The type II cAMP-protein kinase (PKA) is a multifunctional kinase with a broad range of substrates (1). Specificity of PKA signaling is thought to be mediated by the compartmentalization of the kinase to specific sites within the cell. To maintain this specific localization, the R subunit (RII) of PKA interacts with specific RII-anchoring proteins. This family of proteins has been designated A-kinase anchoring proteins (AKAP) (1-3). Members of this family, including MAP2 (microtubule-associated protein 2), neuronally expressed AKAP 79 and AKAP 150, and the DNA binding AKAP 95, display differential tissue specificity and localization (4-6). Evidence suggests that AKAP 79 and AKAP 150 are both capable of anchoring PKA to postsynaptic densities (PSD), which are a network of proteins located on the internal surfaces of excitatory synapses。