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cAMP-dependent Protein Kinase (PKA) is composed of two distinct subunits: catalytic (C) and regulatory (R). Four regulatory subunits have been identified: RIα, RIβ, RIIα, and RIIβ.These subunits define type I and II cAMP-dependent protein kinases. Following binding of cAMP, the regulatory subunits dissociate from the catalytic subunits, rendering the enzyme active. Type I and type II holoenzymes have three potential C subunits (Cα, Cβ, or Cγ). Type II PKA can be distinguished by autophosphorylation of the R-subunits, while type I PKA binds Mg/ATP with high affinity. Most cells express both type I and type II PKAs. Although the Rα isoforms are ubiquitously expressed, the Rβ isoforms are predominant in nervous and adipose tissues. There are indications that the deletion of the gene for PKA RIIβ results in lack of long-term potentiation in a select group of hippocampal cells, suggesting an important role for this protein in the neurosciences.Immunofluorescence, Immunoprecipitation, Western Blotting
