Protein folding: a missing redox link in the endoplasmic reticulum.
Native disulphide-bond formation during protein folding in the endoplasmic reticulum requires oxidative machinery, the components and mechanism of which are not yet fully understood. Two recent papers have identified a novel protein component that appears to play a key role in this important redox pathway.
Freedman
R B
RB
Research School of Biosciences, University of Kent, Canterbury.
Dunn
A D
AD
Ruddock
L W
LW
D004220:Disulfides / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000201:enzymology / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D008562:Membrane Glycoproteins; D010084:Oxidation-Reduction; D010088:Oxidoreductases; D019704:Protein Disulfide-Isomerases / Q000378:metabolism; D017510:Protein Folding
D004220:Disulfides; D006023:Glycoproteins; D008562:Membrane Glycoproteins; C405327:ERO1A protein, human; C491864:Ero1l protein, mouse; D010088:Oxidoreductases; D019704:Protein Disulfide-Isomerases