Our laboratory seeks to understand a fundamental but very poorly understood question in biology: When a cell encounters stress (i.e., anything that perturbs normal cellular function), how does it decide whether to adapt to the stress or die? We use diverse experimental approaches to address this question, encompassing systems biology, molecular and cell biology, and vertebrate genetics and physiology. By tackling this question, we hope to better understand diseases of stress, including neurodegeneration, cancer, metabolic syndrome, and others, and even normal cellular development and function. There are many ways in which stress can be manifested to a cell, including pathogenic infection, chemical insult, genetic mutation, nutrient deprivation, and the course of normal cellular function. The endoplasmic reticulum (ER) is the site of synthesis and folding of secretory and cell-surface proteins. The cellular response to ER stress (also known as the Unfolded Protein Response, or UPR) serves as a model for understanding not only the mechanisms by which stress is sensed, but also the ways in which the consequences of alterations of homeostasis in one location (i.e., the ER) impact diverse areas of cell function, including gene expression, metabolism, cancer, cell signaling, and apoptosis.

I was born and raised in St. Louis, Missouri, then went to college in Delaware and grad school in San Francisco before finding myself by happenstance again in the Midwest. In my spare time I’m a triathlete/runner, crossworder, and some-time cartoonist, and of late am spending time in the kitchen making bread, ice cream, tortillas, and other goodies. Scientifically, I translocated into the endoplasmic reticulum in graduate school and have never left it, so I apparently have a KDEL tag.