| First Author | Ushioda R | Year | 2008 |
| Journal | Science | Volume | 321 |
| Issue | 5888 | Pages | 569-72 |
| PubMed ID | 18653895 | Mgi Jnum | J:169878 |
| Mgi Id | MGI:4943381 | Doi | 10.1126/science.1159293 |
| Citation | Ushioda R, et al. (2008) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321(5888):569-72 |
| abstractText | Membrane and secretory proteins cotranslationally enter and are folded in the endoplasmic reticulum (ER). Misfolded or unassembled proteins are discarded by a process known as ER-associated degradation (ERAD), which involves their retrotranslocation into the cytosol. ERAD substrates frequently contain disulfide bonds that must be cleaved before their retrotranslocation. Here, we found that an ER-resident protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins, and accelerated ERAD through its physical and functional associations with EDEM (ER degradation-enhancing alpha-mannosidase-like protein) and an ER-resident chaperone BiP. Thus, ERdj5 is a member of a supramolecular ERAD complex that recognizes and unfolds misfolded proteins for their efficient retrotranslocation. |
