Munc18-bound syntaxin readily forms SNARE complexes with synaptobrevin in native plasma membranes - Wikidata - awgldk - TriplyDB

Munc18-bound syntaxin readily forms SNARE complexes with synaptobrevin in native plasma membranes

Munc18-bound syntaxin readily forms SNARE complexes with synaptobrevin in native plasma membranes

http://www.wikidata.org/entity/Q21092770

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Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide Munc18-1 binds directly to the neuronal SNARE complex Multiple roles for the actin cytoskeleton during regulated exocytosis Molecular machines governing exocytosis of synaptic vesicles Distinct initial SNARE configurations underlying the diversity of exocytosis Resident CAPS on dense-core vesicles docks and primes vesicles for fusion TNFα induces co-trafficking of TRPV1/TRPA1 in VAMP1-containing vesicles to the plasmalemma via Munc18-1/syntaxin1/SNAP-25 mediated fusion.Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation Organization and dynamics of SNARE proteins in the presynaptic membrane The specificity of SNARE pairing in biological membranes is mediated by both proof-reading and spatial segregation Vesicle fusion probability is determined by the specific interactions of munc18 Imaging the assembly and disassembly kinetics of cis-SNARE complexes on native plasma membranes Reconstituting SNARE-mediated membrane fusion at the single liposome level.Exocytosis mechanisms underlying insulin release and glucose uptake: conserved roles for Munc18c and syntaxin 4 Differential 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.Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex Basolateral sorting of syntaxin 4 is dependent on its N-terminal domain and the AP1B clathrin adaptor, and required for the epithelial cell polarity.Dual roles of Munc18-1 rely on distinct binding modes of the central cavity with Stx1A and SNARE complex Native presynaptic metabotropic glutamate receptor 4 (mGluR4) interacts with exocytosis proteins in rat cerebellum Differential Regulation of Synaptic Vesicle Tethering and Docking by UNC-18 and TOM-1.The functions of Munc18-1 in regulated exocytosis.Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.Contact-induced clustering of syntaxin and munc18 docks secretory granules at the exocytosis site.Resolving the function of distinct Munc18-1/SNARE protein interaction modes in a reconstituted membrane fusion assay.Single-molecule measurements of dissociation rates and energy landscapes of binary trans snare complexes in parallel versus antiparallel orientation Doc2b serves as a scaffolding platform for concurrent binding of multiple Munc18 isoforms in pancreatic islet β-cells Dynamical Organization of Syntaxin-1A at the Presynaptic Active Zone Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission.FRAP to Characterize Molecular Diffusion and Interaction in Various Membrane Environments.Munc18-1 is critical for plasma membrane localization of syntaxin1 but not of SNAP-25 in PC12 cells.Quantitative Proteomic Analysis Reveals Molecular Adaptations in the Hippocampal Synaptic Active Zone of Chronic Mild Stress-Unsusceptible Rats.Synaptic vesicle fusion.Munc18a scaffolds SNARE assembly to promote membrane fusion UNC-18 modulates ethanol sensitivity in Caenorhabditis elegans.Friends and foes in synaptic transmission: the role of tomosyn in vesicle priming.Cab45b, a Munc18b-interacting partner, regulates exocytosis in pancreatic beta-cells.Abrogating Munc18-1-SNARE complex interaction has limited impact on exocytosis in PC12 cells.Rescuing the subprime meltdown in insulin exocytosis in diabetes.Rescue of Munc18-1 and -2 double knockdown reveals the essential functions of interaction between Munc18 and closed syntaxin in PC12 cells.

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Munc18-bound syntaxin readily forms SNARE complexes with synaptobrevin in native plasma membranes

http://www.wikidata.org/entity/Q21092770

description

2006 nî lūn-bûn

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2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Munc18-bound syntaxin readily ...... vin in native plasma membranes

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Munc18-bound syntaxin readily ...... vin in native plasma membranes

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Munc18-bound syntaxin readily ...... vin in native plasma membranes

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Munc18-bound syntaxin readily ...... vin in native plasma membranes

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type

label

Munc18-bound syntaxin readily ...... vin in native plasma membranes

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Munc18-bound syntaxin readily ...... vin in native plasma membranes

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Munc18-bound syntaxin readily ...... vin in native plasma membranes

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Munc18-bound syntaxin readily ...... vin in native plasma membranes

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Munc18-Bound Syntaxin Readily ...... vin in Native Plasma Membranes

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prefLabel

Munc18-bound syntaxin readily ...... vin in native plasma membranes

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Munc18-bound syntaxin readily ...... vin in native plasma membranes

@en

Munc18-bound syntaxin readily ...... vin in native plasma membranes

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Munc18-bound syntaxin readily ...... vin in native plasma membranes

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JOURNAL.PBIO.0040330

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Munc18-bound syntaxin readily ...... vin in native plasma membranes

@en

P2093

Felipe E Zilly

http://www.w3.org/2001/XMLSchema#string

Thorsten Lang

http://www.w3.org/2001/XMLSchema#string

P2860

How Tlg2p/syntaxin 16 'snares' Vps45

A conformational switch in syntaxin during exocytosis: role of munc18.

Alternative splicing of SNAP-25 regulates secretion through nonconservative substitutions in the SNARE domain.

Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p.

Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A

Munc18-1 stabilizes syntaxin 1, but is not essential for syntaxin 1 targeting and SNARE complex formation.

Sec1p directly stimulates SNARE-mediated membrane fusion in vitro.

Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes.

Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation.

Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis.

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e330

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scholarly article

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222963

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10.1371/JOURNAL.PBIO.0040330

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10

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4

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Jakob B. Sørensen

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2006-10-01T00:00:00Z

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6791123

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17002520

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1570500

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