Compartmental exchange regulates steady states and stochastic switching of a phosphorylation network.

ABSTRACT: The phosphoregulation of proteins with multiple phosphorylation sites is governed by biochemical reaction networks that can exhibit multistable behavior. However, the behavior of such networks is typically studied in a single reaction volume, while cells are spatially organized into compartments that can exchange proteins. In this work, we use stochastic simulations to study the impact of compartmentalization on a two-site phosphorylation network. We characterize steady states and fluctuation-driven transitions between them as a function of the rate of protein exchange between two compartments. Surprisingly, the average time spent in a state before stochastically switching to another depends nonmonotonically on the protein exchange rate, with the most frequent switching occurring at interm

SUBMITTER: Schmidt HN 

PROVIDER: S-EPMC10938077 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature