Aims: The activity of SGK1 (serum and glucocorticoid-inducible kinase 1) is dependent upon the phosphorylation of SGK1- Ser⁴²² by TORC2 (target of rapamycin complex 2) (García-Martínez & Alessi, 2008) and, since SGK1 may allow insulin to stimulate Na+ absorption in the distal nephron (Huang et al., 2006), we now explore the effects of a novel TORC1/2 inhibitor (PP242) upon insulin-induced Na+ transport in cortical collecting duct cells. Methods. Confluent mpkCCD cells were mounted in Ussing chambers to study the effects of PP242 and rapamycin upon insulin-evoked Na transport whilst endogenous SGK1 activity was assayed by monitoring (Western analysis) the phosphorylation of residues within the protein encoded by the n-myc downstream regulated gene 1 (NDRG1-Thr^346/356/366) that are phosphorylated by SGK but not by other kinases (Murray et al. 2005). Results. Insulin (20 nM, 30 min) normally stimulated electrogenic Na absorption and increased the phosphorylation of NDRG1-Thr^346/356/366, and it is therefore clear that insulin-induced Na transport is associated with activation of SGK1. PP242 (1 M, 30 min preincubation) essentially abolished insulin-induced Na transport and also caused complete dephosphorylation of NDRG1- Thr^346/356/366 in both unstimulated and insulin stimulated cells. A selective inhibitor of TORC1 (rapamycin, 0.1 mM, 30 min preincubation) had no effect upon these parameters and these effects of PP242 cannot, therefore, be attributed to effects upon this kinase. Conclusion. TORC2 inhibition inactivates SGK1 and blocks insulin-induced Na absorption and compounds that inhibit TORC2 may thus provide a means of treating the salt sensitive hypertension that can complicate the clinical management of type 2 diabetes. Huang DY et al. (2006). Am J Physiol Regul Integr Comp Physiol 290, R935-R944. García-Martínez JM, Alessi, DR (2008). Biochem. J. 416, 375-385. Murray, J.T. et al. (2005). Biochem. J. 385, 1- 12.