Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum.
Efficient protein folding and quality control in the endoplasmic reticulum (ER) require that disulphide bonds are formed in nascent proteins, isomerised during assisted folding and reduced in terminally misfolded molecules. Recent findings in yeast and mammalian cells indicate that specific protein-protein interactions underlie redox control in the ER, allowing these competing reactions to occur simultaneously during protein quality control.
Fassio
Anna
A
DiBiT-HSR and Università Vita-Salute San Raffaele, Milan, Italy.
Sitia
Roberto
R
D000818:Animals; D004220:Disulfides / Q000737:chemistry; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D007536:Isomerism; D008562:Membrane Glycoproteins; D009844:Oligosaccharides / Q000378:metabolism; D010088:Oxidoreductases; D050862:Oxidoreductases Acting on Sulfur Group Donors; D019704:Protein Disulfide-Isomerases / Q000378:metabolism; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins
D004220:Disulfides; D006023:Glycoproteins; D008562:Membrane Glycoproteins; D009844:Oligosaccharides; D011506:Proteins; D029701:Saccharomyces cerevisiae Proteins; C405327:ERO1A protein, human; D010088:Oxidoreductases; D050862:Oxidoreductases Acting on Sulfur Group Donors; C113186:ERO1 protein, S cerevisiae; D019704:Protein Disulfide-Isomerases