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Access to the article is free, however registration and sign-in are required. A specific enzyme that reduces protein disulfide bonds is part of a complex that eliminates aggregated, misfolded proteins. In eukaryotic cells, most newly synthesized secretory proteins are first translocated into the endoplasmic reticulum (ER) and transit through organelles that constitute a secretory pathway. However, proteins that misfold in the ER are retrotranslocated out of this organelle to the cytoplasm, where they are degraded by the ubiquitin-proteasome system (a process called ER-associated degradation). For efficient retrotranslocation, the disulfide bonds of misfolded proteins must be reduced, and on page 569 in this issue, Ushioda et al. (1) report that this reaction is catalyzed by ERdj5, the first dedicated reductase identified in the ER.
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