PKA is an important class of kinases known as Arg-directed kinases or AGC family kinases, including cAMP-dependent protein kinases (PKA or cAPK), cGMP-dependent protein kinases (PKG), protein kinase C, Akt, and RSK. These kinases share a substrate specificity characterized by Arg at position 3 relative to the phosphorylated serine or threonine2-4. The second messenger cyclic AMP (cAMP) activates PKA in mammalian cells and controls many cellular mechanisms such as gene transcription, ion transport, and protein phosphorylation2.PKA is implicated in many cellular processes, including regulation of other protein kinases, regulation of intracellular calcium concentration, and regulation of transcription. The transcriptional response to increased cAMP is achieved through activation of cAMP response element binding protein (CREB), cAMP response element regulator (CREM) and activating transcription factor 1 (ATF1). Each of these transcription factors contains a kinase-inducible structural domain containing a conserved PKA phosphorylation site.