J. Paul Taylor, MD, PhD
Investigator, Howard Hughes Medical Institute, Chair, Cell & Molecular Biology Department, Director, St. Jude Translational Neuroscience Initiative, Edward F. Barry Endowed Chair in Cell and Molecular Biology, St. Jude Children’s Research Hospital

Abstract:
Ribonucleoprotein (RNP) granules are a diverse group of RNA-protein assemblies that populate the nucleus, cytoplasm and distal processes of complex cells such as neurons. RNP granule assembly exerts temporal and spatial control over much of RNA metabolism, such as splicing and other processing events in the nucleus, and translation and RNA stability in the cytoplasm and in distal processes. Paradigm-shifting advances over the past 8 years has revealed that RNP granules assemble via liquid-liquid phase separation. The driving forces for phase separation arise from a diverse set of protein-protein, protein-RNA and RNA-RNA interactions that are a hotspot for genetic mutations causative of ALS and related neurodegenerative diseases. In my talk I will present evidence generated in my lab over the last 8 years indicating that the defect underlying many forms of ALS and FTD is disturbance of phase transitions that alters the dynamic properties of RNP granules.