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BP: Fachverband Biologische Physik

BP 20: Regulation

BP 20.9: Vortrag

Donnerstag, 29. März 2012, 12:00–12:15, H 1058

Modeling MARCKS and Protein Kinase C binding at cellular membranes — •Sergio Alonso and Markus Bär — Physikalisch-Technische Bundesanstalt, Abbestrasse 2-12, 10587 Berlin, Germany

Phosphorylation and dephosphorylation of proteins are mechanisms of activation and deactivation which regulate many cell processes. MARCKS is a protein which binds to the membrane by electrostatic interaction. It is phosphorylated by Protein Kinase C and translocated from the membrane. In the cytoplasm phosphorylated MARCKS is dephosphorylated by phosphatases and can bind again at the membrane. The three processes give rise to a cyclic dynamics known as myristoyl-electrostatic switch. We propose a reaction-diffusion model obeying mass conservation for the binding, phosphorylation and dephosphorylation of MARCKS proteins. Furthermore, we add to the model the dynamics of binding and unbinding of PKC enzymes, which are activated by spikes of calcium.