TY - JOUR T1 - Redox regulation in the endoplasmic reticulum JF - Biochemical Society Transactions JO - Biochem Soc Trans SP - 905 LP - 908 DO - 10.1042/BST20140065 VL - 42 IS - 4 AU - Bulleid, Neil J. AU - van Lith, Marcel Y1 - 2014/08/01 UR - http://www.biochemsoctrans.org/content/42/4/905.abstract N2 - The efficient folding, assembly and secretion of proteins from mammalian cells is a critically important process for normal cell physiology. Breakdown of the ability of cells to secrete functional proteins leads to disease pathologies caused by a lack of protein function or by cell death resulting from an aggravated stress response. Central to the folding of secreted proteins is the formation of disulfides which both aid folding and provide stability to the protein structure. For disulfides to form correctly necessitates the appropriate redox environment within the endoplasmic reticulum: too reducing and disulfides will not form, too oxidizing and non-native disulfides will not be resolved. How the endoplasmic reticulum maintains the correct redox balance is unknown. Although we have a good appreciation of the processes leading to a more oxidizing environment, our understanding of how any counterbalancing reductive pathway operates is limited. The present review looks at potential mechanisms for introducing reducing equivalents into the endoplasmic reticulum and discusses an approach to test these hypotheses.Abbreviations: ER, endoplasmic reticulum; ERdj5, ER DnaJ homology 5; ERFAD, ER flavoprotein associated with degradation; ERp57, ER protein 57; PDI, protein disulfide-isomerase; roGFP, redox-sensitive GFP ER -