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Science 286 (5449): 2514-2517

Copyright © 1999 by the American Association for the Advancement of Science

Reduced MAP Kinase Phosphatase-1 Degradation After p42/p44MAPK-Dependent Phosphorylation

Jean-Marc Brondello, * Jacques Pouysségur, Fergus R. McKenzie dagger

The mitogen-activated protein (MAP) kinase cascade is inactivated at the level of MAP kinase by members of the MAP kinase phosphatase (MKP) family, including MKP-1. MKP-1 was a labile protein in CCL39 hamster fibroblasts; its degradation was attenuated by inhibitors of the ubiquitin-directed proteasome complex. MKP-1 was a target in vivo and in vitro for p42MAPK or p44MAPK, which phosphorylates MKP-1 on two carboxyl-terminal serine residues, Serine 359 and Serine 364. This phosphorylation did not modify MKP-1's intrinsic ability to dephosphorylate p44MAPK but led to stabilization of the protein. These results illustrate the importance of regulated protein degradation in the control of mitogenic signaling.

Institute of Signaling, Developmental Biology and Cancer Research, CNRS UMR 6543, Centre A. Lacassagne, 33 Avenue de Valombrose, Nice 06189, France.
*   Present address: The Scripps Research Institute, Department of Molecular Biology, MB-3, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

