ERdj5 Is Required as a Disulfide Reductase for Degradation of Misfolded Proteins in the ER
Copyright policy )ERdj5 Is Required as a Disulfide Reductase for Degradation of Misfolded Proteins in the ER
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 α-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.
- Japan Science and Technology Agency Japan
- Kyoto University Japan
- McGill University Canada
Protein Folding, Amino Acid Motifs, Protein Disulfide-Isomerases, Membrane Proteins, Protein Disulfide Reductase (Glutathione), HSP40 Heat-Shock Proteins, Endoplasmic Reticulum, Glutathione, Cell Line, Protein Structure, Tertiary, Mice, Amino Acid Substitution, Immunoglobulin J-Chains, Mutation, Animals, Humans, Endoplasmic Reticulum Chaperone BiP, Oxidation-Reduction, Heat-Shock Proteins, Molecular Chaperones
Protein Folding, Amino Acid Motifs, Protein Disulfide-Isomerases, Membrane Proteins, Protein Disulfide Reductase (Glutathione), HSP40 Heat-Shock Proteins, Endoplasmic Reticulum, Glutathione, Cell Line, Protein Structure, Tertiary, Mice, Amino Acid Substitution, Immunoglobulin J-Chains, Mutation, Animals, Humans, Endoplasmic Reticulum Chaperone BiP, Oxidation-Reduction, Heat-Shock Proteins, Molecular Chaperones
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