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Protein kinase A (PKA) is a serine/threonine kinase that is regulated by its R subunits. The best-characterized feature of R subunit function is its ability to be phosphorylated by the catalytic subunit (C) and this is a shared feature of all R subunits. However, despite this common feature of all R subunits, PKA regulated by different R subunits can generate strikingly different actions, including stimulation or inhibition of C. Here, we use rational mutagenesis to selectively mimic phosphorylated and unphosphorylated R subunits. This approach enabled us to show that the unphosphorylated R subunits of PKA are kinase inhibitors, as well as kinase activators. The transition from inhibition to stimulation takes place as the phosphorylation of residue Ser-190 of the R subunits by C destabilizes a negative charge clamp.techo
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