Correction: Conserved amphipathic helices mediate lipid droplet targeting of perilipins 1–3

Abstract

In Figure 8C, the V130D Merge + DIC image was inadvertently duplicated and presented as both the V130D Merge + DIC image and the L164D Merge + DIC image. The L164D Merge + DIC image has therefore been replaced with the correct original source image. This correction does not affect the quantification in Figure 8D, the results or conclusions of the experimental work. Conserved Amphipathic Helices Mediate Lipid Droplet Targeting of Perilipins 1–3Journal of Biological ChemistryVol. 291Issue 13PreviewPerilipins (PLINs) play a key role in energy storage by orchestrating the activity of lipases on the surface of lipid droplets. Failure of this activity results in severe metabolic disease in humans. Unlike all other lipid droplet-associated proteins, PLINs localize almost exclusively to the phospholipid monolayer surrounding the droplet. To understand how they sense and associate with the unique topology of the droplet surface, we studied the localization of human PLINs in Saccharomyces cerevisiae, demonstrating that the targeting mechanism is highly conserved and that 11-mer repeat regions are sufficient for droplet targeting. Full-Text PDF Open Access