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Manipulation of phospholipid composition alters protein binding to lipid droplets (606.3)
Author(s) -
Hains Anastasia,
Listenberger Laura
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.606.3
Subject(s) - phospholipid , phosphatidylcholine , lipid droplet , phosphatidylethanolamine , chemistry , phosphocholine , biochemistry , organelle , membrane
Lipid droplets are cytoplasmic organelles that store excess lipid. Each lipid droplet consists of a core of neutral lipid surrounded by a phospholipid monolayer. Proteins interact with the phospholipid surface and regulate lipid droplet synthesis and degradation. We have shown that the phospholipid composition of synthetic lipid droplets can influence protein binding in an in vitro assay. We aimed to determine if protein binding to lipid droplets is influenced by the lipid droplet phospholipid composition in cells. We altered the phospholipid composition of lipid droplets in NIH3T3 cells with hexadecylphosphocholine (HePC), an inhibitor of phosphatidylcholine (PC) synthesis. Isolation of lipid droplets from inhibitor treated and control cells and separation of phospholipids by thin layer chromatography, demonstrated a decrease in PC relative to phosphatidylethanolamine in HePC‐treated cells. Furthermore, HePC treatment prevented the lipid droplet localization of CTP:phosphocholine cytidylyltransferase, the enzyme that catalyzes the rate‐limiting step in PC synthesis. Other changes in protein localization to lipid droplets were observed by SDS‐PAGE and silver staining of lipid droplet proteins in HePC‐treated and control cells. Current and future experiments continue to examine how changes in phospholipid composition alter the protein composition of this important storage compartment. Grant Funding Source : Supported by an award from Research Corporation for Science Advancement