Mical modulates Tau toxicity via cysteine oxidation in vivo
Engie Prifti, Eleni Tsakiri, Ergina Vourkou, George Stamatakis, Martina Samiotaki, Euthimios M.C. Skoulakis, Katerina Papanikolopoulou · FENS Forum 2024
Tau accumulation is clearly linked to pathogenesis in Alzheimer’s disease and other Tauopathies. However, processes leading to Tau fibrillization and reasons for its pathogenicity remain largely elusive. Mical emerged as a novel interacting protein of human Tau expressed in Drosophila brains. Mical is characterized by the presence of a flavoprotein monooxygenase domain that generates redox potential with which it can oxidize target proteins. In the well-established Drosophila Tauopathy model, we use genetic interactions to show that Mical alters Tau interactions with microtubules and the Actin