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Originally published In Press as doi:10.1074/jbc.M206995200 on October 30, 2002

J. Biol. Chem., Vol. 278, Issue 2, 1059-1066, January 10, 2003
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ERdj5, an Endoplasmic Reticulum (ER)-resident Protein Containing DnaJ and Thioredoxin Domains, Is Expressed in Secretory Cells or following ER Stress*

Paula M. CunneaDagger , Antonio Miranda-VizueteDagger §, Gloria Bertoli§, Thomas Simmen||, Anastasios E. DamdimopoulosDagger , Stefan Hermann**, Saku LeinonenDagger Dagger , Markku Pelto HuikkoDagger Dagger , Jan-Åke GustafssonDagger , Roberto Sitia§§¶¶, and Giannis SpyrouDagger ¶¶||||

From the Dagger  Centre for Biotechnology, Department of Biosciences at Novum, Karolinska Institute, and the ** Steroid Group, Södertörns Högskola, S-14157 Huddinge, Sweden,  Department of Biological and Technological Research, San Raffaele Scientific Institute, and the §§ Università Vita-Salute San Raffaele, 20132 Milan, Italy, and the Dagger Dagger  Department of Developmental Biology, Tampere University Medical School, and the Department of Pathology, Tampere University Hospital, Fin-33101 Tampere, Finland

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.

* This work was supported in part by Swedish Medical Research Council Projects 13X-10370 and 19X-11622-03C and by grants from the Medical Research Fund of Tampere University Hospital, the Funds of University of Tampere, the Karolinska Institute, Södertörns Högskola, the Associazione Italiana per la Ricerca sul Cancro (AIRC), the Italian Ministry of University and Research (MIUR, Center of Excellence in Physiopathology of Cell Differentiation), PRIN (2002.058218_006), and Telethon (GP0117/01). The CELERA Database was used under, license agreement with the Karolinska Institute (Stockholm).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF038503 and AF255459.

§ Both authors contributed equally to this work.

|| Recipient of a fellowship from Telethon (380/bs).

¶¶ Both authors contributed equally to this work.

|||| To whom correspondence should be addressed. Tel.: 46-8-608-9162; Fax: 46-8-774-5538; E-mail: giannis.spyrou@cbt.ki.se.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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