PMID:10671517

Citation	Cabibbo, A, Pagani, M, Fabbri, M, Rocchi, M, Farmery, MR, Bulleid, NJ and Sitia, R (2000) ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J. Biol. Chem. 275:4827-33
Abstract	Oxidizing conditions must be maintained in the endoplasmic reticulum (ER) to allow the formation of disulfide bonds in secretory proteins. Here we report the cloning and characterization of a mammalian gene (ERO1-L) that shares extensive homology with the Saccharomyces cerevisiae ERO1 gene, required in yeast for oxidative protein folding. When expressed in mammalian cells, the product of the human ERO1-L gene co-localizes with ER markers and displays Endo-H-sensitive glycans. In isolated microsomes, ERO1-L behaves as a type II integral membrane protein. ERO1-L is able to complement several phenotypic traits of the yeast thermosensitive mutant ero1-1, including temperature and dithiothreitol sensitivity, and intrachain disulfide bond formation in carboxypeptidase Y. ERO1-L is no longer functional when either one of the highly conserved Cys-394 or Cys-397 is mutated. These results strongly suggest that ERO1-L is involved in oxidative ER protein folding in mammalian cells.
Links	PubMed
Keywords	Amino Acid Sequence; Disulfides/metabolism; Endoplasmic Reticulum/metabolism; Genetic Complementation Test; Humans; Intracellular Membranes/metabolism; Membrane Glycoproteins/chemistry; Membrane Glycoproteins/genetics; Membrane Glycoproteins/metabolism; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Microsomes/metabolism; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Protein Biosynthesis; Protein Folding; Saccharomyces cerevisiae/genetics; Sequence Homology, Amino Acid
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