Submission Date

5-1-2026

Document Type

Paper- Restricted to Campus Access

Department

Biology

Adviser

Erica Gorenberg

Committee Member

Martha Davis

Committee Member

Erin Benfer

Department Chair

Denise Finney

External Reviewer

Edward Barbieri

Distinguished Honors

This paper has met the requirements for Distinguished Honors.

Project Description

Correct protein folding is essential for maintaining structural integrity and biological function, whereas misfolded proteins can form toxic aggregates that contribute to disease. One mechanism of aggregation is liquid-liquid phase separation (LLPS), a process that creates dense protein droplets that can undergo a liquid-to-solid phase transition, resulting in insoluble aggregates that disrupt downstream cellular processes. Proteins such as TDP-43 and FUS are amongst the most prominent aggregating proteins associated with amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). In TDP-43, the low complexity domain (LCD) is the main region responsible for LLPS, making it crucial for further investigation. Research has identified the DnaJ/Hsp40 family of proteins to have unique disaggregase abilities that can counteract this aggregation. This study utilizes yeast as a model organism to investigate whether the LCD of TDP-43 can mediate the targeting of other proteins to TDP-43 aggregates. Red and green fluorescent proteins were tagged to TDP-43 and its LCD region respectively to visualize if colocalization can occur. We hypothesize that the LCD of TDP-43 will drive fusion proteins towards TDP-43, which will be visualized via the colocalization of fluorescent proteins and their respective tag using fluorescent microscopy.

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