Education
Ph.D. 1989, Oregon State University
Research
The focus of this laboratory is the mechanism of signal transduction mediated by members of the nuclear receptor superfamily, a large group of ligand-dependent transcription factors. We use a variety of genetic, molecular biological and biochemical techniques to dissect the molecular basis of ligand activation of nuclear receptors and the mechanisms underlying the ability of these proteins to modulate transcriptional processes, the latter of which involves interaction of the receptors with two other groups of cellular proteins known as transcriptional corepressors and coactivators. In addition, we are interested in the isolation of genes that are transcriptional targets of nuclear receptors toward the goal of understanding the cellular and organismal effects of nuclear receptor activation. Three subfamilies of nuclear receptors are currently studied in the laboratory: (1) the retinoic acid (RAR) and retinoid X (RXR) receptors that mediate cellular effects of vitamin A (retinoic acids) and related retinoids, (2) peroxisomeproliferator-activated receptors that appear to be receptors for fatty acids and, in addition, mediate the toxicity of a large group of environmental contaminants known as peroxisome proliferators, and (3) the COUP-TF family of orphan receptors that appear tofunction as constitutive repressors of transcription.
