Oxidative conditions must be generated in the endoplasmic reticuinm (ER) to allow disulfide bond formation in secretory proteins. A family of conserved genes, termed ERO for ER oxidoreductins, plays a key role in this process. We have previously described the human gene ERO1-L, which complements several phenotypic traits of the yeast thermo-sensitive mutant ero1-1 (Cabibbo, A., Pagani, M., Fabbri, M., Rocchi, M., Farmery, M. R., Bulleid, N. J., and Sitia, R. (2000) J. Biol. Chem. 275, 4827-4833). Here, we report the cloning and characterization of a novel human member of this family, ERO1-Lβ. Immunofluorescence, endoglycosidase sensitivity, and in vitro translatlon/translocation assays reveal that the products of the ERO1-Lβ gene are primarily localized in the ER of mammalian cells. The ability to allow growth at 37 °C and to alleviate the 'unfolded protein response' when expressed in ero1-1 cells indicates that ERO1-Lβ is involved also in generating oxidative conditions in the ER. ERO1-L and ERO1-Lβ display different tissue distributions. Furthermore, only ERO1-Lβ transcripts are induced in the course of the unfolded protein response. Our results suggest a complex regulation of ER redox homeostasis in mammalian cells.
|Titolo:||Endoplasmic reticulum oxidoreductin 1-L beta (ERO1-L beta), a human gene induced in the course of the unfolded protein response|
PAGANI, MASSIMILIANO (Primo)
|Parole Chiave:||disulfide-bond formation; Escherichia-coli; transmembrane protein; transcription factor; respiratory-chain; mammalian-cells; CXXC motif; pathwvay; kinase; membrane|
|Settore Scientifico Disciplinare:||Settore BIO/11 - Biologia Molecolare|
|Data di pubblicazione:||2000|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1074/jbc.M003061200|
|Appare nelle tipologie:||01 - Articolo su periodico|