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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway.

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.[1]

References

  1. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Hiller, M.M., Finger, A., Schweiger, M., Wolf, D.H. Science (1996) [Pubmed]
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