SGK1 is a member of the serum- and glucocorticoid-induced protein kinase that is activated in vitro by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and in vivo in response to signals that activate phosphatidylinositol (PI) 3-kinase. SGK1 mRNA is expressed in all tissues and the level of SGK1 mRNA is increased by stimulation with serum or dexamethasone. SGK1 promotes cell survival by phosphorylating and inactivating FKHRL1. SGK and Akt display differences with respect to the efficacy with which they phosphorylate the three regulatory sites on FKHRL1.
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Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.2 5mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.
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Molecular and cellular biology, 21(3), 952-965 (2001-01-12)
Serum- and glucocorticoid-inducible kinases (SGKs) form a novel family of serine/threonine kinases that are activated in response to a variety of extracellular stimuli. SGKs are related to Akt (also called PKB), a serine/threonine kinase that plays a crucial role in
The Biochemical journal, 344 Pt 1, 189-197 (1999-11-05)
The catalytic domain of serum- and glucocorticoid-induced protein kinase (SGK) is 54% identical with protein kinase B (PKB) and, like PKB, is activated in vitro by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and in vivo in response to signals that activate phosphatidylinositol
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