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Updated: Apr 5, 2026

Detection of Detergent-sensitive Interactions Between Membrane Proteins
Published on: March 7, 2018
A potential link between insulin signaling and GLUT4 translocation: Association of Rab10-GTP with the exocyst subunit
Hiroyuki Sano1, Grantley R Peck1, Stephanie Blachon2
1Department of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA.
Abstract:
Insulin increases glucose transport in fat and muscle cells by stimulating the exocytosis of specialized vesicles containing the glucose transporter GLUT4. This process, which is referred to as GLUT4 translocation, increases the amount of GLUT4 at the cell surface. Previous studies have provided evidence that insulin signaling increases the amount of Rab10-GTP in the GLUT4 vesicles and that GLUT4 translocation requires the exocyst, a complex that functions in the tethering of vesicles to the plasma membrane, leading to exocytosis. In the present study we show that Rab10 in its GTP form binds to Exoc6 and Exoc6b, which are the two highly homologous isotypes of an exocyst subunit, that both isotypes are found in 3T3-L1 adipocytes, and that knockdown of Exoc6, Exoc6b, or both inhibits GLUT4 translocation in 3T3-L1 adipocytes. These results suggest that the association of Rab10-GTP with Exoc6/6b is a molecular link between insulin signaling and the exocytic machinery in GLUT4 translocation.
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