TY - JOUR
T1 - ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress
AU - Cunnea, Paula M.
AU - Miranda-Vizuete, Antonio
AU - Bertoli, Gloria
AU - Simmen, Thomas
AU - Damdimopoulos, Anastasios E.
AU - Hermann, Stefan
AU - Leinonen, Saku
AU - Huikko, Markku Pelto
AU - Gustafsson, Jan Åke
AU - Sitia, Roberto
AU - Spyrou, Giannis
N1 - Copyright:
Copyright 2021 Elsevier B.V., All rights reserved.
PY - 2003/1/10
Y1 - 2003/1/10
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M206995200
DO - 10.1074/jbc.M206995200
M3 - Article
C2 - 12411443
AN - SCOPUS:0037428470
VL - 278
SP - 1059
EP - 1066
JO - The Journal of biological chemistry
JF - The Journal of biological chemistry
SN - 0021-9258
IS - 2
ER -