MAP2c (Microtubule associated protein 2c) is expressed in neuronal dendrites during embryonic brain development and is involved in the regulation of microtubule formation. Its C-terminal part shows high sequence similarity to the Tau protein, which forms aggregates in the brain of patients suffering from Alzheimer's disease. However, the localization of MAP2c and the assumed physiological roles of Tau and MAP2c differ. Both MAP2c and Tau are naturally disordered proteins that do not form stable three-dimensional structures. These two proteins are substrates of multiple kinases in vivo, which phosphorylate them at different Serine/Threonines. The phosphorylation of MAP2c and Tau regulates their binding to the microtubules and to different proteins important for neurons plasticity. The task of the student will be to express proline directed kinases, determine the phosphorylated sites on MAP2c using NMR, and study how the phosphorylation influences the binding to proteins interacting with MAP2c characterized in our laboratory.