Journal
SCIENCE
Volume 321, Issue 5888, Pages 569-572Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1159293
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Funding
- Grants-in-Aid for Scientific Research [19GS0314, 19058008] Funding Source: KAKEN
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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.
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