Insulin-triggered repositioning of munc18c on syntaxin-4 in GLUT4 signalling

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Insulin-triggered repositioning of munc18c on syntaxin-4 in GLUT4 signalling.

One of the most important actions of insulin is the stimulation of the uptake of glucose into fat and muscle cells. Crucial to this response is the translocation of GLUT4 (glucose transporter-4) to the plasma membrane. The insulin-stimulated GLUT4 vesicle docking at the plasma membrane requires an interaction between VAMP-2 (vesicle-associated membrane protein-2) on the GLUT4 vesicle and syntax...

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Skeletal muscle munc18c and syntaxin 4 in human obesity

BACKGROUND Animal and cell culture data suggest a critical role for Munc18c and Syntaxin 4 proteins in insulin mediated glucose transport in skeletal muscle, but no studies have been published in humans. METHODS We investigated the effect of a 12 vs. 48 hr fast on insulin action and skeletal muscle Munc18c and Syntaxin 4 protein in lean and obese subjects. Healthy lean (n = 14; age = 28.0 +/-...

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Exocytosis mechanisms underlying insulin release and glucose uptake: conserved roles for Munc18c and syntaxin 4.

Type 2 diabetes has been coined "a two-hit disease," as it involves specific defects of glucose-stimulated insulin secretion from the pancreatic beta cells in addition to defects in peripheral tissue insulin action required for glucose uptake. Both of these processes, insulin secretion and glucose uptake, are mediated by SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein recept...

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DOC2B: A Novel Syntaxin-4 Binding Protein Mediating Insulin-Regulated GLUT4 Vesicle Fusion in Adipocytes

OBJECTIVE Insulin stimulates glucose uptake in skeletal muscle and adipose tissues primarily by stimulating the translocation of vesicles containing a facilitative glucose transporter, GLUT4, from intracellular compartments to the plasma membrane. The formation of stable soluble N-ethyl-maleimide-sensitive fusion protein [NSF] attachment protein receptor (SNARE) complexes between vesicle-associ...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 2008

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj20070802