Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes.
Mol Cell, 1999/6;3(6):751-60.
Min J[1], Okada S, Kanzaki M, Elmendorf JS, Coker KJ, Ceresa BP, Syu LJ, Noda Y, Saltiel AR, Pessin JE
Affiliations
PMID: 10394363
Impact factor: 19.328
Abstract
Insulin-stimulated glucose transport and GLUT4 translocation require regulated interactions between the v-SNARE, VAMP2, and the t-SNARE, syntaxin 4. We have isolated a novel syntaxin 4-binding protein, Synip, which specifically interacts with syntaxin 4. Insulin induces a dissociation of the Synip:syntaxin 4 complex due to an apparent decrease in the binding affinity of Synip for syntaxin 4. In contrast, the carboxyterminal domain of Synip does not dissociate from syntaxin 4 in response to insulin stimulation but inhibits glucose transport and GLUT4 translocation. These data implicate Synip as an insulin-regulated syntaxin 4-binding protein directly involved in the control of glucose transport and GLUT4 vesicle translocation.
MeSH terms
Adipocytes; Amino Acid Sequence; Animals; Binding, Competitive; Biological Transport; Carrier Proteins; Cell Line; Cloning, Molecular; Cricetinae; Genes, Dominant; Glucose; Glucose Transporter Type 4; Humans; Insulin; Membrane Proteins; Mice; Molecular Sequence Data; Monosaccharide Transport Proteins; Muscle Proteins; Mutation; Organelles; Protein Binding; Qa-SNARE Proteins; Qb-SNARE Proteins; Qc-SNARE Proteins; R-SNARE Proteins; RNA, Messenger; Vesicular Transport Proteins; Yeasts
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