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Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space
Author(s) -
CardenasRodriguez Mauricio,
Tokatlidis Kostas
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12766
Subject(s) - mitochondrial intermembrane space , intermembrane space , thioredoxin , microbiology and biotechnology , endoplasmic reticulum , mitochondrion , oxidative phosphorylation , periplasmic space , glutaredoxin , oxidative folding , chemistry , biochemistry , protein folding , cytosol , biology , protein disulfide isomerase , oxidative stress , bacterial outer membrane , escherichia coli , gene , enzyme
Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways. The major thiol‐reducing pathways engage the thioredoxin and the glutaredoxin systems which are involved in removal of oxidants, protein proofreading and folding. Alterations in redox balance likely affect the flux of these redox pathways and are related to ageing and diseases such as neurodegenerative disorders and cancer. Here, we first review the well‐studied oxidative and reductive processes in the bacterial periplasm and the endoplasmic reticulum, and then discuss the less understood process in the mitochondrial intermembrane space, highlighting its importance for the proper function of the cell.