JOURNAL BROWSE
Search
Advanced SearchSearch Tips
Peroxiredoxins in Regulation of MAPK Signalling Pathways; Sensors and Barriers to Signal Transduction
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
  • Journal title : Molecules and Cells
  • Volume 39, Issue 1,  2016, pp.40-45
  • Publisher : Korea Society for Molecular and Cellular Biology
  • DOI : 10.14348/molcells.2016.2327
 Title & Authors
Peroxiredoxins in Regulation of MAPK Signalling Pathways; Sensors and Barriers to Signal Transduction
Latimer, Heather R.; Veal, Elizabeth A.;
  PDF(new window)
 Abstract
Peroxiredoxins are highly conserved and abundant peroxidases. Although the thioredoxin peroxidase activity of peroxiredoxin (Prx) is important to maintain low levels of endogenous hydrogen peroxide, Prx have also been shown to promote hydrogen peroxide-mediated signalling. Mitogen activated protein kinase (MAPK) signalling pathways mediate cellular responses to a variety of stimuli, including reactive oxygen species (ROS). Here we review the evidence that Prx can act as both sensors and barriers to the activation of MAPK and discuss the underlying mechanisms involved, focusing in particular on the relationship with thioredoxin.
 Keywords
kinase;peroxiredoxin;phosphatase;redox;thioredoxin;
 Language
English
 Cited by
1.
Overview on Peroxiredoxin,;

Molecules and Cells, 2016. vol.39. 1, pp.1-5 crossref(new window)
1.
Vitamin K2 Induces Mitochondria-Related Apoptosis in Human Bladder Cancer Cells via ROS and JNK/p38 MAPK Signal Pathways, PLOS ONE, 2016, 11, 8, e0161886  crossref(new windwow)
2.
The Role of Peroxiredoxins in the Transduction of H2O2 Signals, Antioxidants & Redox Signaling, 2017  crossref(new windwow)
3.
Overview on Peroxiredoxin, Molecules and Cells, 2016, 39, 1, 1  crossref(new windwow)
4.
An Atlas of Peroxiredoxins Created Using an Active Site Profile-Based Approach to Functionally Relevant Clustering of Proteins, PLOS Computational Biology, 2017, 13, 2, e1005284  crossref(new windwow)
5.
Differential representation of liver proteins in obese human subjects suggests novel biomarkers and promising targets for drug development in obesity, Journal of Enzyme Inhibition and Medicinal Chemistry, 2017, 32, 1, 672  crossref(new windwow)
6.
Experimentally Dissecting the Origins of Peroxiredoxin Catalysis, Antioxidants & Redox Signaling, 2017  crossref(new windwow)
7.
Dietary oxidized tyrosine (O-Tyr) stimulates TGF-β1-induced extracellular matrix production via the JNK/p38 signaling pathway in rat kidneys, Amino Acids, 2017, 49, 2, 241  crossref(new windwow)
8.
The active site architecture in peroxiredoxins: a case study on Mycobacterium tuberculosis AhpE, Chem. Commun., 2016, 52, 67, 10293  crossref(new windwow)
9.
Aspergillus fumigatus -induced early inflammatory response in pulmonary microvascular endothelial cells: Role of p38 MAPK and inhibition by silibinin, International Immunopharmacology, 2017, 49, 195  crossref(new windwow)
10.
New Challenges to Study Heterogeneity in Cancer Redox Metabolism, Frontiers in Cell and Developmental Biology, 2017, 5  crossref(new windwow)
11.
Activation of adrenergic receptor in H9c2 cardiac myoblasts co-stimulates Nox2 and the derived ROS mediate the downstream responses, Molecular and Cellular Biochemistry, 2017  crossref(new windwow)
12.
Enhancement of CCL2 expression and monocyte migration by CCN1 in osteoblasts through inhibiting miR-518a-5p: implication of rheumatoid arthritis therapy, Scientific Reports, 2017, 7, 1  crossref(new windwow)
 References
1.
Bokov, A., Chaudhuri, A., and Richardson, A. (2004). The role of oxidative damage and stress in aging. Mech. Ageing Dev. 125, 811-826. crossref(new window)

