Research in the Sevier lab focuses on defining how reactive oxygen species (ROS) act as both damaging agents and essential signaling molecules to regulate protein homeostasis. While excessive ROS drive irreversible macromolecular damage and contribute to diseases such as neurodegeneration, diabetes, and cancer, lower physiological ROS levels promote beneficial signaling through the reversible oxidation of protein cysteine and methionine residues. Despite growing recognition of ROS-based signaling, relatively few redox pathways have been mechanistically defined, and the functional consequences of most protein oxidation events remain unknown. Our research addresses this gap by elucidating how cysteine- and methionine-based redox pathways control protein folding, quality control, and stress adaptation, which are core processes essential to maintain a functional proteome and organism health. Using molecular, genetic, and biochemical approaches, we identify ROS sources, redox-sensitive protein targets, and regulatory mechanisms that determine the outcomes of oxidation at the protein and cellular levels. By uncovering fundamental principles of redox regulation that preserve proteome integrity, our work provides insight into basic cellular organization and informs how its failure contributes to human disease.

• PhD, Biochemistry, John Hopkins University School of Medicine, 2000
• BA, Biological Chemistry, Wellesley College, 1993