My laboratory is investigating how cells die via a process called apoptosis.

Apoptotic cell death is a normal process that helps remove excess or damaged cells. When apoptotic cell death goes wrong, the results are often cancer or autoimmune diseases.

My laboratory is interested in the proteins inside cells that orchestrate apoptosis. We are focusing on how the killer proteins, BAX and BAK, cause organelles called mitochondria to be leaky and kill the cell. Understanding this process is critical to developing new treatments that either enhance or block apoptosis in cancer and autoimmune disease.

Research interest

Our research program uses biochemical, cell biological and structural approaches to examine how the BCL-2 protein family regulates the mitochondrial pathway of apoptosis.

We are particularly interested in how two pore-forming BCL-2 family members, BAX and BAK, undergo conformation change and generate pores in the mitochondrial outer membrane. The goal of our research is to identify new means of specifically regulating apoptotic cell death in cancer and other diseases. 

We have found that following major conformation changes, both BAX and BAK form unusual symmetric homodimers that act as the basic unit of the apoptotic pore, and are using different strategies to determine how dimers form clusters that disrupt the membrane. 

We also discovered that BAK can be activated by antibodies, and are testing whether these antibodies can be delivered into cancer cells to directly trigger BAK-mediated apoptosis.