Abstract
Presentation Description :
The proteasome is a proteolytic complex that plays a fundamental role in cellular functions, including cell signaling, gene expression, and many repair processes. The immunoproteasome is a proteasome subtype that varies from the standard proteasome in the type of catalytic subunits present in the core particle. The term immunoproteasome was coined based on its abundant levels in cells associated with the immune system. However, we and others have previously shown that the immunoproteasome is present in non-immune cells of the brain and retina, suggesting other roles is likely. We have also reported that under a variety of conditions associated with stress, such as oxidative stress applied to cultured cells, aging and optic nerve crush in mice, immunoproteasome is upregulated. These results suggest an alternative role for the immunoproteasome as a critical stress response protein. A recent focus has been on identifying specific cell signaling pathways that are altered in response to knocking out (KO) the immunoproteasome subunits. Our data have shown that specific cell signaling pathways, i.e., NFkB, AKT, are altered in KO cells. We have also observed significant effects on autophagy in KO cells, suggesting a direct link between autophagy and the immunoproteasome. Taken together, there is strong support for the idea that the immunoproteasome has many previously unrecognized roles in the cell.
This is an abstract that was submitted for the 2018 ARVO Annual Meeting, held in Honolulu, Hawaii, April 29 - May 3, 2018.