Aims: Migration requires cellular Ca²⁺ entry which may be accomplished by Orai1, the pore forming protein mediating the store operated, calcium release-activated calcium current (I_CRAC). Upon depletion of the intracellular calcium stores Orai is activated by the calciumsensor molecule STIM1. Most recently, mast cell I_CRAC and degranulation have been shown to critically depend on the serum- and glucocorticoid-inducible kinase 1 (SGK1). The present study thus explored the contribution of SGK1 to the regulation of Ca²⁺ dependent migration. Methods: Experiments were performed in human embryonic kidney (HEK) cells stably expressing STIM1 and transfected with Orai1 and/or SGK1. Orai1 protein abundance in the cell membrane was determined by confocal microscopy, migration determined by transwell assays and cytosolic Ca²⁺ activity by Fura 2 fluorescence. In an additional series of experiments, migration was determined utilizing fibroblasts from SGK1 knockout mice (sgk1^-/-) and fibroblasts from their wild-type littermates (sgk1^+/+). Results: Surface expression of Orai1 was enhanced by additional expression of STIM1 and further enhanced by additional expression of constitutively active ^S422DSGK1. Expression of inactive ^K127NSGK1 decreased Orai surface expression. Similarly, migration was significantly enhanced by additional expression of STIM1 and ^S422DSGK1, and decreased by additional expression of ^K127NSGK1. Migration was significantly blunted in sgk1^-/- fibroblasts as compared to sgk1^+/+ fibroblasts. Conclusion: These observations disclose a decisive role for SGK1 in the regulation of Orai1, Ca²⁺ entry and migration.