ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum

Andrea Cabibbo, Massimiliano Pagani, Marco Fabbri, Mariano Rocchi, Mark R. Farmery, Neil J. Bulleid, Roberto Sitia

Research output: Contribution to journalArticlepeer-review


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 colocalizes 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.

Original languageEnglish
Pages (from-to)4827-4833
Number of pages7
JournalJournal of Biological Chemistry
Issue number7
Publication statusPublished - Feb 18 2000

ASJC Scopus subject areas

  • Biochemistry


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