Phosphorylation Dependent Interactions of Perilipin 5 with Adipocyte Triacylglycerol Lipase

Abstract

Diseases such as non‐alcoholic fatty liver disease, obesity and type II diabetes are on the rise in the US, and the dysfunction of cellular lipid metabolism is a major contributor to them. Perilipins are a class of five proteins found on the exterior of lipid droplets which play a role in proper lipid metabolism. Perilipin 5 is expressed in tissues that are oxidative such as the liver, heart and skeletal muscle. We used CHO cells expressing perilipin 5 protein and immunofluorescence microscopy to examine lipase interactions with perilipin 5 under different phosphorylation states. We hypothesized that the interactions of lipases such as adipocyte triacylglyerol lipase (ATGL) and perilipin 5 were phosphorylation dependent. Using immunofluorescence microscopy, we confirmed that perilipin 5 changes its subcellular localization and moves from lipid droplets and cytosol to the nucleus when stimulated with forskolin and IBMX to activate the PKA signaling pathway. Identification of lipase‐perilipin 5 interactions are ongoing. Collectively these data show that perilipin 5 interactions and localization in the cell are phosphorylation dependent.This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.