Abstract
FOXO (Forkhead box, class O) proteins are transcriptional regulators ubiquitously expressed in mammalian cells with roles in modulating fuel metabolism, stress resistance and cell death. FOXO transcription factors are regulated by redox processes at several levels, including enzymatic and nonenzymatic posttranslational modification. Target genes controlled by FOXO proteins include genes encoding antioxidant proteins, thus likely contributing to the key role FOXOs play in the cellular response to oxidative stress. Here, an overview is provided on (i) the modulation of FOXO proteins by thiol depleting agents, (ii) consequences of thiol depletion for stress resistance and life span of a model organism, Caenorhabditis elegans and (iii) the role of FOXO proteins therein.
Highlights
FOXO transcription factors are regulated by posttranslational modification, including phosphorylation, acetylation and ubiquitinylation
Thiol depletion elicited by attenuation of glutathione biosynthesis through RNA interference with expression of C. elegans γ-glutamyl-cysteine synthetase confirms that glutathione depletion may cause an adaptive response eliciting life span extension [3]
diethyl maleate (DEM) affects C. elegans life span via modulation of the nematode FOXO ortholog, no change in transcriptional regulatory activity is observed for mammalian FOXO1 in cells exposed to DEM [5]
Summary
FOXO transcription factors are regulated by posttranslational modification, including phosphorylation, acetylation and ubiquitinylation. Nonenzymatic modification, such as thiol oxidation to generate intermolecular disulfide bonds between FOXOs and regulating proteins was described to occur under exposure to reactive oxygen species, such as hydrogen peroxide [1], constituting one of the several layers of redox regulation of these transcription factors [2].
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