Regulation of phosphorylation of neuronal MAP2c protein by GSK3 beta and the effect of phosphorylation on its interaction with apolipoprotein E3

Róbert Šándor

(presentation of BINFO Master's Degree Programme)

Abstract:

Cytoskeletal microtubule-associated proteins (MAPs) regulate the stability and dynamics of the microtubules. Inside the neurons, the occurrence of various MAPs differs.
Microtubule-associated protein 2 (MAP2) is found in cell bodies and dendrites. It is classified as an intrinsically disordered protein (IDP) and plays a vital role in neuronal development. MAP2 is subject to frequent post-translational modifications, in particular phosphorylation by various protein kinases. We utilized NMR spectroscopy to investigate the phosphorylation of the juvenile form of MAP2, MAP2c, by Ser/Thr kinase glycogen synthase kinase 3 beta (GSK 3 beta) and observed the influence of phosphorylation on its interaction with the N-terminal domain of apolipoprotein E3.