Searching across hundreds of databases
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.
Pubmed ID: 10394363 RIS Download
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
Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.
SciCrunch is a data sharing and display platform. Anyone can create a custom portal where they can select searchable subsets of hundreds of data sources, brand their web pages and create their community. SciCrunch will push data updates automatically to all portals on a weekly basis. User communities can also add their own data to SciCrunch, however this is not currently a free service.
