Boncella, Amy E., authorRoss, Eric D., author2017-11-132017-11-132017https://hdl.handle.net/10217/184833Mutations in a number of stress granule-associated proteins have been linked to various neurodegenerative diseases. Several of these mutations are found in aggregation-prone intrinsically disordered domains (IDRs) of these proteins. My studies have focused on two IDR-containing yeast stress granule proteins, Pab1 and Pbp1. I have introduced mutations designed to enhance aggregation of these proteins and observed effects on stress granule dynamics. Results suggest that these mutations affect IDR localization in the context of overexpression, but do not affect stress granule dynamics in an endogenous system. This has led to questions about how the proteostasis machinery affects stress granule dynamics.born digitalStudent workspostersengCopyright and other restrictions may apply. User is responsible for compliance with all applicable laws. For information about copyright law, please see https://libguides.colostate.edu/copyright.Text