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J Biol Chem. 2011 Aug 12;286(32):27872-4. doi: 10.1074/jbc.C111.266452. Epub 2011 Jun 21.

Lipid droplet formation is dispensable for endoplasmic reticulum-associated degradation.

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  • 1Department of Biology, Stanford University, Stanford, California 94305, USA.


Proteins that fail to fold or assemble in the endoplasmic reticulum (ER) are destroyed by cytoplasmic proteasomes through a process known as ER-associated degradation. Substrates of this pathway are initially sequestered within the ER lumen and must therefore be dislocated across the ER membrane to be degraded. It has been proposed that generation of bicellar structures during lipid droplet formation may provide an "escape hatch" through which misfolded proteins, toxins, and viruses can exit the ER. We have directly tested this hypothesis by exploiting yeast strains defective in lipid droplet formation. Our data demonstrate that lipid droplet formation is dispensable for the dislocation of a plant toxin and the degradation of both soluble and integral membrane glycoproteins.

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