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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/47474
Título

ERdj5, an Endoplasmic Reticulum (ER)-resident Protein Containing DnaJ and Thioredoxin Domains, Is Expressed in Secretory Cells or following ER Stress

AutorCunnea, Paula M.; Miranda-Vizuete, Antonio ; Bertoli, Gloria; Simmen, Thomas; Damdimopoulos, Anastasios E.; Hermann, Stefan; Leinonen, Saku; Pelto-Huikko, Markku; Gustafsson, Jan-Åke; Sitia, Roberto; Spyrou, Giannis
Palabras claveAdenosine triphosphate
Carrier protein
Chromosome
Cloning
Endoplasmic reticulum
Molecular chaperones
Thioredoxin
Fecha de publicación10-ene-2003
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónJournal of Biological Chemistry 278(2): 1059-1066 (2003)
ResumenA 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.
Descripción8 páginas, 7 figuras.
Versión del editorhttp://dx.doi.org/10.1074/jbc.M206995200
URIhttp://hdl.handle.net/10261/47474
DOI10.1074/jbc.M206995200
ISSN0021-9258
E-ISSN1083-351X
ReferenciasPMID: 12411443
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