Background/Aim: Expression of the constitutively active form of serum and glucocorticoid-dependent kinase (<sup>S422D</sup>SGK1) in Xenopus oocytes has recently been shown to upregulate endogenous Na<sup>+</sup>/K<sup>+</sup>-ATPase activity, an effect presumably participating in the regulation of cellular K<sup>+</sup> uptake and transepithelial Na<sup>+</sup> transport. SGK1 and the two isoforms SGK2 and SGK3 are stimulated by insulin and insulin-like growth factor-1 (IGF-1), which have been shown to enhance Na<sup>+</sup>/K<sup>+</sup>-ATPase activity in a variety of cells. The present experiments have been performed to elucidate whether or not wild-type SGK1, SGK2 and SGK3 are similar to <sup>S422D</sup>SGK1 in being effective regulators of Na<sup>+</sup>/K<sup>+</sup>-ATPase. Methods: To this end, dual-electrode voltage clamp experiments were performed in Xenopus oocytes injected either with water or with mRNA of constitutively active <sup>S422D</sup>SGK1 and wild-type SGK1, SGK2 or SGK3. Na<sup>+</sup>/K<sup>+</sup>-ATPase activity was estimated from the outward-directed current created by readdition of extracellular K<sup>+</sup> in the presence of K<sup>+</sup> channel blocker Ba<sup>2+</sup> following a 10-min exposure to K<sup>+</sup>-free extracellular fluid. Results: The outward-directed current was fully abolished by incubation with 1 m M ouabain and was significantly larger in oocytes expressing <sup>S422D</sup>SGK1, SGK1, SGK2 or SGK3, as compared to those injected with water. Conclusion: The stimulating effect of SGK1 on the Xenopus oocyte Na<sup>+</sup>/K<sup>+</sup>-ATPase is mimicked by the isoforms SGK2 and SGK3. Thus, all three kinases may participate in the regulation of Na<sup>+</sup>/K<sup>+</sup>-ATPase activity by hormones such as insulin and IGF-1.