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SGK1 is a serine/threonine protein kinase induced by serum and glucocorticoids, first cloned as a gene upregulated by dexamethasone in rat mammary tumor cells. It is ubiquitously expressed in human tissues and regulates diverse cellular processes via phosphorylation of downstream proteins, including modulation of ion channels, cell survival, glucose uptake, apoptosis, proliferation, and immune responses. SGK1 plays a transducer role in multiple signaling pathways, notably PI3K-AKT and NF-κB. High SGK1 expression and activity are implicated in cancer progression, diabetic complications, cardiovascular diseases, neurological disorders, and infertility. It is considered a promising drug target, but currently lacks validated clinical inhibitors. The submitted query refers to a family rather than a single target, and the scientifically accurate name for therapeutic targeting is “Serum and glucocorticoid-regulated kinase 1 (SGK1)”[1][4][3][6][7][8].
Kinase inhibitors bind to the ATP-binding pocket or allosteric sites, blocking SGK1 phosphorylation activity. Modulation of signaling cascades such as PI3K-AKT-mTOR, NF-κB.
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