Abstract by Colten McEwan
Chemistry and Biochemistry
Identifying LRBA as a Novel Regulator of ATG9A
Autophagy is an essential catabolic process that degrades cellular materials to support cell growth and survival. Aberrant autophagy has been linked to disease and there are few therapeutics that target autophagy. This is partly because autophagic mechanisms are still unclear. A key apical protein involved in autophagy is ATG9A, but the mechanisms surrounding its autophagic role are poorly understood. Using a novel biotin labeling approach, our lab uncovered an ATG9A interactor called Lipopolysaccharide-Responsive Beige-Like Anchor Protein (LRBA). Mutations in LRBA cause human immune defects characterized by abnormal autophagy, but the mechanism is unknown. I have validated LRBA as an ATG9A-interacting protein and shown that CRISPR deletion of LRBA results in defective autophagic flux. My goal is to uncover how LRBA regulates ATG9A and if disrupting LRBA-ATG9A interaction facilitates autophagy-related disease. This will lead to possible therapeutic development to treat diseases that are currently difficult to treat.