Protein kinases catalyze the phosphorylation of serine/threonine or tyrosine residues, which may directly alter a protein's functional properties. Kinases can also regulate protein functions indirectly, for example, by controlling the composition and/or subcellular localization of members of multiprotein complexes that associate with the regulated protein. In this issue of the JCI, two separate studies by Weinman et al. and Yang et al. examine the second of these two modes of kinase-mediated regulation and demonstrate the effects of kinases on two Na(+)-driven renal cotransporters (see the related articles beginning on pages 3403 and 3412). Their results reveal important implications for phosphate and salt homeostasis, respectively.