Aldosterone-induced intestinal Na⁺ absorption is mediated by increased activities of apical membrane NHE3 (aNHE3) and basolateral membrane Na⁺-K⁺-ATPase (BLM-Na⁺-K⁺-ATPase) activities. Because the processes coordinating these events were not well understood, we investigated human intestinal Caco2BBE cells where aldosterone increases within 2-4 hrs apical NHE3 (aNHE3) and alpha subunit of BLM-Na⁺-K⁺-ATPase, but not total abundance of these proteins. Although aldosterone activated Akt2 and serum glucorticoid kinase-1 (SGK-1), the latter through stimulation of phosphatidyl-inositol-3-kinase (PI3K), only the SGK-1 pathway mediated its effects on Na⁺-K⁺-ATPase. Ouabain-inhibition of the early increase in aldosterone-induced Na⁺-K⁺-ATPase activation blocked most of the apical NHE3 insertion, possibly by inhibiting Na⁺-K⁺-ATPase-induced changes in [Na]_i. Over the next 6-48 hrs, further increases in aNHE3 and BLM-Na⁺-K⁺-ATPase activity and total protein expression were observed in large part mediated by aldosterone-activated serum glucorticoid kinase-1 (SGK-1) pathway. Aldosterone-induced increases in NHE3 mRNA, for instance, could be inhibited by RNA silencing of SGK-1, but not Akt2. Additionally, aldosterone-induced increases in NHE3 promoter activity were blocked by silencing SGK-1 as well as pharmacological inhibition of PI3K. In conclusion, aldosterone-stimulated intestinal Na⁺ absorption involves two phases. The first phase involves stimulation of PI3K which increases SGK-dependent insertion and function of BLM-Na⁺-K⁺-ATPase and subsequent increased membrane insertion of aNHE3. The latter may be caused by Na⁺-K⁺-ATPase-induced changes in [Na] or transcellular Na flux. The second phase involves SGK-dependent increases in total NHE3 and Na⁺-K⁺-ATPase protein expression and activities. The coordination of apical and BLM transporters after aldosterone stimulation is therefore a complex process that requires multiple time- and inter-dependent cellular processes.