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Papers In Press, published online ahead of print September 1, 2004
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Department of Nutritional Sciences, Rutgers, The State University of New Jersey, New Brunswick, NJ 08901
Corresponding Author: Brasaemle{at}AESOP.Rutgers.edu
Perilipins play a key role in regulating triacylglycerol storage and hydrolysis in adipocytes. We have found that the central 25% of the amino acid sequence of perilipin A, including three moderately hydrophobic sequences (H1, H2, and H3) and an acidic region, is sufficient to target and anchor perilipins to lipid droplets. To extend these findings, we hypothesized that H1, H2, and H3 target and anchor perilipins to lipid droplets. In the current study, we show that the deletion of any single hydrophobic sequence or the combinations of H1 and H3 or H2 and H3 does not prevent targeting of the mutated perilipin to lipid droplets in stably transduced 3T3-L1 fibroblasts, as detected by immunofluorescence microscopy or immunoblotting of lipid droplet proteins. In contrast, mutated perilipin lacking H1 and H2 showed less efficient targeting when compared to intact perilipin, while mutated perilipin lacking H1, H2, and H3 targeted poorly to lipid droplets; thus, H3 is a relatively weak targeting signal and either H1 or H2 is required for optimal targeting. The complete elimination of perilipin targeting was observed only when all three hydrophobic sequences were deleted in combination with either the acidic region or amino-terminal sequences predicted to form amphipathic b-strands. Unlike intact perilipin A, mutated perilipin lacking either H1 and H2, or H1, H2, and H3 was released from lipid droplets following alkaline carbonate treatment, suggesting that they are loosely associated with lipid droplets. In conclusion, the three hydrophobic sequences play a major role in targeting and anchoring perilipins to lipid droplets.
Revised on August 19, 2004
Accepted on August 19, 2004
Hydrophobic sequences target and anchor perilipin A to lipid droplets
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