The goals of my research program are to determine the molecular mechanisms underlying formation, function, and clearance of amyloid-like structures. Additionally, I plan to develop yeast meiosis as a tool for screening for anti-amyloid compounds. Amyloids are fibrous protein deposits best known for their association with a variety of human neurodegenerative diseases. Although amyloids have been predominantly understood in pathological contexts as toxic protein deposits and/or metabolic byproducts, amyloid-like structures are beginning to be recognized as having critical physiological functions. I previously found that yeast cells assemble proteins into structures that share many properties of amyloid as an essential feature of reproductive cell division (i.e. meiosis). Due to the biochemical similarity these structures have with disease-related amyloid they are termed 'amyloid-like.' Research in my lab in part focuses on understanding yeast's remarkable ability to efficiently regulate both assembly and clearance of amyloid-like structures during meiosis. Yeast meiosis is unique as an experimental system in that one can grow cultures of cells that synchronously produce and clear amyloid-like structures in coordination with developmental cues. Each finding provides the potential lead to a pathway or gene that could be a therapeutic target. Furthermore, yeast cells build amyloid-like structures to serve a critical function, which is to repress translation of critical mRNA transcripts. I use a combination of in vitro and in vivo approaches to decipher the mechanisms by which these repressor complexes bind and repress mRNA. I will further investigate my lab's discoveries from yeast in animal and cell culture disease models with the goal of ultimately translating our findings into human health benefits.