My research characterizes molecular mechanisms related to a fatal, incurable disease called ALS (Lou Gehrig's Disease). We cannot yet cure ALS because we do not understand what causes it in the majority of cases. A hallmark of ALS is the appearance of protein clumps called aggregates within motor neurons. We do not know what leads to this protein aggregation, and elucidating this process may help us identify the cause of ALS. Several types of dynamic, membraneless bodies called biomolecular condensates that form within cells have been linked to ALS pathology. My research characterizes assembly and disassembly of condensates called stress granules that are hypothesized to become aggregates if they persist. I also study a protein called Ubiquilin-2 that can cause inheritable ALS when mutated. I demonstrate that UBQLN2 forms condensates in response to cellular stress, and show that ALS-linked mutations in UBQLN2 alter the assembly and properties of these condensates.

Links to Project Materials:

Additional support provided by: Honors Funding

College of Arts & Sciences 2020, Natural Science & Engineering Projects 2020