Toggle Main Menu Toggle Search

Open Access padlockePrints

Syntaxin 6 regulates Glut4 trafficking in 3T3-L1 adipocytes

Lookup NU author(s): Dr Nick Morris


Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


Insulin stimulates the movement of glucose transporter-4 (Glut4)-containing vesicles to the plasma membrane of adipose cells. We investigated the role of post-Golgi t-soluble N-ethylma-leimide-sensitive factor attachment protein receptors (SNAREs) in the trafficking of Glut4 in 3T3-L1 adipocytes. Greater than 85% of syntaxin 6 was found in Glut4-containing vesicles, and this t-SNARE exhibited insulin-stimulated movement to the plasma membrane. In contrast, the colocalization of Glut4 with syntaxin 7, 8, or 12/13 was limited and these molecules did not translocate to the plasma membrane. We used adenovirus to overexpress the cytosolic domain of these syntaxin's and studied their effects on Glut4 traffic. Overexpression of the cytosolic domain of syntaxin 6 did not affect insulin-stimulated glucose transport, but increased basal deGlc transport and cell surface Glut4 levels. Moreover, the syntaxin 6 cytosolic domain significantly reduced the rate of Glut4 reinternalization after insulin withdrawal and perturbed subendosomal Glut4 sorting; the corresponding domains of syntaxins 8 and 12 were without effect. Our data suggest that syntaxin 6 is involved in a membrane-trafficking step that sequesters Glut4 away from traffic destined for the plasma membrane. We speculate that this is at the level of traffic of Glut4 into its unique storage compartment and that syntaxin 16 may be involved.

Publication metadata

Author(s): Perera HKI, Clarke M, Morris NJ, Hong W, Chamberlain LH, Gould GW

Publication type: Article

Publication status: Published

Journal: Molecular Biology of the Cell

Year: 2003

Volume: 14

Issue: 7

Pages: 2946-2958

ISSN (print): 1059-1524

ISSN (electronic): 1939-4586

Publisher: American Society for Cell Biology


DOI: 10.1091/mbc.E02-11-0722

PubMed id: 12857877


Altmetrics provided by Altmetric