Building new windows to view proteostasis in health and disease
Protein aggregation is a central pathological hallmark of most of the major neurodegenerative diseases. My lab has been developing new tools and approaches to understand the molecular sequence of events that leads up to intracellular aggregation and how this process negatively impacts on cellular functioning. The approaches have been from two fronts. First is unmasking which molecular changes can be attributed to distinct steps of the aggregation process using cellular models of Huntington Disease. Second is defining the effectiveness of protein homeostasis systems (or proteostasis) and how this is influenced under settings of protein folding stress and protein aggregation. I will discuss our unpublished new methods and approaches and surprising insights we found from these approaches that challenge some of the long standing dogmas in the field.
Biography: Danny Hatters runs a research program on the mechanisms of toxicity in neurodegenerative disease with a particular focus on building new molecular tools, and using these to decipher mechanisms of protein quality control, protein misfolding and aggregation in these diseases. Danny received his PhD from the University of Melbourne, 2002 and then undertook a postdoctoral fellowship at the Gladstone Institutes of Cardiovascular and Neurological Diseases and University of California, San Francisco. He rejoined the Department of Biochemistry and Molecular Biology at the University of Melbourne as the CR Roper Fellow in March 2007. In 2009 he was awarded a Grimwade Fellowship and then in 2012 an ARC Future Fellowship. In 2015 he was promoted to Associate Professor, and in 2017 appointed as Deputy Head of Department.