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Thioredoxins, glutaredoxins, and glutathionylation: new crosstalks to explore

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Abstract

Oxidants are widely considered as toxic molecules that cells have to scavenge and detoxify efficiently and continuously. However, emerging evidence suggests that these oxidants can play an important role in redox signaling, mainly through a set of reversible post-translational modifications of thiol residues on proteins. The most studied redox system in photosynthetic organisms is the thioredoxin (TRX) system, involved in the regulation of a growing number of target proteins via thiol/disulfide exchanges. In addition, recent studies suggest that glutaredoxins (GRX) could also play an important role in redox signaling especially by regulating protein glutathionylation, a post-translational modification whose importance begins to be recognized in mammals while much less is known in photosynthetic organisms. This review focuses on oxidants and redox signaling with particular emphasis on recent developments in the study of functions, regulation mechanisms and targets of TRX, GRX and glutathionylation. This review will also present the complex emerging interplay between these three components of redox-signaling networks.

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Abbreviations

GAPDH:

Glyceraldehyde-3-phosphate dehydrogenase

GRX:

Glutaredoxin

GSH:

Reduced glutathione

GSSG:

Oxidized glutathione

H2O2 :

Hydrogen peroxide

MSR:

Methionine sulfoxide reductase

NO· :

Nitric oxide radical

NTR:

NADPH TRX reductase

PCD:

Programmed cell death

PKC:

Protein kinase C

PRX:

Peroxiredoxin

PTP:

Protein tyrosine phosphatase

RNS:

Reactive nitrogen species

ROS:

Reactive oxygen species

SOH:

Sulfenic acid

SO2H:

Sulfinic acid

SO3H:

Sulfonic acid

TPI:

Triose phosphate isomerase

TRX:

Thioredoxin

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Acknowledgments

This work was supported by Agence Nationale de la Recherche Grant JC-45751 (to S.D.L.).

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  1. Institut de Biotechnologie des Plantes, Unité Mixte de Recherche 8618, Centre National de la Recherche Scientifique/Université Paris-Sud, Bâtiment 630, Orsay Cedex, 91405, France

    Laure Michelet, Mirko Zaffagnini, Vincent Massot, Eliane Keryer, Hélène Vanacker, Myroslawa Miginiac-Maslow, Emmanuelle Issakidis-Bourguet & Stéphane D. Lemaire

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  1. Laure Michelet
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  2. Mirko Zaffagnini
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  3. Vincent Massot
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  7. Emmanuelle Issakidis-Bourguet
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  8. Stéphane D. Lemaire
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Correspondence to Stéphane D. Lemaire.

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Michelet, L., Zaffagnini, M., Massot, V. et al. Thioredoxins, glutaredoxins, and glutathionylation: new crosstalks to explore. Photosynth Res 89, 225–245 (2006). https://doi.org/10.1007/s11120-006-9096-2

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  • DOI: https://doi.org/10.1007/s11120-006-9096-2

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