Abstract
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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have