The role of small G-proteins in the regulation of glucose transport (review).
Insulin increases the rate of glucose transport into fat and muscle cells by stimulating the translocation of intracellular Glut 4-containing vesicles to the plasma membrane. This results in a marked increase in the amount of the facilitative glucose transporter Glut 4 at the cell surface, allowing for an enhanced glucose uptake. This process requires a continuous cycling through the early endosomes, a Glut 4 specific storage compartment and the plasma membrane. The main effect of insulin is to increase the rate of Glut 4 trafficking from its specific storage compartment to the plasma membrane. The whole phenomenon involves signal transduction from the insulin receptor, vesicle trafficking (sorting and fusion processes) and actin cytoskeleton modifications, which are all supposed to require small GTPases. This review describes the potential role of the various members of the Ras, Rad, Rho, Arf and Rab families in the traffic of the Glut 4-containing vesicles.
Cormont
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M
INSERM E99-11 and IFR 50, Faculté de Médecine, Nice, France. cormont@unice.fr
Le Marchand-Brustel
Y
Y
D020727:ADP-Ribosylation Factors / Q000378:metabolism; D000818:Animals; D001692:Biological Transport; D005947:Glucose / Q000378:metabolism*; D006801:Humans; D020559:Monomeric GTP-Binding Proteins / Q000378:metabolism*; D020691:rab GTP-Binding Proteins / Q000378:metabolism; D018631:ras Proteins / Q000378:metabolism; D020741:rho GTP-Binding Proteins / Q000378:metabolism
D020727:ADP-Ribosylation Factors; D020559:Monomeric GTP-Binding Proteins; D020691:rab GTP-Binding Proteins; D018631:ras Proteins; D020741:rho GTP-Binding Proteins; D005947:Glucose