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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5888
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pubmed:dateCreated |
2008-7-25
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pubmed: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.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNAJC10 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ERdj5 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/HSP40 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin J-Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Disulfide Reductase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Disulfide-Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/alpha 1-Antitrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/molecular chaperone GRP78
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
25
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pubmed:volume |
321
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
569-72
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:18653895-Amino Acid Motifs,
pubmed-meshheading:18653895-Amino Acid Substitution,
pubmed-meshheading:18653895-Animals,
pubmed-meshheading:18653895-Cell Line,
pubmed-meshheading:18653895-Endoplasmic Reticulum,
pubmed-meshheading:18653895-Glutathione,
pubmed-meshheading:18653895-HSP40 Heat-Shock Proteins,
pubmed-meshheading:18653895-Heat-Shock Proteins,
pubmed-meshheading:18653895-Humans,
pubmed-meshheading:18653895-Immunoglobulin J-Chains,
pubmed-meshheading:18653895-Membrane Proteins,
pubmed-meshheading:18653895-Mice,
pubmed-meshheading:18653895-Molecular Chaperones,
pubmed-meshheading:18653895-Mutation,
pubmed-meshheading:18653895-Oxidation-Reduction,
pubmed-meshheading:18653895-Protein Disulfide Reductase (Glutathione),
pubmed-meshheading:18653895-Protein Disulfide-Isomerases,
pubmed-meshheading:18653895-Protein Folding,
pubmed-meshheading:18653895-Protein Structure, Tertiary,
pubmed-meshheading:18653895-Proteins,
pubmed-meshheading:18653895-Recombinant Proteins,
pubmed-meshheading:18653895-Transfection,
pubmed-meshheading:18653895-Two-Hybrid System Techniques,
pubmed-meshheading:18653895-alpha 1-Antitrypsin
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pubmed:year |
2008
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pubmed:articleTitle |
ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER.
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pubmed:affiliation |
Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8397, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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