The Impact of Inhibiting Palmitoylation of the DEK Protein on Cell Viability in Ovarian Cancer
Location
Oyate Hall
Event Website
https://2026undergraduateresearchsy.sched.com/event/2Ix8q/the-impact-of-inhibiting-palmitoylation-of-the-dek-protein-on-cell-viability-in-ovarian-cancer
Start Date
15-4-2026 6:00 PM
End Date
15-4-2026 8:00 PM
Description
Ovarian cancer is a highly lethal form of gynecologic cancer often found in advanced stages, and understanding the functions promoting cancer cell growth and survival is an important step towards developing treatments. Contributing to the success of ovarian cancer are mutations in DNA repair mechanisms that amplify cell growth activity and inhibit apoptosis. This form of overexpression is often seen in DNA repair proteins such as DEK. DEK is modified by the addition of a lipid through a process called palmitoylation, which increases DEK's regulatory activity. Palmitoylation is the reversible addition of a lipid, which can activate or deactivate certain DEK interactions; however, the role of this mechanism in cancer is poorly understood. The goal of this research is to identify the specific amino acid responsible for DEK palmitoylation, with the hypothesis that inhibiting this palmitoylation will reduce ovarian cancer cell viability in vitro. To do this, site-directed mutagenesis of DEK DNA was successfully performed to convert the amino acid cystine 200 to an alanine in the DEK protein sequence. From here, we will knock out the functional wild-type DEK within cells to replace it with the alanine 200 mutant and evaluate the response of cells to determine if inhibiting palmitoylation negatively impacts the growth and survival of ovarian cancer cells. The information from this research can further our understanding of the protein DEK and how its operation is involved in the persistence of ovarian cancer.
Publication Date
2026
The Impact of Inhibiting Palmitoylation of the DEK Protein on Cell Viability in Ovarian Cancer
Oyate Hall
Ovarian cancer is a highly lethal form of gynecologic cancer often found in advanced stages, and understanding the functions promoting cancer cell growth and survival is an important step towards developing treatments. Contributing to the success of ovarian cancer are mutations in DNA repair mechanisms that amplify cell growth activity and inhibit apoptosis. This form of overexpression is often seen in DNA repair proteins such as DEK. DEK is modified by the addition of a lipid through a process called palmitoylation, which increases DEK's regulatory activity. Palmitoylation is the reversible addition of a lipid, which can activate or deactivate certain DEK interactions; however, the role of this mechanism in cancer is poorly understood. The goal of this research is to identify the specific amino acid responsible for DEK palmitoylation, with the hypothesis that inhibiting this palmitoylation will reduce ovarian cancer cell viability in vitro. To do this, site-directed mutagenesis of DEK DNA was successfully performed to convert the amino acid cystine 200 to an alanine in the DEK protein sequence. From here, we will knock out the functional wild-type DEK within cells to replace it with the alanine 200 mutant and evaluate the response of cells to determine if inhibiting palmitoylation negatively impacts the growth and survival of ovarian cancer cells. The information from this research can further our understanding of the protein DEK and how its operation is involved in the persistence of ovarian cancer.
https://digitalcommons.morris.umn.edu/urs_event/2026/posters/3