Proteins execute a vast array of cellular functions from cell signaling to ion transport to structural support. To carry out these tasks, proteins adopt unique shapes in a process called protein folding. When proteins lose their shape, or “unfold”, they fail to function correctly and can further cause other proteins to unfold. A signaling network known as the integrated stress response (ISR) protects cells under these conditions by triggering a shut down of global protein synthesis. This pause in the production of proteins allows cells time and resources to mitigate protein unfolding-induced stress and prevent plaque-like aggregation. While great strides have been made in characterizing the ISR, there is more to be learned about stress responses and translational control. I am interested in furthering our mechanistic knowledge of the ISR and parallel pathways that regulate the synthesis of new proteins.
Current research interest:
Recently a small molecule modulator of the ISR called ISRIB (integrated stress response inhibitor) was discovered in our lab. My work is focused on determining a mechanism of action for this compound that can explain its blunting effects on the ISR.
Former Lab Affiliations
|2010-2013||Dr. John Tainer , Lawrence Berkeley National Laboratory|
|2007-2011||BA Molecular and Cell Biology, University of California, Berkeley|
|2011-Present||PhD Biochemistry, University of California, San Francisco|