Cellular responses to protein misfolding
Instructor: Prof. Amy Chang
Time: Lecture: Friday 3:00 – 4:00 pm
Labs: Tuesday 9:00 am – 12:00 pm, Tuesday 2:00 – 5:00 pm
Coming Fall 2019
Note: Please submit only ONE application form no matter how many courses you are applying to. There is just one application link and you will be prompted to select all courses you wish to apply for and then rank your preferences. If you apply more than once, we will consider your most recent application as the valid one and disregard previous applications.
In eukaryotic cells, newly synthesized proteins enter the secretory pathway at the endoplasmic reticulum (ER) where they first assume their folded state. Because proper protein folding is essential for cell survival, accumulation of unfolded or misfolded proteins at the ER is known as ER stress, and contributes to numerous diseases from cystic fibrosis to diabetes. The goal of this course is to study cell response to ER stress using yeast as a model system. Recent evidence suggests that in response to ER stress, accumulation of toxic reactive oxygen species (ROS) generated by the mitochondrial electron transport chain can lead to cell death. At the same time, remodeling of mitochondria can occur as an adaptive response to ER stress to reduce ROS accumulation. Students will learn to perform assays to detect ER stress, measure mitochondrial ROS generation, and assess mitochondrial remodeling. Students will also participate in a yeast genetic screen to characterize the cellular machinery that promotes an adaptive mitochondrial response to ER stress. In this way, our efforts represent first steps towards devising therapeutic strategies for disorders linked to ER stress.