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Site-specific mapping and quantification of protein S-sulphenylation in cells

Author

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  • Jing Yang

    (Departmemt of Biochemistry, Vanderbilt University School of Medicine
    Jim Ayers Institute for Precancer Detection and Diagnosis, Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine)

  • Vinayak Gupta

    (The Scripps Research Institute)

  • Kate S. Carroll

    (The Scripps Research Institute)

  • Daniel C. Liebler

    (Departmemt of Biochemistry, Vanderbilt University School of Medicine
    Jim Ayers Institute for Precancer Detection and Diagnosis, Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine)

Abstract

Cysteine S-sulphenylation provides redox regulation of protein functions, but the global cellular impact of this transient post-translational modification remains unexplored. We describe a chemoproteomic workflow to map and quantify over 1,000 S-sulphenylation sites on more than 700 proteins in intact cells. Quantitative analysis of human cells stimulated with hydrogen peroxide or epidermal growth factor measured hundreds of site selective redox changes. Different cysteines in the same proteins displayed dramatic differences in susceptibility to S-sulphenylation. Newly discovered S-sulphenylations provided mechanistic support for proposed cysteine redox reactions and suggested novel redox mechanisms, including S-sulphenyl-mediated redox regulation of the transcription factor HIF1A by SIRT6. S-sulphenylation is favored at solvent-exposed protein surfaces and is associated with sequence motifs that are distinct from those for other thiol modifications. S-sulphenylations affect regulators of phosphorylation, acetylation and ubiquitylation, which suggest regulatory crosstalk between redox control and signalling pathways.

Suggested Citation

  • Jing Yang & Vinayak Gupta & Kate S. Carroll & Daniel C. Liebler, 2014. "Site-specific mapping and quantification of protein S-sulphenylation in cells," Nature Communications, Nature, vol. 5(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5776
    DOI: 10.1038/ncomms5776
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    Cited by:

    1. Yan Xu & Jun Ding & Ling-Yun Wu, 2016. "iSulf-Cys: Prediction of S-sulfenylation Sites in Proteins with Physicochemical Properties of Amino Acids," PLOS ONE, Public Library of Science, vol. 11(4), pages 1-9, April.

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