Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Sci. STKE, 10 October 2000
Vol. 2000, Issue 53, p. pe1
[DOI: 10.1126/stke.2000.53.pe1]

PERSPECTIVES

Hydrogen Peroxide: A Key Messenger That Modulates Protein Phosphorylation Through Cysteine Oxidation

Sue Goo Rhee, Yun Soo Bae, Seung-Rock Lee, and Jaeyul Kwon

S. G. Rhee, S.-R. Lee, and J. Kwon are at the Laboratory of Cell Signaling, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. E-mail: rheesg{at}nhlbi.nih.gov (S.G.R.)
Y. S. Bae is at the Center for Cell Signaling Research, Ewha Womans University, Seoul 120-750, Korea.

Abstract: Ligand-receptor interactions can generate the production of hydrogen peroxide (H2O2) in cells, the implications of which are becoming appreciated. Fluctuations in H2O2 levels can affect the intracellular activity of key signaling components including protein kinases and protein phosphatases. Rhee et al. discuss recent findings on the role of H2O2 in signal transduction. Specifically, H2O2 appears to oxidize active site cysteines in phosphatases, thereby inactivating them. H2O2 also can activate protein kinases; however, although the mechanism of activation for some kinases appears to be similar to that of phosphatase inactivation (cysteine oxidation), it is unclear how H2O2 promotes increased activation of other kinases. Thus, the higher levels of intracellular phosphoproteins observed in cells most likely occur because of the concomitant inhibition of protein phosphatases and activation of protein kinases.

Citation: S. G. Rhee, Y. S. Bae, S.-R. Lee, J. Kwon, Hydrogen Peroxide: A Key Messenger That Modulates Protein Phosphorylation Through Cysteine Oxidation. Sci. STKE 2000, pe1 (2000).

Read the Full Text

THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Mitochondria-derived Hydrogen Peroxide Selectively Enhances T Cell Receptor-initiated Signal Transduction.
T. Gill and A. D. Levine (2013)
J. Biol. Chem. 288, 26246-26255
   Abstract »    Full Text »    PDF »
Prolonged Production of Reactive Oxygen Species in Response to B Cell Receptor Stimulation Promotes B Cell Activation and Proliferation.
M. L. Wheeler and A. L. DeFranco (2012)
J. Immunol. 189, 4405-4416
   Abstract »    Full Text »    PDF »
Neuroprotective Effects of Reactive Oxygen Species Mediated by BDNF-Independent Activation of TrkB.
Y. Z. Huang and J. O. McNamara (2012)
J. Neurosci. 32, 15521-15532
   Abstract »    Full Text »    PDF »
Hydrogen peroxide enhances the expression of Gi{alpha} proteins in aortic vascular smooth cells: role of growth factor receptor transactivation.
N. Mbong and M. B. Anand-Srivastava (2012)
Am J Physiol Heart Circ Physiol 302, H1591-H1602
   Abstract »    Full Text »    PDF »
Mitochondrial redox signalling at a glance.
Y. Collins, E. T. Chouchani, A. M. James, K. E. Menger, H. M. Cocheme, and M. P. Murphy (2012)
J. Cell Sci. 125, 801-806
   Full Text »    PDF »
Sulfiredoxin Protein Is Critical for Redox Balance and Survival of Cells Exposed to Low Steady-state Levels of H2O2.
J. Y. Baek, S. H. Han, S. H. Sung, H. E. Lee, Y.-m. Kim, Y. H. Noh, S. H. Bae, S. G. Rhee, and T.-S. Chang (2012)
J. Biol. Chem. 287, 81-89
   Abstract »    Full Text »    PDF »
Hyperglycemia Enhances IGF-I-Stimulated Src Activation via Increasing Nox4-Derived Reactive Oxygen Species in a PKC{zeta}-Dependent Manner in Vascular Smooth Muscle Cells.
G. Xi, X. Shen, L. A. Maile, C. Wai, K. Gollahon, and D. R. Clemmons (2012)
Diabetes 61, 104-113
   Abstract »    Full Text »    PDF »
Regulation of protein tyrosine phosphatases by reversible oxidation.
A. Ostman, J. Frijhoff, A. Sandin, and F.-D. Bohmer (2011)
J. Biochem. 150, 345-356
   Abstract »    Full Text »    PDF »
ROS-induced ROS release in vascular biology: redox-redox signaling.
N. S. Zinkevich and D. D. Gutterman (2011)
Am J Physiol Heart Circ Physiol 301, H647-H653
   Abstract »    Full Text »    PDF »
Dual Oxidase 1 Induced by Th2 Cytokines Promotes STAT6 Phosphorylation via Oxidative Inactivation of Protein Tyrosine Phosphatase 1B in Human Epidermal Keratinocytes.
S. Hirakawa, R. Saito, H. Ohara, R. Okuyama, and S. Aiba (2011)
J. Immunol. 186, 4762-4770
   Abstract »    Full Text »    PDF »
Thiol peroxidases mediate specific genome-wide regulation of gene expression in response to hydrogen peroxide.
D. E. Fomenko, A. Koc, N. Agisheva, M. Jacobsen, A. Kaya, M. Malinouski, J. C. Rutherford, K.-L. Siu, D.-Y. Jin, D. R. Winge, et al. (2011)
PNAS 108, 2729-2734
   Abstract »    Full Text »    PDF »
Reactive oxygen species are indispensable in ovulation.
K. Shkolnik, A. Tadmor, S. Ben-Dor, N. Nevo, D. Galiani, and N. Dekel (2011)
PNAS 108, 1462-1467
   Abstract »    Full Text »    PDF »
Hydrogen Peroxide-Mediated Activation of MAP Kinase 6 Modulates Nitric Oxide Biosynthesis and Signal Transduction in Arabidopsis.
P. Wang, Y. Du, Y. Li, D. Ren, and C.-P. Song (2010)
PLANT CELL 22, 2981-2998
   Abstract »    Full Text »    PDF »
Reactive Oxygen Species Mediate Mitogenic Growth Factor Signaling Pathways in Human Leiomyoma Smooth Muscle Cells.
F. S. Mesquita, S. N. Dyer, D. A. Heinrich, S. E. Bulun, E. E. Marsh, and R. A. Nowak (2010)
Biol Reprod 82, 341-351
   Abstract »    Full Text »    PDF »
Bacterial-Modulated Signaling Pathways in Gut Homeostasis.
W.-J. Lee (2008)
Science Signaling 1, pe24
   Abstract »    Full Text »    PDF »
Localizing NADPH Oxidase-Derived ROS.
M. Ushio-Fukai (2006)
Sci. STKE 2006, re8
   Abstract »    Full Text »    PDF »

To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882