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C85 - Studying the interactions between monoubiquitinated CHIP with Hsp70
Protein quality control is essential for maintaining cellular function by regulating protein folding, activity, and degradation. Disruptions in this system can lead to the accumulation of misfolded proteins, contributing to diseases such as Alzheimer’s and Parkinson’s.
C85 - Studying the interactions between monoubiquitinated CHIP with Hsp70
Mentor: Rick Page, Ph.D.
Protein quality control is essential for maintaining cellular function by regulating protein folding, activity, and degradation. Disruptions in this system can lead to the accumulation of misfolded proteins, contributing to diseases such as Alzheimer’s and Parkinson’s.
This study investigates how autoubiquitination of CHIP, an E3 ubiquitin ligase, influences its interaction with the chaperone protein Hsp70. Using site-directed mutagenesis and ubiquitination assays, different CHIP variants were generated and analyzed. Protein interactions were measured using Bio-Layer Interferometry (BLI).
Results showed that wild-type CHIP exhibited polyubiquitination, while the CHIP9R mutant showed no ubiquitination, confirming successful mutation design. These findings suggest that specific lysine residues are critical for CHIP function and may influence its interaction with Hsp70.
This work provides insight into how protein regulation mechanisms contribute to cellular health and disease.