The most prominent function of the neuronal protein Tau is its binding to and stabilization of axonal microtubules in the brain. Infamous prominence of Tau arises from its intra-neuronal aggregation and accumulation in the brain in multiple neurodegenerative diseases, for example Alzheimer’s disease, Frontotemporal dementia, and others. Alike other proteins that accumulate in protein aggregation diseases, Tau in its soluble monomeric form is an intrinsically disordered protein (IDP), which structurally converts during aggregation and forms large amyloid-like fibrils. We recently described that liquid-liquid phase separation (LLPS) of Tau can initiate its conversion from IDP to aggregate, however, liquid condensed phases of Tau are also involved in other (patho)physiological functions of Tau. In this seminar, I will summarize the status quo of knowledge of liquid-like Tau phases and outline potential implications for neurobiology.


Tuesday, October 3, 2019, 12:00. Seminar Room

Hosted by Prof. Michael Krieg