Insulin stimulates glucose transport into adipocytes by enhancement of GLUT1 and GLUT4 glucose transporter abundance in the plasma membrane, an effect thought to be mediated by protein kinase B (PKB). The serum and glucocorticoid inducible kinase (SGK1) is similarly activated by insulin and capable to regulate cell surface expression of several metabolite transporters including GLUT1. To evaluate the putative role of SGK1 in the modulation of GLUT4 activity and expression, we heterologously expressed the kinase with or without the GLUT4 glucose transporter in Xenopus laevis oocytes. Coexpression of the kinase resulted in an increase of radiolabeled 2-deoxy-glucose uptake while coinjection of SGK1 in water injected control oocytes did not display any significant effect on intrinsic glucose transport. The enhanced GLUT4 activity was paralleled by and at least partially due to enhanced transporter abundance in the plasma membrane. Coexpression of the constitutively inactive mutant K127NSGK1 failed to modulate both GLUT4 activity and plasma membrane expression, indicating that SKG1 is effective through phosphorylation. In summary, SGK1 stimulates glucose transport by enhancing GLUT4 abundance in the cell membrane. The results suggest that SGK1 contributes to the stimulation of glucose uptake by insulin.