Document Type
Text
Publication Date
1-2025
Abstract
All biological functions in living organisms depend on the activity of proteins, long molecules that must twist and fold into specific shapes to become functional. A subset of proteins known as molecular chaperones is essential for maintaining cellular health by assisting other proteins in folding correctly and refolding those damaged by stress. When proteins misfold and clump together, they can form toxic aggregates linked to many neurodegenerative diseases, including Alzheimer’s disease (AD), one of the leading causes of death in the United States. In AD, these protein aggregates form organized, elongated structures referred to as amyloid-like fibrils, which damage neurons and lead to memory loss and brain dysfunction. One molecular chaperone, DNAJB1, can recognize and facilitate breaking apart these fibrils. DNAJB1 belongs to a family of helper proteins to another chaperone, Hsp70, and exists in cells as a stable pair of identical units, so-called homodimer. However, how both units cooperate with Hsp70 and contribute to processing the neurodegenerative-specific protein aggregates remains unclear, and this is the focus of my research. To begin exploring how the two units behave within the homodimer, we need the ability to alter them individually. To form a "heterodimer," where only one unit is modified and the other remains intact, we must first prevent uncontrolled homodimerization and then precisely regulate which units can pair together. Here, I present my work on creating two types of DNAJB1 units, both lacking the ability to homodimerize, yet able to form a heterodimer when mixed with each other. I also conducted a series of tests to verify their activity and ability to interact with Hsp70. This approach represents a first step toward uncovering how the two DNAJB1 units collaborate—and how they work with Hsp70—to dismantle harmful protein aggregates that contribute to diseases like Alzheimer’s.
Recommended Citation
Kotreli, Erina; Le, Trang; and Ciesielski, Szymon, "The Relevance of DNAJB1 Protein Dimerization Against the Human Neurodegenerative Diseases" (2025). Dean's Leadership Council Library Research Prize. 9.
https://digitalcommons.unf.edu/dlc_research_prize/9
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
Comments
Winner (Undergraduate) Spring, 2026 DLC Library Research Prize Cycle