Date of Award

Winter 5-3-2021

Thesis Access

Open Access Honors Thesis

Degree Name



Physics and Astronomy

Faculty Advisor

Christopher Kelly


Proper regulation of neutral lipid storage (lipogenesis) and release (lipolysis) are critical molecular processes localized to an organelle called the Lipid Droplet (LD). The LD consists of a core with neutral lipids such as triacylglycerols (TAGs) and sterol esters surrounded by a phospholipid monolayer. Dysregulation of the processes localized to the LD are involved in the pathology of various diseases such as Neutral Lipid Storage Disease, diabetes, stroke and cancer. The non-enzymatic protein ABHD5 (α-β Hydrolase Domain-Containing Protein 5), is thought to play a key role in the process of lipolysis by forming homo-oligomers on the surface of the LD that create packing defects on phospholipids and allowing the TAGs to be liberated by another protein called PNPLA2 (Patatin-Like Phospholipase Domain-Containing Protein 2). The goal of my research is to understand how ABHD5 changes the morphology of membranes by using various model membrane systems. Localization of the protein to the membrane and morphological changes of the lipids are visualized with epifluorescence microscopy. Results from this study will enable us to understand how lipolysis is regulated via protein interactions with lipid membranes to induce functional lipase activation perhaps through inducing membrane shape change.