Abstract
Multisite protein phosphorylation plays a prominent role in intracellular processes like signal transduction, cell-cycle control and nuclear signal integration. Many proteins are phosphorylated in a sequential and distributive way at more than one phosphorylation site. Mathematical models of -site sequential distributive phosphorylation are therefore studied frequently. In particular, in {\em Wang and Sontag, 2008,} it is shown that models of -site sequential distributive phosphorylation admit at most steady states. Wang and Sontag furthermore conjecture that for odd , there are at most and that, for even , there are at most steady states. This, however, is not true: building on earlier work in {\em Holstein et.al., 2013}, we present a scalar determining equation for multistationarity which will lead to parameter values where a -site system has steady states and parameter values where a -site system has steady states. Our results therefore are counterexamples to the conjecture of Wang and Sontag. We furthermore study the inherent geometric properties of multistationarity in -site sequential distributive phosphorylation: the complete vector of steady state ratios is determined by the steady state ratios of free enzymes and unphosphorylated protein and there exists a linear relationship between steady state ratios of phosphorylated protein.
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