dagger    To whom correspondence should be addressed. E-mail: mckenzie{at}

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Differential regulation of p38 mitogen-activated protein kinase mediates gender-dependent catecholamine-induced hypertrophy.
R. Dash, A. G Schmidt, A. Pathak, M. J Gerst, D. Biniakiewicz, V. J Kadambi, B. D Hoit, W. T Abraham, and E. G Kranias (2003)
Cardiovasc Res 57, 704-714
   Abstract »    Full Text »    PDF »
Inhibition of Protein Tyrosine/Mitogen-Activated Protein Kinase Phosphatase Activity Is Associated with D2 Dopamine Receptor Supersensitivity in a Rat Model of Parkinson's Disease.
X. Zhen, C. Torres, G. Cai, and E. Friedman (2002)
Mol. Pharmacol. 62, 1356-1363
   Abstract »    Full Text »    PDF »
Restraint of Proinflammatory Cytokine Biosynthesis by Mitogen-Activated Protein Kinase Phosphatase-1 in Lipopolysaccharide-Stimulated Macrophages.
P. Chen, J. Li, J. Barnes, G. C. Kokkonen, J. C. Lee, and Y. Liu (2002)
J. Immunol. 169, 6408-6416
   Abstract »    Full Text »    PDF »
Dexamethasone Causes Sustained Expression of Mitogen-Activated Protein Kinase (MAPK) Phosphatase 1 and Phosphatase-Mediated Inhibition of MAPK p38.
M. Lasa, S. M. Abraham, C. Boucheron, J. Saklatvala, and A. R. Clark (2002)
Mol. Cell. Biol. 22, 7802-7811
   Abstract »    Full Text »    PDF »
Sustained Activation of the Extracellular Signal-regulated Kinase Pathway Protects Cells from Photofrin-mediated Photodynamic Therapy.
Z. Tong, G. Singh, and A. J. Rainbow (2002)
Cancer Res. 62, 5528-5535
   Abstract »    Full Text »    PDF »
IEX-1: a new ERK substrate involved in both ERK survival activity and ERK activation.
J. Garcia, Y. Ye, V. Arranz, C. Letourneux, G. Pezeron, and F. Porteu (2002)
EMBO J. 21, 5151-5163
   Abstract »    Full Text »    PDF »
The Dual Specificity JKAP Specifically Activates the c-Jun N-terminal Kinase Pathway.
A. J. Chen, G. Zhou, T. Juan, S. M. Colicos, J. P. Cannon, M. Cabriera-Hansen, C. F. Meyer, R. Jurecic, N. G. Copeland, D. J. Gilbert, et al. (2002)
J. Biol. Chem. 277, 36592-36601
   Abstract »    Full Text »    PDF »
MAP Kinase Phosphatase As a Locus of Flexibility in a Mitogen-Activated Protein Kinase Signaling Network.
U. S. Bhalla, P. T. Ram, and R. Iyengar (2002)
Science 297, 1018-1023
   Abstract »    Full Text »    PDF »
Evidence That Inhibition of p44/42 Mitogen-activated Protein Kinase Signaling Is a Factor in Proteasome Inhibitor-mediated Apoptosis.
R. Z. Orlowski, G. W. Small, and Y. Y. Shi (2002)
J. Biol. Chem. 277, 27864-27871
   Abstract »    Full Text »    PDF »
Identification of Two Sp1 Phosphorylation Sites for p42/p44 Mitogen-activated Protein Kinases: THEIR IMPLICATION IN VASCULAR ENDOTHELIAL GROWTH FACTOR GENE TRANSCRIPTION.
J. Milanini-Mongiat, J. Pouyssegur, and G. Pages (2002)
J. Biol. Chem. 277, 20631-20639
   Abstract »    Full Text »    PDF »
Cross-talk between ERK and p38 MAPK Mediates Selective Suppression of Pro-inflammatory Cytokines by Transforming Growth Factor-{beta}.
Y. Q. Xiao, K. Malcolm, G. S. Worthen, S. Gardai, W. P. Schiemann, V. A. Fadok, D. L. Bratton, and P. M. Henson (2002)
J. Biol. Chem. 277, 14884-14893
   Abstract »    Full Text »    PDF »
Estrogen Activates Phosphatases and Antagonizes Growth-Promoting Effect of Angiotensin II.
Y. Takeda-Matsubara, H. Nakagami, M. Iwai, T.-X. Cui, T. Shiuchi, M. Akishita, C. Nahmias, M. Ito, and M. Horiuchi (2002)
Hypertension 39, 41-45
   Abstract »    Full Text »    PDF »
Glucocorticoids inhibit MAP kinase via increased expression and decreased degradation of MKP-1.
O. Kassel, A. Sancono, J. Kratzschmar, B. Kreft, M. Stassen, and A. C. B. Cato (2001)
EMBO J. 20, 7108-7116
   Abstract »    Full Text »    PDF »
Transcriptional Induction of MKP-1 in Response to Stress Is Associated with Histone H3 Phosphorylation-Acetylation.
J. Li, M. Gorospe, D. Hutter, J. Barnes, S. M. Keyse, and Y. Liu (2001)
Mol. Cell. Biol. 21, 8213-8224
   Abstract »    Full Text »    PDF »
The nucleus, a site for signal termination by sequestration and inactivation of p42/p44 MAP kinases.
V. Volmat, M. Camps, S. Arkinstall, J. Pouyssegur, and P. Lenormand (2001)
J. Cell Sci. 114, 3433-3443
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Hyperactivation of P21ras and the Hematopoietic-Specific Rho Gtpase, Rac2, Cooperate to Alter the Proliferation of Neurofibromin-Deficient Mast Cells in Vivo and in Vitro.
D. A. Ingram, K. Hiatt, A. J. King, L. Fisher, R. Shivakumar, C. Derstine, M. J. Wenning, B. Diaz, J. B. Travers, A. Hood, et al. (2001)
J. Exp. Med. 194, 57-70
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PTP-{epsilon}, a tyrosine phosphatase expressed in endothelium, negatively regulates endothelial cell proliferation.
L. J. Thompson, J. Jiang, N. Madamanchi, M. S. Runge, and C. Patterson (2001)
Am J Physiol Heart Circ Physiol 281, H396-H403
   Abstract »    Full Text »    PDF »
Mitogen-activated protein kinase phosphatase is required for genotoxic stress relief in Arabidopsis.
R. Ulm, E. Revenkova, G.-P. di Sansebastiano, N. Bechtold, and J. Paszkowski (2001)
Genes & Dev. 15, 699-709
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The proteasome regulates the UV-induced activation of the AP-1-like transcription factor Gcn4.
M. L. Stitzel, R. Durso, and J. C. Reese (2001)
Genes & Dev. 15, 128-133
   Abstract »    Full Text »

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