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Sci. Signal., 29 September 2009
Vol. 2, Issue 90, p. re7
[DOI: 10.1126/scisignal.290re7]

REVIEWS

Transduction of Redox Signaling by Electrophile-Protein Reactions

Tanja K. Rudolph1,2 and Bruce A. Freeman1*

1 Department of Pharmacology and Chemical Biology, University of Pittsburgh, Pittsburgh, PA 15261, USA.
2 Department of Cardiology, University Heart Center Hamburg, Hamburg, Germany.

Abstract: Over the last 50 years, the posttranslational modification (PTM) of proteins has emerged as a central mechanism for cells to regulate metabolism, growth, differentiation, cell-cell interactions, and immune responses. By influencing protein structure and function, PTM leads to a multiplication of proteome diversity. Redox-dependent PTMs, mediated by environmental and endogenously generated reactive species, induce cell signaling responses and can have toxic effects in organisms. PTMs induced by the electrophilic by-products of redox reactions most frequently occur at protein thiols; other nucleophilic amino acids serve as less favorable targets. Advances in mass spectrometry and affinity-chemistry strategies have improved the detection of electrophile-induced protein modifications both in vitro and in vivo and have revealed a high degree of amino acid and protein selectivity of electrophilic PTM. The identification of biological targets of electrophiles has motivated further study of the functional impact of various PTM reactions on specific signaling pathways and how this might affect organisms.

* Corresponding author. E-mail, freerad{at}pitt.edu

Citation: T. K. Rudolph, B. A. Freeman, Transduction of Redox Signaling by Electrophile-Protein Reactions. Sci. Signal. 2, re7 (2009).

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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