Protein SUMOylation: an emerging pathway in Alzheimer’s Diseases

Venue: Edificio Povo 2, via Sommarive nr. 9, Povo (Tn) - Room B105
 at 2:00 p.m.

• Marco Feligioni -  European Brain Research Institute (EBRI), Laboratory of Synaptic Plasticity, Rome, Italy.

Small ubiquitin-like modifier (SUMO) conjugation and binding to target proteins regulate a wide variety of cellular pathways. The functional aspects of SUMOylation include changes in protein-protein interactions, intracellular trafficking as well as protein aggregation and degradation. SUMO has also been linked to specialized cellular pathways such as neuronal development and synaptic transmission. In addition, SUMOylation is associated with neurological diseases linked with abnormal protein accumulations such as Alzheimer’s disease and other tauopathies, Huntington’s disease, Amyotrophic Lateral Sclerosis, etc. SUMO may contribute to the changes in protein solubility and proteolytic processing. Our research focuses on understanding how protein SUMOylation contributes to the onset and progression of Alzheimer’s disease and how SUMOylation unbalance can affect synaptic transmission.