| Phosphorylation and dephosphorylation of proteins are mechanisms of activation and deactivation which regulate many cell processes. Some of such reactions or some molecules are restricted to particular compartments of the cell and, therefore, the spatio-temporal distribution of the proteins in the cell may be important. MARCKS are proteins which bind at the membrane by electrostatic interaction. They lost the interaction with the membrane under phosphorylation by Protein Kinase C. In the cytoplasm phosphorylated MARCKS are dephosphorylated by phosphatases and they can bind again at the membrane. The three processes give rise to a cyclic dynamics known as myristoyl-electrostatic switch. We propose a mass-conserved reaction-diffusion model for the binding, phosphorylation and dephosphorylation of MARCKS proteins. The model predicts the formation of domains with high concentration of MARCKS proteins at the membrane. The generation of such domains in living cells produces their polarization. In general, the formation of patterns at the membrane is the initial ingredient to produce the autonomous motion of a cell. |
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