|Education||BS, University of North Carolina, Chapel Hill|
|Current Position||Genome Scientist|
Requirements for E3 ligase-substrate interaction for post-ER protein quality control
Many human diseases are a result of the dysfunction of protein quality control, such as neurodegenerative and aging-related disorders. We study the Dsc E3 ligase complex, a candidate machinery for post-endoplasmic reticulum (ER) protein degradation. The Dsc E3 ligase complex is a multi-subunit transmembrane complex in the Golgi, homologous to the components of ER-associated degradation (ERAD), which recognize and remove misfolded and mutant proteins in the ER. Each of the 5 core subunits of the Golgi Dsc E3 ligase complex is required for the cleavage of a substrate known as Sterol Regulatory Element Binding Protein (SREBP), important for cholesterol metabolism in mammals. My study will utilize biochemical, genetic and genomic approaches to characterize requirements for SREBP-Dsc interaction.