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  • Title: ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway.
    Author: Hiller MM, Finger A, Schweiger M, Wolf DH.
    Journal: Science; 1996 Sep 20; 273(5282):1725-8. PubMed ID: 8781238.
    Abstract:
    Secretion of proteins is initiated by their uptake into the endoplasmic reticulum (ER), which possesses a proteolytic system able to degrade misfolded and nonassembled proteins. The ER degradation system was studied with yeast mutants defective in the breakdown of a mutated soluble vacuolar protein, carboxypeptidase yscY (CPY*). The ubiquitin-conjugating enzyme Ubc7p participated in the degradation process, which was mediated by the cytosolic 26S proteasome. It is likely that CPY* entered the ER, was glycosylated, and was then transported back out of the ER lumen to the cytoplasmic side of the organelle, where it was conjugated with ubiquitin and degraded.
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