Effect of Phosphorylation and O-GlcNAcylation on Proline-Rich Domains of Tau.

ABSTRACT: The microtubule-associated protein Tau (MAPT) is a phosphoprotein in neurons of the brain. Aggregation of Tau is the leading cause of tauopathies such as Alzheimer's disease. Tau undergoes several post-translational modifications of which phosphorylation and O-GlcNAcylation are key chemical modifications. Tau aggregates into paired helical filaments and neurofibrillary tangles upon hyperphosphorylation, whereas O-GlcNAcylation stabilizes the soluble form of Tau. How specific phosphorylation and/or O-GlcNAcylation events influence Tau conformations remains largely unknown due to the disordered nature of Tau. In this study, we have investigated the phosphorylation- and O-GlcNAcylation-induced conformational effects on a Tau segment (Tau_225-246) from the proline-rich domain (P2), b

SUBMITTER: Rani L 

PROVIDER: S-EPMC7459333 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature