My laboratory studies chaperone proteins that bind to and regulate the steroid hormone receptors. At least twelve chaperone and cochaperone proteins are required for normal receptor function, including Hsp70 and Hsp90. All of these factors offer the potential opportunity for therapeutic intervention. We are interested in understanding the manner in which these factors influence receptor folding, hormone binding, nuclear translocation, dimerization, and DNA binding. One group of cochaperones termed immunophilins are of particular interest as they are the only receptor-associated cochaperones that display specificity towards small subsets of Hsp90 substrate proteins. Two immunophilins, FKBP51 and FKBP52, specifically regulate glucocorticoid, androgen and progesterone receptor function in cells and whole animal models. Using various biochemical and cellular approaches in yeast and mammalian cells, my lab is actively working to understand the molecular mechanism by which the FKBP proteins influence receptor function. In addition, we are developing and employing strategies to identify selective FKBP inhibitors that could be used to treat hormone-related diseases such as prostate cancer. Over the last fourteen years I have worked in the areas of steroid hormone receptor function, environmental endocrine disruption, and chaperone biology. During that time I acquired a vast amount of experience in both the molecular chaperone field and the steroid hormone receptor field. I have published extensively on the cochaperone regulation of receptor function, most recently focused on the FKBP immunophilin proteins.