Hydrogen peroxide reactivity and specificity in thiol-based cell signalling

Biochem Soc Trans. 2020 Jun 30;48(3):745-754. doi: 10.1042/BST20190049.

Abstract

Reversible oxidation of thiol proteins is an important cell signalling mechanism. In many cases, this involves generation or exposure of the cells to H2O2, and oxidation of proteins that are not particularly H2O2-reactive. There is a conundrum as to how these proteins are oxidised when other highly reactive proteins such as peroxiredoxins are present. This article discusses potential mechanisms, focussing on recent evidence for oxidation being localised within the cell, redox relays involving peroxiredoxins operating in some signalling pathways, and mechanisms for facilitated or directed oxidation of specific targets. These findings help define conditions that enable redox signalling but there is still much to learn regarding mechanisms.

Keywords: hydrogen peroxide; peroxiredoxins; redox signalling; thiol oxidation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Aquaporins / metabolism
  • Carbonates / metabolism
  • Humans
  • Hydrogen Peroxide / metabolism*
  • Models, Theoretical
  • Nicotinamide Phosphoribosyltransferase / metabolism
  • Oxidation-Reduction
  • Oxygen / metabolism*
  • Peroxiredoxins / metabolism*
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1 / metabolism
  • Proteomics
  • Saccharomyces cerevisiae
  • Schizosaccharomyces
  • Signal Transduction*
  • Sulfhydryl Compounds / metabolism*

Substances

  • Aquaporins
  • Carbonates
  • Sulfhydryl Compounds
  • peroxycarbonic acid
  • Hydrogen Peroxide
  • Peroxiredoxins
  • Nicotinamide Phosphoribosyltransferase
  • PTPN1 protein, human
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1
  • Oxygen