2.
Bozonet, S.M., Findlay, V.J., Day, A.M., Cameron, J., Veal, E.A., and Morgan, B.A. (2005). Oxidation of a eukaryotic 2-Cys peroxiredoxin is a molecular switch controlling the transcriptional response to increasing levels of hydrogen peroxide. J. Biol. Chem. 280, 23319-23327. crossref(new window)

3.
Brown, J.D., Day, A.M., Taylor. S.R., Tomalin, L.E., Morgan, B.A., and Veal, E.A.. (2013). A peroxiredoxin promotes H2O2 signaling and oxidative stress resistance by oxidizing a thioredoxin family protein. Cell Rep. 5, 1425-1435. crossref(new window)

4.
Cao, J., Schulte, J., Knight, A., Leslie, N.R., Zagozdzon, A., Bronson, R., Manevich, Y., Beeson, C., and Neumann, C.A. (2009). Prdx1 inhibits tumorigenesis via regulating PTEN/AKT activity. EMBO J. 28, 1505-1517. crossref(new window)

5.
Choi, M.H., Lee, I.K., Kim, G.W., Kim, B.U., Han, Y.H., Yu, D.Y., Park, H.S., Kim, K.Y., Lee, J.S., Choi. C., et al. (2005). Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II. Nature 435, 347-353. crossref(new window)

6.
Conway, J.P., and Kinter, M. (2006). Dual role of peroxiredoxin I in macrophage-derived foam cells. J. Biol. Chem. 281, 27991-28001. crossref(new window)

7.
da Silva Dantas, A., Patterson, M.J., Smith, D.A., Maccallum, D.M., Erwig, L.P., Morgan, B.A., and Quinn, J. (2010). Thioredoxin regulates multiple hydrogen peroxide-induced signaling pathways in Candida albicans. Mol. Cell. Biol. 30, 4550-4563. crossref(new window)

8.
Day, A.M., and Veal, E.A. (2010). Hydrogen peroxide-sensitive cysteines in the Sty1 MAPK regulate the transcriptional response to oxidative stress. J. Biol. Chem. 285, 7505-7516. crossref(new window)

9.
Day, A.M., Brown, J.D., Taylor, S.R., Rand, J.D., Morgan, B.A., and Veal EA. (2012). Inactivation of a peroxiredoxin by hydrogen peroxide is critical for thioredoxin-mediated repair of oxidized proteins and cell survival. Mol. Cell 45, 398-408. crossref(new window)

10.
Gotoh, Y., and Cooper, J.A. (1998). Reactive oxygen species- and dimerization-induced activation of apoptosis signal-regulating kinase 1 in tumor necrosis factor-alpha signal transduction. J. Biol. Chem. 273, 17477-17482. crossref(new window)

11.
Gutteridge, J.M.C., and Halliwell, B. (1999). Free Radicals in Biology and Medicine. (Oxford, UK: Oxford University Press).

12.
Hashimoto, S., Gon, Y., Matsumoto, K., Takeshita, I., and Horie, T. (2001). N-acetylcysteine attenuates TNF-alpha-induced p38 MAP kinase activation and p38 MAP kinase-mediated IL-8 production by human pulmonary vascular endothelial cells. Br J. Pharmacol. 132, 270-276. crossref(new window)

13.
Holmgren, A., and Lu, J. (2010). Thioredoxin and thioredoxin reductase: current research with special reference to human disease. Biochem. Biophys. Res. Commun. 396, 120-124. crossref(new window)

14.
Holmström, K.M., and Finkel, T. (2014). Cellular mechanisms and physiological consequences of redox-dependent signalling. Nat. Rev. Mol. Cell Biol. 15, 411-421. crossref(new window)

15.
Ichijo, H., Nishida, E., Irie, K., ten Dijke, P., Saitoh, M., Moriguchi, T., Takagi, M., Matsumoto, K., Miyazono, K., and Gotoh, Y. (1997). Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. Science 275, 90-94. crossref(new window)

