ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress

Paula M. Cunnea, Antonio Miranda-Vizuete, Gloria Bertoli, Thomas Simmen, Anastasios E. Damdimopoulos, Stefan Hermann, Saku Leinonen, Markku Pelto Huikko, Jan Åke Gustafsson, Roberto Sitia, Giannis Spyrou

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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.

Original languageEnglish
Pages (from-to)1059-1066
Number of pages8
JournalJournal of Biological Chemistry
Volume278
Issue number2
DOIs
Publication statusPublished - Jan 10 2003

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Cunnea, P. M., Miranda-Vizuete, A., Bertoli, G., Simmen, T., Damdimopoulos, A. E., Hermann, S., Leinonen, S., Huikko, M. P., Gustafsson, J. Å., Sitia, R., & Spyrou, G. (2003). ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress. Journal of Biological Chemistry, 278(2), 1059-1066. https://doi.org/10.1074/jbc.M206995200