Microtubule associated protein 2c (MAP2c) is a key factor regulating microtubule dynamics in
developing brain neurons, and an example of an intrinsically disordered proteins with an
important physiological function and detectable structure-function relationship. We propose to
study interactions of MAP2c defining and controlling its biological function. We focus on two
regions in the N-terminal half of MAP2c sequence that bind molecules not interacting with the
homologous protein Tau and contain structural motifs unique for MAP2c and not found in Tau.
We will study interactions with steroids, regulatory subunit of kinase PKA, plectin, and evaluate
effects of phosphorylation and interactions with regulatory 14-3-3 proteins. We also propose to
study impact of the interactions on microtubule binding and address biological relevance of the
in vitro results by recording NMR spectra at near-to-native conditions (in cells and/or cell
lysates) and performing cryo-electron tomography on monolayered neurons to observed
interactions of cytoskeleton components regulated by MAP2c binding in situ.

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