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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.
Centre for Biotechnology, Department of Biosciences at Novum, Karolinska Institute, Södertörns Högskola, S-14157 Huddinge, Sweden..
Centre for Biotechnology, Department of Biosciences at Novum, Karolinska Institute, Södertörns Högskola, S-14157 Huddinge, Sweden..
Università Vita-Salute San Raffaele, 20132 Milan, Italy.
Università Vita-Salute San Raffaele, 20132 Milan, Italy.
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2003 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 278, no 2, 1059-66 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2003. Vol. 278, no 2, 1059-66 p.
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Medical and Health Sciences
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URN: urn:nbn:se:liu:diva-98801DOI: 10.1074/jbc.M206995200PubMedID: 12411443OAI: oai:DiVA.org:liu-98801DiVA: diva2:655915
Available from: 2013-10-14 Created: 2013-10-14 Last updated: 2017-12-06

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Spyrou, Giannis

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