The stimulus-induced tyrosine phosphorylation of Munc18c facilitates vesicle exocytosis.
about
Negative regulation of syntaxin4/SNAP-23/VAMP2-mediated membrane fusion by Munc18c in vitroMunc18c depletion selectively impairs the sustained phase of insulin releaseDifferential phosphorylation of RhoGDI mediates the distinct cycling of Cdc42 and Rac1 to regulate second-phase insulin secretion.Exocytosis mechanisms underlying insulin release and glucose uptake: conserved roles for Munc18c and syntaxin 4Doc2b enrichment enhances glucose homeostasis in mice via potentiation of insulin secretion and peripheral insulin sensitivityTyrosine phosphorylation of Munc18c on residue 521 abrogates binding to Syntaxin 4Munc18c: a controversial regulator of peripheral insulin action.Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide binding mode of Sec1/Munc18 proteins.Munc18c phosphorylation by the insulin receptor links cell signaling directly to SNARE exocytosisStimulus-induced S-nitrosylation of Syntaxin 4 impacts insulin granule exocytosisBariatric surgery in morbidly obese insulin resistant humans normalises insulin signalling but not insulin-stimulated glucose disposal.Doc2b serves as a scaffolding platform for concurrent binding of multiple Munc18 isoforms in pancreatic islet β-cellsGelsolin associates with the N terminus of syntaxin 4 to regulate insulin granule exocytosis.Munc18-1 regulates first-phase insulin release by promoting granule docking to multiple syntaxin isoformsDoc2b is a key effector of insulin secretion and skeletal muscle insulin sensitivityMunc18c is not rate-limiting for glucose and long-chain fatty acid uptake in the heartGlucose-stimulated Cdc42 signaling is essential for the second phase of insulin secretionWNK1 is a novel regulator of Munc18c-syntaxin 4 complex formation in soluble NSF attachment protein receptor (SNARE)-mediated vesicle exocytosis.Ins (endocytosis) and outs (exocytosis) of GLUT4 traffickingMechanisms of biphasic insulin-granule exocytosis - roles of the cytoskeleton, small GTPases and SNARE proteins.SNARE proteins underpin insulin-regulated GLUT4 traffic.Modes of exocytosis and electrogenesis underlying canine biphasic insulin secretion.Studies of the regulated assembly of SNARE complexes in adipocytes.Exocytosis proteins as novel targets for diabetes prevention and/or remediation?The tyrosine phosphorylation of Munc18c induces a switch in binding specificity from syntaxin 4 to Doc2beta.Regulation of the SNARE-interacting protein Munc18c tyrosine phosphorylation in adipocytes by protein-tyrosine phosphatase 1BDisruption of protein complexes containing protein phosphatase 2B and Munc18c reduces the secretion of von Willebrand factor from endothelial cells.Doc2b Protects β-Cells Against Inflammatory Damage and Enhances Function.
P2860
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P2860
The stimulus-induced tyrosine phosphorylation of Munc18c facilitates vesicle exocytosis.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
The stimulus-induced tyrosine phosphorylation of Munc18c facilitates vesicle exocytosis.
@ast
The stimulus-induced tyrosine phosphorylation of Munc18c facilitates vesicle exocytosis.
@en
type
label
The stimulus-induced tyrosine phosphorylation of Munc18c facilitates vesicle exocytosis.
@ast
The stimulus-induced tyrosine phosphorylation of Munc18c facilitates vesicle exocytosis.
@en
prefLabel
The stimulus-induced tyrosine phosphorylation of Munc18c facilitates vesicle exocytosis.
@ast
The stimulus-induced tyrosine phosphorylation of Munc18c facilitates vesicle exocytosis.
@en
P2860
P356
P1476
The stimulus-induced tyrosine phosphorylation of Munc18c facilitates vesicle exocytosis.
@en
P2093
Debbie C Thurmond
P2860
P304
17624-17634
P356
10.1074/JBC.M601581200
P407
P577
2006-04-25T00:00:00Z