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Science 24 December 1999: Vol. 286. no. 5449, pp. 2514 - 2517 DOI: 10.1126/science.286.5449.2514
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Reports
Reduced MAP Kinase Phosphatase-1 Degradation After p42/p44MAPK-Dependent Phosphorylation
Jean-Marc Brondello,
*
Jacques Pouysségur,
Fergus R. McKenzie
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.
To whom correspondence should be addressed. E-mail:
mckenzie{at}unice.fr
Read the Full Text
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- 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
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- 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
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- 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
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- 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
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- 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
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- 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
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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
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- Insulin-Induced c-Jun N-Terminal Kinase Activation Is Negatively Regulated by Protein Kinase C {{delta}}.
- K. Morino, H. Maegawa, T. Fujita, N. Takahara, K. Egawa, A. Kashiwagi, and R. Kikkawa (2001)
Endocrinology
142, 2669-2676
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- Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions.
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Endocr. Rev.
22, 153-183
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- Mitogen-activated protein kinase phosphatase is required for genotoxic stress relief in Arabidopsis.
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Genes & Dev.
15, 699-709
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- The proteasome regulates the UV-induced activation of the AP-1-like transcription factor Gcn4.
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Genes & Dev.
15, 128-133
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- The nucleus, a site for signal termination by sequestration and inactivation of p42/p44 MAP kinases.
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J. Cell Sci.
114, 3433-3443
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- Ptc1, a Type 2C Ser/Thr Phosphatase, Inactivates the HOG Pathway by Dephosphorylating the Mitogen-Activated Protein Kinase Hog1.
- J. Warmka, J. Hanneman, J. Lee, D. Amin, and I. Ota (2001)
Mol. Cell. Biol.
21, 51-60
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- Herpes Simplex Virus Type 1 ICP0 Protein Does Not Accumulate in the Nucleus of Primary Neurons in Culture.
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J. Virol.
74, 10132-10141
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- Sequential Activation of ERK and Repression of JNK by Scatter Factor/Hepatocyte Growth Factor in Madin-Darby Canine Kidney Epithelial Cells.
- R. Paumelle, D. Tulasne, C. Leroy, J. Coll, B. Vandenbunder, and V. Fafeur (2000)
Mol. Biol. Cell
11, 3751-3763
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- A Constitutive Active MEK right-arrow ERK Pathway Negatively Regulates NF-kappa B-dependent Gene Expression by Modulating TATA-binding Protein Phosphorylation.
- A. B. Carter and G. W. Hunninghake (2000)
J. Biol. Chem.
275, 27858-27864
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- Regulation of Dual-specificity Phosphatases M3/6 and hVH5 by Phorbol Esters. ANALYSIS OF A DELTA-LIKE DOMAIN.
- T. R. Johnson, J. R. Biggs, S. E. Winbourn, and A. S. Kraft (2000)
J. Biol. Chem.
275, 31755-31762
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- MAP Kinase Phosphatase-1 Gene Transcription in Rat Neuroendocrine Cells Is Modulated by a Calcium-sensitive Block to Elongation in the First Exon.
- S. Ryser, S. Tortola, G. van Haasteren, M. Muda, S. Li, and W. Schlegel (2001)
J. Biol. Chem.
276, 33319-33327
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- Activation of p42 Mitogen-activated Protein Kinase (MAPK), but not c-Jun NH2-Terminal Kinase, Induces Phosphorylation and Stabilization of MAPK Phosphatase XCL100 in Xenopus Oocytes.
- M. L. Sohaskey and J. E. Ferrell Jr. (2002)
Mol. Biol. Cell
13, 454-468
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- Thrombomodulin Prolongs Thrombin-Induced Extracellular Signal-Regulated Kinase Phosphorylation and Nuclear Retention in Endothelial Cells.
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Circ. Res.
88, 681-687
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