Amino acid transporters of the SLC1 and SLC38 family play an essential role in regulating glutamine/glutamate concentration and metabolism in the central nervous system. The serum and glucocorticoid inducible kinase (SGK) is expressed in brain tissue and upregulated by ischemia, neuronal excitation and dehydration. The present work explored whether SGK protein kinases influence neuronal and glial sodium dependent amino acid transport and to elucidate the molecular mechanisms involved. Coexpression studies in Xenopus oocytes showed that the excitatory amino acid transporters EAAT1-5 are all activated by SGK isoforms and that they may be downregulated by the ubiquitin ligase Nedd4-2. The SGK effects are prevented upon disruption of the SGK consensus site present on various SLC38 transporters. As indicated by kinetic analysis and cell surface expression studies, SGK1 and Nedd4-2 regulate the respective amino acid transporters by modulating their abundance at the plasma membrane without altering their substrate affinity. In summary, SGK1 stimulates neuronal and glial amino acid transport by direct transporter phosphorylation as well as indirectly by inhibiting the ubiquitin ligase Nedd4-2. Thus SGK participates in the regulation of glutamate/glutamine transport under neuronal stress conditions.