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Protein quality mechanisms are fundamental for proteostasis of eukaryotic cells. Endoplasmic reticulum associated degradation (ERAD) is a well-studied pathway that ensures quality control of secretory and endoplasmic reticulum (ER)-resident proteins. Different branches of ERAD are involved in degradation of malfolded secretory proteins, depending on the localization of the misfolded part, the ER lumen (ERAD-L), the ER membrane (ERAD-M), and the cytosol (ERAD-C). Here we report that modification of several ER transmembrane proteins with the photo-sensitive degron (psd) module resulted in light-dependent degradation of the membrane proteins via the ERAD-C pathway. We found dependency on the ubiquitylation machinery including the ubiquitin-activating enzyme Uba1, the ubiquitin-conjugating enzymes Ubc6 and Ubc7 as well as the ubiquitin-protein ligase Doa10. Moreover, we found involvement of the Cdc48 AAA-ATPase complex members Ufd1 and Npl4 as well as the proteasome in degradation of Sec62-myc-psd. Thus, our work shows that ERAD-C substrates can be systematically generated via synthethic degron constructs, which facilitates future investigations of the ERAD-C pathway.
This article was published in the following journal.
Name: Molecular biology of the cell
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