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Redox regulation

Scaffolding H2O2 signaling

Nature Chemical Biology volume 13, pages 818–819 (2017)Cite this article

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Peroxidases, rather than simply reducing H2O2 to water, also convey oxidation signals to proteins such as transcription factors. A new study reveals how a scaffold protein enables formation of a mixed disulfide between the peroxidase and a transcription factor.

Mysteries continue to abound in the field of redox signaling. Although it is well established that the thiol–disulfide transitions that activate transcription factors, kinases, and phosphatases in living cells are controlled by reaction kinetics, oxidation products that seem to be kinetically disfavored are widely observed. In this issue, Bersweiler et al.1 provide a compelling answer to the fundamental question of how H2O2 is able to overcome these kinetic barriers to induce the oxidation of transcription factors such as Yap1 in yeast.

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Figure 1: A ternary complex ensures H2O2-mediated oxidation of Yap1.

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  1. Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA

    Hadley D Sikes

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  1. Hadley D Sikes
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Correspondence to Hadley D Sikes.

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Sikes, H. Scaffolding H2O2 signaling. Nat Chem Biol 13, 818–819 (2017). https://doi.org/10.1038/nchembio.2432

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