• aggregation
• gene expression
• nuclear Tau
• tauopathies
• VGluT1.

The thesis focuses on the study of the Tau P301S mutant, involved in Frontotemporal Dementia, and the Tau Q336H mutant, involved in Pick’s Disease. By imaging experiments, I observed that Tau P301S is able to aggregate both in the cytoplasm and in the nucleus in amyloidogenic structures. Further experiments suggested that nuclear aggregation is mainly due to the self-assembly of the nuclear Tau and not to the translocation of cytoplasmic aggregates into the nucleus. Since our group previously demonstrated that nuclear Tau modulates the expression of VGluT1, a disease-related gene, I evaluated its expression following aggregation.
In this project I also analysed the novel Tau mutant Q336H characterized by unusual behaviour. By FRAP experiments I observed that it is more stably bound to microtubules than wild-type Tau. Despite this, by performing an aggregation assay, I observed the formation of aggregates similar to those formed with other Tau mutants.