Honors Theses and Capstones

Date Completed

Spring 2026

Abstract

Epichaperomes are long-lasting, stable assemblies of chaperones, co-chaperones, and associated factors that facilitate cell survival in maladaptive cellular states. Their inhibition has emerged as an attractive therapeutic strategy for the treatment of cancer and neurodegenerative diseases (Rodina et al., 2016). Epichaperomes are hallmarks of robust proliferation in cancer cell populations across many cancer types and are abundantly present in several stem cell varieties, including induced pluripotent stem cells, human embryonic kidney cells, and cancer stem cells (Kishinevsky et al., 2018).

The core protein of the eukaryotic heat shock protein machinery, Heat Shock Protein 90 (Hsp90), is a central chaperone that maintains proteostasis and exists in two major isoforms, Hsp90α and Hsp90β. In healthy cellular states, Hsp90β plays a greater role in embryonic development and proteostasis maintenance, whereas Hsp90α is more strongly associated with the DNA damage response (Maiti et al., 2022). Although the two isoforms share many overlapping functions, differences in their protein interactions and post-translational modifications within higher-molecular-weight complexes in embryonic stem cells, such as the E14 cell line, remain poorly understood.

In this proposed project, we will test the hypothesis that Hsp90α and Hsp90β engage in distinct protein interaction networks associated with isoform-specific functions and post-translational modifications. The findings from this work may provide insight into the functional specialization of Hsp90 isoforms and contribute to the development of more selective and personalized therapeutic strategies for cancer and neurodegenerative diseases.

Document Type

Undergraduate Thesis

First Advisor

Rick Cote

Second Advisor

Luke Botticelli

College or School

COLSA

Department or Program

Biochemistry, Molecular and Cellular Biology

Degree Name

Bachelor of Science

Download

Share

COinS