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Science 24 December 1999:
Vol. 286. no. 5449, pp. 2514 - 2517
DOI: 10.1126/science.286.5449.2514

Reports

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}unice.fr


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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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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 »
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
   Abstract »    Full Text »    PDF »
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions.
G. Pearson, F. Robinson, T. Beers Gibson, B.-e Xu, M. Karandikar, K. Berman, and M. H. Cobb (2001)
Endocr. Rev. 22, 153-183
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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
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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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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.
X.-p. Chen, J. Li, M. Mata, J. Goss, D. Wolfe, J. C. Glorioso, and D. J. Fink (2000)
J. Virol. 74, 10132-10141
   Abstract »    Full Text »
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
   Abstract »    Full Text »    PDF »
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.
J.-M. Olivot, E. Estebanell, M. Lafay, B. Brohard, M. Aiach, and F. Rendu (2001)
Circ. Res. 88, 681-687
   Abstract »    Full Text »    PDF »



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