Thioredoxins, glutaredoxins, and glutathionylation: new crosstalks to explore

被引：88

作者：

Michelet, Laure ^{[1
]}

Zaffagnini, Mirko ^{[1
]}

Massot, Vincent ^{[1
]}

Keryer, Eliane ^{[1
]}

Vanacker, Helene ^{[1
]}

Miginiac-Maslow, Myroslawa ^{[1
]}

Issakidis-Bourguet, Emmanuelle ^{[1
]}

Lemaire, Stephane D. ^{[1
]}

机构：

[1] Univ Paris 11, Inst Biotechnol Plantes, CNRS, UMR 8618, F-91405 Orsay, France

来源：

PHOTOSYNTHESIS RESEARCH | 2006年 / 89卷 / 2-3期

关键词：

Arabidopsis; Chlamydomonas; glutaredoxin; glutathione; glutathionylation; oxidants; photosynthetic organism; redox signaling; thioredoxin;

D O I：

10.1007/s11120-006-9096-2

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

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.

引用

页码：225 / 245

页数：21

共 225 条

[1] S-glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide [J].

Adachi, T ;

Weisbrod, RM ;

Pimentel, DR ;

Ying, J ;

Sharov, VS ;

Schöneich, C ;

Cohen, RA .

NATURE MEDICINE, 2004, 10 (11) :1200-1207

[2] S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells [J].

Adachi, T ;

Pimentel, DR ;

Heibeck, T ;

Hou, XY ;

Lee, YJ ;

Jiang, BB ;

Ido, Y ;

Cohen, RA .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (28) :29857-29862

[3] Reactive oxygen species: Metabolism, oxidative stress, and signal transduction [J].

Apel, K ;

Hirt, H .

ANNUAL REVIEW OF PLANT BIOLOGY, 2004, 55 :373-399

[4] Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria [J].

Åslund, F ;

Berndt, KD ;

Holmgren, A .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (49) :30780-30786

[5] Phloem sap proteins from Cucurbita maxima and Ricinus communis have the capacity to traffic cell to cell through plasmodesmata [J].

Balachandran, S ;

Xiang, Y ;

Schobert, C ;

Thompson, GA ;

Lucas, WJ .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (25) :14150-14155

[6] Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria [J].

Balmer, Y ;

Vensel, WH ;

Tanaka, CK ;

Hurkman, WJ ;

Gelhaye, E ;

Rouhier, N ;

Jacquot, JP ;

Manieri, W ;

Schüurmann, P ;

Droux, M ;

Buchanan, BB .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (08) :2642-2647

[7] Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts [J].

Balmer, Y ;

Koller, A ;

del Val, G ;

Schürmann, P ;

Buchanan, BB .

PHOTOSYNTHESIS RESEARCH, 2004, 79 (03) :275-280

[8] Proteomics gives insight into the regulatory function of chloroplast thioredoxins [J].

Balmer, Y ;

Koller, A ;

del Val, G ;

Manieri, W ;

Schürmann, P ;

Buchanan, BB .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (01) :370-375

[9] Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I [J].

Bandyopadhyay, S ;

Starke, DW ;

Mieyal, JJ ;

Gronostajski, RM .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (01) :392-397

[10] Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B [J].

Barrett, WC ;

DeGnore, JP ;

Keng, YF ;

Zhang, ZY ;

Yim, MB ;

Chock, PB .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (49) :34543-34546

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