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 carboxy-terminal 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.
Original language | English (US) |
---|---|
Pages (from-to) | 751-760 |
Number of pages | 10 |
Journal | Molecular Cell |
Volume | 3 |
Issue number | 6 |
DOIs | |
State | Published - Jun 1999 |
Externally published | Yes |
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology