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Protein Quality Control At The Endoplasmic Reticulum And Nucleus In Caenorhabditis Elegans, Daniel Hassell
Protein Quality Control At The Endoplasmic Reticulum And Nucleus In Caenorhabditis Elegans, Daniel Hassell
WWU Honors College Senior Projects
Cells need proteins to carry out molecular functions, but proteins can become damaged or misfolded, which inhibits their function and can cause aggregation. Misfolded protein aggregation is associated with degenerative diseases in mammals. In Eukaryotic cells, chronically misfolded proteins can be destroyed by the Ubiquitin Proteasome System (UPS) as a way to prevent aggregation and disease. For my thesis work, I have investigated two pathways that participate in the UPS.
First, I investigate Endoplasmic Reticulum Associated Degradation (ERAD), a UPS pathway is active in the Endoplasmic Reticulum (ER) of eukaryotic cells. ERAD is well characterized in Saccharomyces cerevisiae (yeast), but …