Reactions and rate constants of signaling pathways in the model.

Rates were either obtained from the biochemical measurements, adjusted (adj) to reproduce other data, such as basal phosphoThr75-DARPP-32, or constrained by the thermodynamic principle of microscopic reversibility (PMR). R2C_cAMP4 is comprised of 2 regulatory PKA subunits and a single catalytic subunit.
*The cAMP saturated PKA holoenzyme likely binds to various targets at a lower rate than binding by the catalytic subunit [34]. Two types of reactions were added because NeuroRD is restricted to first or second order reactions:
&CaMKII phosphorylation reactions involving “Complex” are required to produce the observed calcium sensitivity [45], and capture the probability that two calmodulin bound CaMKII subunits are adjacent in the holoenzyme;
#Rapid dissociation after enzyme reaction prevents accumulation of these intermediate forms. PP2A_X indicate either BPR72 or B56d regulatory subunit. Phosphorylation of Ser845 and Ser831 are independent of each other, thus only one of two possible reactions are listed. Similarly, dephosphorylation of Ser831 is independent of whether Ser845 is phosphorylated or not, and dephosphorylation of Ser845 by calcineurin is independent of Ser831 phosphorylation.