Evolutionary Acquisition of Cysteines determines FOXO Paralog-Specific Redox Signaling

ABSTRACT: Data from ProteomeXchange, PXD ID: PXD001018. Experiment: HRV_A, file: folder summary. Published as part of Antioxid Redox Signal. 2014 Jul 29 . From the Abstract: {{i}} Reduction-oxidation (redox) signaling, the translation of an oxidative intracellular environment into a cellular response, is mediated by the reversible oxidation of specific cysteine thiols. The latter can result in disulfide formation between protein hetero- or homodimers that alter protein function until the local cellular redox environment has returned to the basal state. We have previously shown that this mechanism promotes the nuclear localization and activity of the Forkhead Box O4 (FOXO4) transcription factor. Aims: in this study we sought to investigate whether redox signaling differentially controls the human FOXO3 and FOXO4 paralogs. Results: We present evidence that FOXO3 and FOXO4 have acquired paralog-specific cysteines throughout vertebrate evolution. Using a proteome-wide screen we identified previously unknown redox-dependent FOXO3 interaction partners ... {{/i}}

INSTRUMENT(S): Instrument

ORGANISM(S): Homo_sapiens_viruses, Human

DISEASE(S): Not Available

SUBMITTER: Putker M, et al.  

PROVIDER: GPM32320002469 | GPMDB |

REPOSITORIES: GPMDB