Proteomics

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Divergent Cysteines in FOXO3 and FOXO4 Mediate Paralog-Specific Redox Signaling

ABSTRACT: 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 results in disulfide formation between protein (hetero)dimers that alter protein function until the cellular redox has returned to the basal state. We have previously shown that this mechanism promotes the nuclear localization and activity of the FOXO4 transcription factor. Here, 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. The nuclear import receptor IPO7 forms a disulfide-dependent heterodimer with FOXO3, but not with FOXO4, which is required for reactive oxygen species (ROS)-induced nuclear translocation . These findings suggest that evolutionary acquisition of cysteines has contributed to functional divergence of FOXO paralogs.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Diploid Cell

SUBMITTER: Harmjan Vos  

LAB HEAD: Tobias Dansen

PROVIDER: PXD001041 | Pride | 2014-08-26

REPOSITORIES: Pride

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20140403_Velos1_HRV_MP_DC_1a.raw Raw
20140403_Velos1_HRV_MP_DC_1b.raw Raw
20140403_Velos1_HRV_MP_DC_1c.raw Raw
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Publications

Evolutionary acquisition of cysteines determines FOXO paralog-specific redox signaling.

Putker Marrit M   Vos Harmjan R HR   van Dorenmalen Kim K   de Ruiter Hesther H   Duran Ana G AG   Snel Berend B   Burgering Boudewijn M T BM   Vermeulen Michiel M   Dansen Tobias B TB  

Antioxidants & redox signaling 20150101 1

<h4>Unlabelled</h4>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 For  ...[more]