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. 2021 Apr 27;12:667343. doi: 10.3389/fimmu.2021.667343

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Copyright © 2021 Sen and Imlay

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Yap1p activation. H₂O₂ oxidizes the C36 residue of glutathione peroxidase (Gpx3). The resulting sulfenate interacts with C598 in the C-terminal domain of Yap1p to form a intermolecular disulfide bond. Subsequent thiol-disulfide exchange reactions produce C303-C598 and C310-C629 disulfide bonds in Yap1p. Yap1p accumulates in the nucleus, leading to the activation of the Yap1p regulated genes. When H₂O₂ diminishes, Yap1p is reduced by the thioredoxin system; this change makes its nuclear export signal accessible to Crm, causing Yap1p to be transported back out of the nucleus.