Computational modeling predicts that oligomerization of AKAP7γ may function to increase target phosphorylation. (a) Time course of target protein X phosphorylation for each oligomeric state. An increase in cAMP production is simulated from 0 to 100 s resulting in activation of AKAP bound PKA and phosphorylation of target protein X. The inset shows the change in [pX] from baseline to maximal phosphorylation relative to the change in phosphorylation produced by the monomeric state. (b) Time course of target X phosphorylation for a mixture of monomer and dimer as measured via PCH. The concentration of monomeric and dimeric AKAP complexes was adjusted so that 71.3% of the total AKAP exists as monomer and 28.7% exists as dimer. An increase in cAMP production was simulated as above. The inset shows the change in [pX] from baseline to maximal phosphorylation relative to 100% monomer.