Rui YinFollow

Date Thesis Awarded


Access Type

Honors Thesis -- Access Restricted On-Campus Only

Degree Name

Bachelors of Science (BS)




Oliver Kerscher

Committee Members

Diane C. Shakes

Phoebe Williams

Douglas D. Young


SUMO (Small Ubiquitin-like Modifier) is a small protein that becomes reversibly attached to a large number of proteins. While research has firmly established SUMO’s importance in modulating protein interactions, activation, targeting, and half-life, little is known about its role in the SUMO-Stress Response (SSR), a phenomenon that involves a rapid increase in SUMOylation in response to cellular stress. Here I describe the use of kmUTAG-fl, a novel fluorescent SUMO trapping UTAG protein, to characterize and study how the SSR unfolds in normal and carcinogenic tissue culture cells. Specifically, fixed cells were stained with the SUMO-conjugate specific kmUTAG-fl reagent to record and quantitate differences between normal (PNT2) and carcinogenic cells (PC3). While both types of cells displayed grossly altered SUMO level, carcinogenic cells featured a more rapid and reproducible increase of SUMOylation in both the nucleus and the cytosol. This elevated SSR, potentially unique to carcinogenic cells, may represent a novel hallmark of cancer and the implications of this finding are discussed.

On-Campus Access Only