secretory vesicle priming.The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p.Abrogating Munc18-1-SNARE complex interaction has limited impact on exocytosis in PC12 cells.
P2860
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P2860
Functionally and spatially distinct modes of munc18-syntaxin 1 interaction
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Functionally and spatially distinct modes of munc18-syntaxin 1 interaction
@en
type
label
Functionally and spatially distinct modes of munc18-syntaxin 1 interaction
@en
prefLabel
Functionally and spatially distinct modes of munc18-syntaxin 1 interaction
@en
P2860
P356
P1476
Functionally and spatially distinct modes of munc18-syntaxin 1 interaction
@en
P2093
Axel Bergmann
Claire N Medine
P2860
P304
12097-12103
P356
10.1074/JBC.M700227200
P407
P577
2007-01-30T00:00:00Z