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Oxysterol binding protein (OSBP) and its related proteins (ORPs) constitute a conserved family of lipid binding proteins in eukaryotic cells. Results from recent studies suggest that they may play a role in the trafficking and sorting of cellular sterols. We aim to dissect the functional domains of these proteins, isolate interacting partners and elucidate the mechanisms that control their membrane association. We will use yeast as a model system because there are seven such proteins in this simple eukaryotic cell. Standard techniques in cell/molecular biology, such as sub-cloning, protein pull-down assays, site-directed mutagenesis, yeast two hybrid analysis etc., will be employed. Understanding cellular sterol transport may lead to better treatments of some forms of neurodegenerative diseases, such as Alzheimer’s disease and Niemann Pick Disease type C. Lastly, in collaboration with Dr. Andrew Brown, we will also extend our studies in yeast to mammalian cells.
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Lipid droplets (LDs, also known as lipid bodies, lipid particles) are intracellular structures consisting primarily of triacylglycerols (TAG) and sterol esters (SE), and are bounded by a monolayer of phospholipids with proteins embedded. LDs are important cellular organelles which not only store lipids but also participate in various cellular functions such as vesicular trafficking. Most importantly, human obesity is characterized by the accumulation of cellular lipid droplets. To date, little is known about the biogenesis and maturation of the LDs. We have isolated a novel gene that appears to regulate the fusion/maturation of the LDs. We will determine the topology of this novel protein and we also aim to isolate other fusion factors.
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