Experts and Doctors on oxidoreductases acting on sulfur group donors in Milano, Lombardy, Italy
Locale: Milano, Lombardy, Italy
Topic: oxidoreductases acting on sulfur group donors
Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery M, Bulleid N, et al
. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J Biol Chem. 2000;275:4827-33 pubmed
..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. ..
Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid N, et al
. Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J Biol Chem. 2000;275:23685-92 pubmed
..Furthermore, only ERO1-Lbeta transcripts are induced in the course of the unfolded protein response. Our results suggest a complex regulation of ER redox homeostasis in mammalian cells. ..
Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 2001;20:6288-96 pubmed
..Mutants in the Ero1-Lalpha CXXCXXC motif act as dominant negatives by limiting immunoglobulin oxidation. PDI-dependent oxidative folding in living cells can thus be manipulated by using hERO variants. ..
Bertoli G, Simmen T, Anelli T, Molteni S, Fesce R, Sitia R. Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum. J Biol Chem. 2004;279:30047-52 pubmed
..These findings suggest that interactions between the two triads, dependent on Cys85 and Cys391, are important for Ero1alpha function, possibly stabilizing a platform for efficient PDI oxidation. ..
Otsu M, Bertoli G, Fagioli C, Guerini Rocco E, Nerini Molteni S, Ruffato E, et al
. Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44. Antioxid Redox Signal. 2006;8:274-82 pubmed
..PDI also prevents Ero1 aggregation and dimerization, thus chaperoning its own oxidase. This dynamic retention mechanism of Ero1 may be important for fine-tuning the regulation of ER redox homeostasis and quality control. ..