Our lab is studying the mechanisms regulating secretory protein homeostasis under both normal and pathological conditions. We focus on understanding how the quality control machinery of the endoplasmic reticulum (ER) promotes efficient protein folding under various conditions. Proper folding and quality control of secretory proteins are crucial to cell viability. Accumulation of misfolded proteins can lead to loss of protein function and cell death. Cells activate the unfolded protein response (UPR) to cope with misfolded protein accumulation in the ER, but excessive UPR can trigger apoptosis. UPR activation has been associated with various diseases such as diabetes, Huntington’s Disease and cardiac dysfunction. We employ mammalian tissue culture models, yeast genetics, molecular biology, quantitative live cell imaging techniques and high-throughput RNA-SEQ to understand how cells detect, respond and cope with misfolded proteins. We study the regulation of gene expression by histone acetylation under various stress conditions, including accumulation of misfolded polyQ proteins linked to Huntington's Disease but also during the normal aging process. We also investigate the cellular responses to antifungal drugs in both Saccharomyces cerevisiae and the human pathogen Candida albicans.