Induction of cAMP results in the activation of the cAMP-dependent protein kinase (PKA) which, in turn, phosphorylates and regulates downstream effectors. The localization and, hence, the specificity of PKA action is mediated by the interaction of four different PKA regulatory subunits (RIα, RIβ, RIIα, and RIIβ) and specific PKA anchoring proteins. Several proteins have been identified as PKA type I/II anchoring proteins and form a family named AKAP (A-Kinase Anchor Proteins). Several AKAPs (AKAP79/75, AKAP350, and AKAP250) associate with PKA type II and direct its localization to cortical actin, centrosomes, and filopodia. AKAP95 is a specific nuclear anchoring protein that contains two zinc finger motifs and an RII binding domain. Although AKAP95 does not interact with RIIβ, it has a high affinity for RIIα. During interphase, AKAP95 is bound to DNA. However, entry into mitosis results in AKAP95 detachment from the DNA and association with RIIα. Although the specific function of this AKAP95/RIIα heterodimer is unknown, its formation is cell cycle-dependent and may be essential for proper progression through the cell cycle.