Advisor: Luigi Puglielli
My thesis work in Dr. Puglielli’s lab has focused on the quality control of protein folding, and its implication in neurological disorders and neurodegenerative diseases. Specifically, the Endoplasmic Reticulum acetylation machinery ensures that properly folded proteins are acetylated; those that are not folded properly must be degraded through autophagy. Acetyl-CoA is the donor for this acetylation, and my research has focused on the implications of dysregulated acetyl-CoA homeostasis throughout the cell.
In fact, we have determined that altered acetyl-CoA flux regulates the proteome and acetyl-proteome in order to maintain intracellular crosstalk. The cell’s metabolic adaptations include lipid metabolism and mitochondria bioenergetics. Importantly, levels of ER acetylation machinery increase with age, and in Alzheimer’s disease. These findings give us insight to the multitude of ways that cellular metabolism is impacted with aging and in patients with AD.