Impact of the AT8 epitope phosphorylation on Tau aggregation, propagation, and neurotoxicity
Charbel Chahla, Fabrice Parat, Diane Allegro, Nicolas Julien, Pascale Barbier, Lotfi Ferhat, Herve Kovacic · FENS Forum 2024
Tau, is an intrinsically disordered protein crucial for stabilizing and polymerizing microtubules (MTs). However, in Alzheimer's disease (AD), Tau undergoes hyperphosphorylation, leading to its misfolding and detachment from MTs, forming droplets termed liquid-liquid phase separation (LLPS), believed to be a precursor to Tau aggregates. Despite being a biomarker for AD, the role of AT8 phosphorylation (S202, T205, and S208) in Tau spread and toxicity remains unclear. To address this issue, we generated Tau variants with different AT8 phosphorylation states: PTau 2A-, 208- (lacking AT8 phosphor
ePoster · Neuroscience