These results provide good examples of the importance of pre-existent and newly generated diversity in the adaptive capacity of populations, and illustrate how the relative amount of each of them determines whether a population needs to increase or reduce the mutation rate to get rapid adaptation. SGK must be phosphorylated on two residues before it is an active kinase, and mutation of one of these sites is sufficient to produce active SGK protein. The utility of these cells for virus propagation is at least three-fold. First, they are infectable by several diverse viruses, perhaps due to an abundant receptor repertoire, or non-specific uptake of virus particles. Second, they have sustained a genetic deletion that ablated the type I IFN locus. Third, Vero E6-encoded interferon regulatory factor 3, a transcription factor necessary for generating responses to virus infection, is relatively inefficient, resulting in a muted initial response to virus infection. For experimental purposes, hantavirus infectious stocks typically consist of the supernatants of infected Vero E6 cells and are used for in vivo and in vitro experiments. At the cellular level, virus infection is detected by interactions between host-encoded pattern recognition receptors and pathogen-associated molecular patterns. Receptor binding activates several well-characterized signaling cascades and results in the activation of type I IFN. More recently, type III IFNs have been described. These IFNs are comprised of three genes that encode proteins for IFNl1, IFNl2 and IFNl3. IFNl expression is controlled by pattern recognition receptor PRR activation, which activates and mobilizes IRF3 and IRF7, which in turn bind to the interferonstimulated response elements of these genes, along with several other genes. IFNls signal through a heterodimeric cell surface receptor comprised of IFNLR1 and IL10R2. Expression of the IFNLR1 is cell-type specific, with high expression in epithelial cells and little or no expression in endothelial and fibroblast cells, rendering the Pazopanib latter unresponsive to the effects of IFNl. Receptor engagement converges with that of the type I IFN receptors in that both activate the Jak/ STAT signaling pathway leading to the formation of ISGF3, a transcription factor that regulates the expression of several ISGs, including MxA. Therefore, both the expression and function of IFNls is much the same as for the type I IFNs. Here we show that SGKS422D binds more strongly to Nedd4-2 WW-domains compared to wildtype SGK, and that SGKS422D is more effective in stimulating Isc-amiloride in ENaC-transfected epithelia. Lack of activation of SGK is unlikely to be the cause of the difference in stimulation of current as the effect was similar in epithelia incubated in both serum-containing and serum-free media.