Research ArticleCell Biology

Spatial and temporal alterations in protein structure by EGF regulate cryptic cysteine oxidation

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Science Signaling  21 Jan 2020:
Vol. 13, Issue 615, eaay7315
DOI: 10.1126/scisignal.aay7315

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Uncovering cryptic cysteine residues for oxidation

Growth factor signaling results in the generation of reactive oxygen species (ROS) that oxidize cysteine residues in target proteins, triggering changes in activity, localization, or abundance. A long-standing question is how different growth factors specify the oxidation of cysteine residues in distinct subsets of proteins. Behring et al. found that many oxidized cysteine residues in target proteins were buried and not accessible under basal conditions. EGF stimulation altered the conformation of the target proteins through phosphorylation or nucleotide substrate flux, exposing the cryptic cysteine residues and enabling their oxidation. Thus, growth factor–mediated redox regulation of cysteine residues may be determined by changes in target protein conformation that occur in a pathway-specific manner.

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