Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes.
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
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
Mol. Cell
Date: Jun. 01, 1999
PubMed ID: 10394363
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