Abstract
A complex array of chaperones and enzymes reside in the endoplasmic reticulum (ER) to assist the folding and assembly of and the disulfide bond formation in nascent secretory proteins. Here we characterize a novel human putative ER co-chaperone (ERdj5) containing domains resembling DnaJ, protein-disulfide isomerase, and thioredoxin domains. Homologs of ERdj5 have been found in Caenorhabditis elegans and Mus musculus. In vitro experiments demonstrated that ERdj5 interacts via its DnaJ domain with BiP in an ATP-dependent manner. ERdj5 is a ubiquitous protein localized in the ER and is particularly abundant in secretory cells. Its transcription is induced during ER stress, suggesting potential roles for ERdj5 in protein folding and translocation across the ER membrane.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / pharmacology
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Amino Acid Sequence
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Carrier Proteins / metabolism
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Chromosome Mapping
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Cloning, Molecular
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Endoplasmic Reticulum / chemistry*
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Endoplasmic Reticulum / metabolism
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Endoplasmic Reticulum Chaperone BiP
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HSP40 Heat-Shock Proteins
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Heat-Shock Proteins / chemistry*
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Humans
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Molecular Chaperones / analysis*
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Molecular Chaperones / chemistry
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Molecular Chaperones / genetics
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Molecular Chaperones / metabolism
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Molecular Sequence Data
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Protein Folding
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Protein Transport
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Sequence Alignment
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Thioredoxins / chemistry*
Substances
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Carrier Proteins
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DNAJC10 protein, human
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Endoplasmic Reticulum Chaperone BiP
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HSP40 Heat-Shock Proteins
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Heat-Shock Proteins
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Molecular Chaperones
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Thioredoxins
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Adenosine Triphosphate
Associated data
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GENBANK/AF038503
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GENBANK/AF255459