Cytoskeletal microtubule-associated Proteins (MAPs) are proteins important for regulating the stability and dynamics of the microtubule. MAP2 and Tau are brain MAPs, MAP2 is localized in dendrites, whereas Tau is localized in axons. 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. We have previously expressed functional GSK3 kinase in our lab, and recorded the phosphorylation of MAP2c by NMR, revealing more than 10 phosphorylation sites on MAP2c. Possible phosphorylation sites were determined by mass spectrometry, and several phosphorylation sites were assigned, mainly in the C-terminal domain of MAP2c using NMR. The task of the student would be to complete the assignement of the residues phosphorylated by GSK, using MAP2c mutants where possible phosphorylation sites have been deleted, and NMR spectra used for assignment. The kinetics of phosphorylation of the different sites will then be determined. The student would also determine how phosphorylation by other kinases such as PKA or ERK2 could regulate the activity of GSK3. The second part of the thesis would be to determine how GSK3 may interfere with binding of MAP2c with interacting partners.