Munc18-1 domain-1 controls vesicle docking and secretion by interacting with syntaxin-1 and chaperoning it to the plasma membrane
about
Conformational states of syntaxin-1 govern the necessity of N-peptide binding in exocytosis of PC12 cells and Caenorhabditis elegansPrefusion structure of syntaxin-1A suggests pathway for folding into neuronal trans-SNARE complex fusion intermediate.Identification of a Munc13-sensitive step in chromaffin cell large dense-core vesicle exocytosisCrucial role of the hydrophobic pocket region of Munc18 protein in mast cell degranulation.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 cellsLow-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide.Hemophagocytic lymphohistiocytosis caused by dominant-negative mutations in STXBP2 that inhibit SNARE-mediated membrane fusion.Contact-induced clustering of syntaxin and munc18 docks secretory granules at the exocytosis site.Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission.Munc18-1 regulates first-phase insulin release by promoting granule docking to multiple syntaxin isoformsMunc18-1 controls SNARE protein complex assembly during human sperm acrosomal exocytosis.Munc18-2 is required for Syntaxin 11 Localization on the Plasma Membrane in Cytotoxic T-Lymphocytes.Munc18-1 is a molecular chaperone for α-synuclein, controlling its self-replicating aggregationBeyond the SNARE: Munc18-1 chaperones α-synuclein.Calcium-dependent activator protein for secretion 1 (CAPS1) binds to syntaxin-1 in a distinct mode from Munc13-1.A pivotal role for pro-335 in balancing the dual functions of Munc18-1 domain-3a in regulated exocytosis.MiR-335 overexpression impairs insulin secretion through defective priming of insulin vesicles.Revisiting interaction specificity reveals neuronal and adipocyte Munc18 membrane fusion regulatory proteins differ in their binding interactions with partner SNARE Syntaxins.UNC-18 and Tomosyn Antagonistically Control Synaptic Vesicle Priming Downstream of UNC-13 in Caenorhabditis elegans.Activity-driven relaxation of the cortical actomyosin II network synchronizes Munc18-1-dependent neurosecretory vesicle docking.LuTHy: a double-readout bioluminescence-based two-hybrid technology for quantitative mapping of protein-protein interactions in mammalian cells
P2860
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P2860
Munc18-1 domain-1 controls vesicle docking and secretion by interacting with syntaxin-1 and chaperoning it to the plasma membrane
description
2011 nî lūn-bûn
@nan
2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Munc18-1 domain-1 controls ves ...... ning it to the plasma membrane
@ast
Munc18-1 domain-1 controls ves ...... ning it to the plasma membrane
@en
type
label
Munc18-1 domain-1 controls ves ...... ning it to the plasma membrane
@ast
Munc18-1 domain-1 controls ves ...... ning it to the plasma membrane
@en
prefLabel
Munc18-1 domain-1 controls ves ...... ning it to the plasma membrane
@ast
Munc18-1 domain-1 controls ves ...... ning it to the plasma membrane
@en
P2093
P2860
P356
P1476
Munc18-1 domain-1 controls ves ...... ning it to the plasma membrane
@en
P2093
Gayoung A Han
Liping Han
Nancy T Malintan
Ner Mu Nar Saw
Shuzo Sugita
P2860
P304
P356
10.1091/MBC.E11-02-0135
P577
2011-09-07T00:00:00Z