The proteasome is a multi-catalytic complex that is responsible for protein degradation in eukaryotic cells. Cellular stress can be caused in diseases that lead to the over production or buildup of misfolded proteins. Specifically, cells experience endoplasmic reticulum (ER) stress caused by the collection of misfolded proteins. The unfolded protein responds (UPR) pathway is a process that aids in returning the cell to homeostasis after experiencing ER stress. A major step in the UPR pathway is the degradation of misfolded proteins within the cell. Small molecule proteasome stimulators have been able to increase proteasome activity and the degradation of misfolded proteins within the cell. These small molecule stimulators have the potential to accelerate the UPR pathway and reduce ER cellular stress. Our goal is to study how modulating 20S CP activity with small molecules can affect ER stress levels in cells.

Relationship of proteasome activity on ER stress

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