Reversible receptor phosphorylation model

Protein kinase activity adds modification, while protein tyrosine phosphatase activity can remove it. An original one-site model shows why a receptor phosphorylation assay cannot determine either process from a single modified fraction. Let $f(t)\in [0,1]$ be the fraction of a fixed receptor population carrying one selected phosphotyrosine residue. Stipulate constant effective first-order rate constants $k_{+},k_{-}>0$, with ATP availability absorbed into $k_{+}$, and no receptor synthesis, degradation or trafficking:Here $f_{\ast }$ is the steady state fraction and $\tau$ the time constant. The ordinary differential equation has the exponential function solutionThe balance equation and a single relaxation step give this result; it is an illustrative model, rather than a fit or a claim about every RTK.

With stipulated rate constants $(k_{+},k_{-})=(2,1){\min }^{-1}$, $f_{\ast }=2/3$ and $\tau =1/3\min$. Doubling both rate constants leaves $f_{\ast }=2/3$ but changes $\tau$ to $1/6\min$. The balanced phosphate turnover per site,doubles from $2/3$ to $4/3{\min }^{-1}$. Identical steady state modification therefore permits different catalytic fluxes. Removing the addition term instead gives $f(t)=f(0)e^{-k_{-}t}$; this illustrates why a perturbation that stops protein kinase activity can expose removal dynamics, subject to the model's unchanged-removal assumption. A maintained steady state with ongoing ATP consumption is not chemical equilibrium.