The dynamic instability of microtubules (MT) is an essential feature in eukaryotic cells and related to basic cellular processes such as intracellular transport, cell division, migration, or polarization. Microtubule-associated proteins (MAPs) are critically involved in such MT dynamics by binding to MTs and reshaping the molecular and structural organization.
Although the structure and dynamics of MTs, as well as the MT interactomic network have been intensively studied over the past decades, a detailed understanding on how different MAPs interact with MTs and how they jointly contribute to MT functioning in the cell remains largely elusive. For this reason, atomic level knowledge about the structural organization of MT-MAPs complexes is indispensable for understanding the mechanistic details of the MT interactome and its dynamic features.
In this thesis, my goal was to study the binding modes of specific MAPs to MTs, and on the other hand investigate structural and dynamical alternations of MTs that occur upon MAP binding. The studies presented in this thesis relied on the advancements in solid-state NMR (ssNMR) spectroscopy to study large protein complexes, including the use of 1H-detected ssNMR and dynamic nuclear polarization (DNP).