Assistant professor Wei Dai has received a CAREER award from NSF to study structural organization of phase transition assemblies formed by proteins with extended polyglutamine (polyQ) homo-repeats. PolyQ proteins are associated with Huntington’s Disease (HD) and at least eight other human neurodegenerative diseases. They are one of the simplest intrinsically disordered proteins (IDPs) that can condense into membraneless liquid-like or gel-like assemblies through a process termed phase transition. At present, it remains a mystery how the ultrastructure of phase transition assemblies supports spatiotemporal control of functions of the enclosed proteins. By applying cutting edge bioimaging of cryo-electron tomography and 3D ultrastructure analysis, this project will assess how the formation of polyQ protein phase transition assemblies are affected by cellular factors such as lipid vesicles, and provide a deeper understanding of how biophysical and structural properties of phase transition assemblies support biological activities of enclosed IDPs. This project also includes a research-driven education component that will introduce interdisciplinary research to undergraduates, and provide engaging online training resources on biostructure imaging to undergraduate and graduate students. This grant will start in Jan. 2021 and run through 2025.