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ACS Chem Biol. 2010 Jan 15;5(1):47-62. doi: 10.1021/cb900258z.

Orchestrating redox signaling networks through regulatory cysteine switches.

Author information

1
Chemical Biology Graduate Program, Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-2216, USA.

Abstract

Hydrogen peroxide (H(2)O(2)) acts as a second messenger that can mediate intracellular signal transduction via chemoselective oxidation of cysteine residues in signaling proteins. This Review presents current mechanistic insights into signal-mediated H(2)O(2) production and highlights recent advances in methods to detect reactive oxygen species (ROS) and cysteine oxidation both in vitro and in cells. Selected examples from the recent literature are used to illustrate the diverse mechanisms by which H(2)O(2) can regulate protein function. The continued development of methods to detect and quantify discrete cysteine oxoforms should further our mechanistic understanding of redox regulation of protein function and may lead to the development of new therapeutic strategies.

PMID:
19957967
PMCID:
PMC4537063
DOI:
10.1021/cb900258z
[Indexed for MEDLINE]
Free PMC Article

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