Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding

• Published in: Scientific reports Vol. 3; no. 1; p. 2456
• Main Authors: Sato, Yoshimi, Kojima, Rieko, Okumura, Masaki, Hagiwara, Masatoshi, Masui, Shoji, Maegawa, Ken-ichi, Saiki, Masatoshi, Horibe, Tomohisa, Suzuki, Mamoru, Inaba, Kenji
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 16.08.2013; Nature Publishing Group
• Subjects: 631/45/470/1463; 631/45/470/1981; 631/535/1266; 631/535/1267; Binding Sites; Chemical bonds; Cooperativity; Crystal structure; Disulfide bonds; Endoplasmic reticulum; Endoplasmic Reticulum - chemistry; Endoplasmic Reticulum - metabolism; Enzymes; Eukaryotes; Fidelity; HEK293 Cells; Humanities and Social Sciences; Humans; multidisciplinary; Oxidation-Reduction; Peroxiredoxin; Peroxiredoxins - chemistry; Peroxiredoxins - metabolism; Peroxiredoxins - ultrastructure; Protein Binding; Protein disulfide-isomerase; Protein Disulfide-Isomerases - chemistry; Protein Disulfide-Isomerases - metabolism; Protein Disulfide-Isomerases - ultrastructure; Protein Folding; Science; Thioredoxin

The mammalian endoplasmic reticulum (ER) harbors disulfide bond-generating enzymes, including Ero1α and peroxiredoxin 4 (Prx4) and nearly 20 members of the protein disulfide isomerase family (PDIs), which together constitute a suitable environment for oxidative protein folding. Here, we clarified th...