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Our lab studies regulated protein post-translational modifications. We’re particularly interested in the ubiquitin-proteasome system as it relates to normal physiology, cancer, infectious diseases, cardiovascular disease, and other disorders. Research is focused in four major areas: 1) structure-function relationships of ubiquitin-conjugating enzymes (E2s), ubiquitin protein ligases (E3s), and deubiquitinating enzymes (DUBs); 2) the ubiquitin system at the endoplasmic reticulum (ER) including: ER-associated degradation (ERAD), cellular stress responses, regulation of lipid biosynthesis, and regulation of the innate immune response; 3) the ubiquitin system in mitochondrial regulatory processes and removal of damaged proteins; and 4) the role of ubiquitin system in removing bacterial toxins from cells. Our research program utilizes a wide variety of approaches and employs systems that include cancer cell lines, yeast, mice, and human tissue samples.
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