Aldosterone effects on Na+ transport in the kidney tubules require new gene transcription, none-the-less, they occur fairly rapidly, with increased Na+ current detectable in < 30 min. SGK1 is one of the most rapidly responding aldosterone-regulated genes, with changes in mRNA level within 10 min, and changes in protein within 20 min. Furthermore, SGK1 is under dual regulation: its protein levels are controlled through aldosterone-dependent changes in transcription, and its activity is controlled by rapid kinase cascades. Recently, significant progress has been made in elucidating these kinase cascades, which alter SGK1 activity in seconds-to-minutes. Notably, SGK1 has two phosphorylation sites—termed the “activation loop” and “hydrophobic motif”, which undergo regulated phosphorylation by PI3-kinase and mTOR, respectively. Our recent work indicates that mTOR-mediated phosphorylation is essential for specific activation of SGK1 under conditions in which other similar kinases are not activated. mTOR is found in two major complexes, mTORC1 and mTORC2. SGK1 is recruited specifically to mTORC2 by an mTORC2 component, mSin1. This interaction is necessary for SGK1 activation, but not activation of other kinases that are activated by mTOR; notably Akt, which is also phosphorylated by mTORC2 does not interact with mSin1. This regulatory cascade is essential for activation of the epithelial sodium channel (ENaC). Thus, SGK1 serves as a key integrator of multiple signals, which feed into aldosterone-dependent regulation of sodium transport in the kidney tubules.