TY - JOUR
T1 - Endoplasmic reticulum oxidoreductin 1-Lβ (ERO1-Lβ), a human gene induced in the course of the unfolded protein response
AU - Pagani, Massimiliano
AU - Fabbri, Marco
AU - Benedetti, Cristina
AU - Fassio, Anna
AU - Pilati, Stefania
AU - Bulleid, Neil J.
AU - Cabibbo, Andrea
AU - Sitia, Roberto
PY - 2000/8/4
Y1 - 2000/8/4
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M003061200
DO - 10.1074/jbc.M003061200
M3 - Article
C2 - 10818100
AN - SCOPUS:0034604675
VL - 275
SP - 23685
EP - 23692
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 31
ER -