16.
Jang, H.H., Lee, K.O., Chi, Y.H., Jung, B.G., Park, S.K., Park, J.H., Lee, J.R., Lee, S.S., Moon, J.C., Yun, J.W., et al. (2004). Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function. Cell 117, 625-635. crossref(new window)

17.
Jarvis, R.M., Hughes, S.M., and Ledgerwood, E.C. (2012). Peroxiredoxin 1 functions as a signal peroxidase to receive, transduce, and transmit peroxide signals in mammalian cells. Free Radic. Biol. Med. 53, 1522-1530. crossref(new window)

18.
Kang, S.W., Chang, T.S., Lee, T.H., Kim, E.S., Yu, D.Y., and Rhee, S.G. (2004). Cytosolic peroxiredoxin attenuates the activation of Jnk and p38 but potentiates that of Erk in Hela cells stimulated with tumor necrosis factor-alpha. J. Biol. Chem. 279, 2535-2543. crossref(new window)

19.
Kil, I.S., Lee, S.K., Ryu, K.W., Woo, H.A., Hu, M.C., Bae, S.H., and Rhee, S.G. (2012). Feedback control of adrenal steroidogenesis via H2O2-dependent, reversible inactivation of peroxiredoxin III in mitochondria. Mol. Cell 46, 584-594. crossref(new window)

20.
Kil, I.S., Ryu, K.W., Lee, S.K., Kim, J.Y., Chu, S.Y., Kim, J.H., Park, S., and Rhee, S.G. (2015). Circadian oscillation of sulfiredoxin in the mitochondria. Mol. Cell 59, 651-663. crossref(new window)

21.
Kwon, J., Lee, S.R., Yang, K.S., Ahn, Y., Kim, Y.J., Stadtman, E.R., and Rhee, S.G. (2004). Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. Proc. Natl. Acad. Sci. USA 101, 16419-16424. crossref(new window)

22.
Marshall, C.J. (1994). MAP kinase kinase kinase, MAP kinase kinase and MAP kinase. Curr. Opin. Genet. Dev. 4, 82-89. crossref(new window)

23.
Nadeau, P.J., Charette, S.J., Toledano, M.B., and Landry, J. (2007). Disulfide Bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H(2)O(2)-induced c-Jun NH(2)-terminal kinase activation and apoptosis. Mol. Biol. Cell 18, 3903-3913. crossref(new window)

24.
Nadeau, P.J., Charette, S.J., and Landry, J. (2009). REDOX reaction at ASK1-Cys250 is essential for activation of JNK and induction of apoptosis. Mol. Biol. Cell 20, 3628-3637. crossref(new window)

25.
Nguyen, A.N., and Shiozaki, K. (1999). Heat-shock-induced activation of stress MAP kinase is regulated by threonine- and tyrosine-specific phosphatases. Genes Dev. 13, 1653-1663. crossref(new window)

26.
Okazaki, S., Naganuma, A., and Kuge, S. (2005). Peroxiredoxinmediated redox regulation of the nuclear localization of Yap1, a transcription factor in budding yeast. Antioxid. Redox Signal. 7, 327-334. crossref(new window)

27.
Olahova, M., Taylor, S.R., Khazaipoul, S., Wang, J., Morgan, B.A., Matsumoto, K., Blackwell, T.K., and Veal, E.A. (2008). A redoxsensitive peroxiredoxin that is important for longevity has tissueand stress-specific roles in stress resistance. Proc. Natl. Acad. Sci. USA 105, 19839-19844. crossref(new window)

28.
Ross, S.J., Findlay, V.J., Malakasi, P., and Morgan, B.A. (2000). Thioredoxin peroxidase is required for the transcriptional response to oxidative stress in budding yeast. Mol. Biol. Cell 11, 2631-2642. crossref(new window)

29.
Sabio, G., and Davis, R.J. (2014). TNF and MAP kinase signalling pathways. Semin. Immunol. 26, 237-245. crossref(new window)

