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Global profiling of distinct cysteine redox forms reveals wide-ranging redox regulation in C. elegans.

Jin Meng | Ling Fu | Keke Liu | Caiping Tian | Ziyun Wu | Youngeun Jung | Renan B Ferreira | Kate S Carroll | T Keith Blackwell | Jing Yang
Nature communications | 2021

Post-translational changes in the redox state of cysteine residues can rapidly and reversibly alter protein functions, thereby modulating biological processes. The nematode C. elegans is an ideal model organism for studying cysteine-mediated redox signaling at a network level. Here we present a comprehensive, quantitative, and site-specific profile of the intrinsic reactivity of the cysteinome in wild-type C. elegans. We also describe a global characterization of the C. elegans redoxome in which we measured changes in three major cysteine redox forms after H2O2 treatment. Our data revealed redox-sensitive events in translation, growth signaling, and stress response pathways, and identified redox-regulated cysteines that are important for signaling through the p38 MAP kinase (MAPK) pathway. Our in-depth proteomic dataset provides a molecular basis for understanding redox signaling in vivo, and will serve as a valuable and rich resource for the field of redox biology.

Pubmed ID: 33658510

Research resources used in this publication

None found

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Associated grants

  • Agency: NIH HHS, United States
    Id: P40 OD010440
  • Agency: NCI NIH HHS, United States
    Id: R01 CA227849
  • Agency: NIGMS NIH HHS, United States
    Id: R35 GM122610
  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM102187
  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM087638
  • Agency: NIDDK NIH HHS, United States
    Id: P30 DK036836

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