| First Author | Min J | Year | 1999 |
| Journal | Mol Cell | Volume | 3 |
| Issue | 6 | Pages | 751-60 |
| PubMed ID | 10394363 | Mgi Jnum | J:55848 |
| Mgi Id | MGI:1339478 | Doi | 10.1016/s1097-2765(01)80007-1 |
| Citation | Min J, et al. (1999) Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes. Mol Cell 3(6):751-60 |
| abstractText | 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. |