30.
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., and Ichijo, H. (1998). Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J. 17, 2596-2606. crossref(new window)

31.
Schwertassek, U., Haque, A., Krishnan, N., Greiner, R., Weingarten, L., Dick, T.P., and Tonks, N.K. (2014). Reactivation of oxidized PTP1B and PTEN by thioredoxin 1. FEBS J, 281, 3545-3558. crossref(new window)

32.
Sobotta, M.C., Liou, W., Stocker, S., Talwar, D., Oehler, M., Ruppert, T., Scharf, A.N., and Dick, T.P. (2015). Peroxiredoxin-2 and STAT3 form a redox relay for H2O2 signaling. Nat. Chem. Biol. 11, 64-70.

33.
Taniuchi, K., Furihata, M., Hanazaki, K., Iwasaki, S., Tanaka, K., Shimizu, T., Saito, M., and Saibara, T. (2015). Peroxiredoxin 1 promotes pancreatic cancer cell invasion by modulating p38 MAPK activity. Pancreas 44, 331-340. crossref(new window)

34.
Tobiume, K., Matsuzawa, A., Takahashi, T., Nishitoh, H., Morita, K., Takeda, K., Minowa, O., Miyazono, K., Noda, T., and Ichijo, H. (2001). ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis. EMBO Rep. 2, 222-228. crossref(new window)

35.
Toone, W.M., and Jones, N. (1998). Stress-activated signalling pathways in yeast. Genes Cells 3, 485-498. crossref(new window)

36.
Turner-Ivey, B., Manevich, Y., Schulte, J., Kistner-Griffin, E., Jezierska-Drutel, A., Liu, Y., and Neumann, C.A. (2013). Role for Prdx1 as a specific sensor in redox-regulated senescence in breast cancer. Oncogene 32, 5302-5314. crossref(new window)

37.
Veal, E., and Day, A. (2011). Hydrogen peroxide as a signaling molecule. Antioxid. Redox Signal. 15, 147-151. crossref(new window)

38.
Veal, E.A., Findlay, V.J., Day, A.M., Bozonet, S.M., Evans, J.M., Quinn, J., and Morgan, B.A. (2004). A 2-Cys peroxiredoxin regulates peroxide-induced oxidation and activation of a stressactivated MAP kinase. Mol. Cell 15, 129-139. crossref(new window)

39.
Veal, E.A., Tomalin, L.E., Morgan, B.A., and Day, A.M. (2014). The fission yeast Schizosaccharomyces pombe as a model to understand how peroxiredoxins influence cell responses to hydrogen peroxide. Biochem. Soc. Trans. 42, 909-916. crossref(new window)

40.
Vivancos AP1, Castillo EA, Biteau B, Nicot C, Ayté J, Toledano MB, Hidalgo E. (2005). A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway. Proc. Natl. Acad. Sci. USA 102, 8875-8880. crossref(new window)

41.
Winterbourn, C.C. (2008). Reconciling the chemistry and biology of reactive oxygen species. Nat. Chem. Biol. 4, 278-286. crossref(new window)

42.
Woo, H.A., Yim, S.H., Shin, D.H., Kang, D., Yu, D.Y., and Rhee, S.G. (2010). Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. Cell 140, 517-528. crossref(new window)

43.
Wood, Z.A., Schröder, E., Robin Harris, J., and Poole, L.B. (2003). Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 28, 32-40. crossref(new window)

44.
Yang, C.S., Lee, D.S., Song, C.H., An, S.J., Li, S., Kim, J.M., Kim, C.S., Yoo, D.G., Jeon, B.H., Yang, H.Y., et al. (2007). Roles of peroxiredoxin II in the regulation of proinflammatory responses to LPS and protection against endotoxin-induced lethal shock. J. Exp. Med. 204, 583-594. crossref(new window)

45.
Yang, K.S., Kang, S.W., Woo, H.A., Hwang, S.C., Chae, H.Z., Kim, K., and Rhee, S.G. (2002). Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J. Biol. Chem. 277, 38029-38036. crossref(new window)