Serum- and glucocorticoid-regulated kinase (SGK), also known as SGK1, is a serine/threonine protein kinase and a member of the "AGC" subfamily, which includes protein kinases A, G, and C. SGK plays an important role in activating certain potassium, sodium, and chloride channels, suggesting an involvement in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion. SGK contains a catalytic domain, which is most similar to Akt1 (also known as protein kinase B or PKB). SGK is a downstream target of PI 3-kinase-stimulated growth factor signaling, with 3-phosphoinositide-dependent protein kinase 1 (PDK1) capable of phosphorylating the activation-loop of SGK at Threonine-256. The adrenal corticosteroid hormone, Aldosterone, induces the transcription of SGK, which mediates Na + transport by stimulating epithelial sodium channel activity. The SGK promoter contains a glucocorticoid response element and an SP-1 regulatory element, and is a transcriptional target for p53. SGK is also a component of the p38 MAPK-mediated response to hyperosmotic stress. The human SGK gene maps to chromosome 6q23 and encodes the 431-amino acid SGK protein.

1. Anacker C et al. Role for the kinase SGK1 in stress, depression, and glucocorticoid effects on hippocampal neurogenesis. Proc Natl Acad Sci U S A 110:8708-13 (2013).
2. Costin BN et al. Ethanol regulation of serum glucocorticoid kinase 1 expression in DBA2/J mouse prefrontal cortex. PLoS One 8:e72979 (2013).