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Science 22 May 1998:
Vol. 280. no. 5367, pp. 1262 - 1265
DOI: 10.1126/science.280.5367.1262
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Reports

Catalytic Activation of the Phosphatase MKP-3 by ERK2 Mitogen-Activated Protein Kinase

Montserrat Camps, * Anthony Nichols, * Corine Gillieron, * Bruno Antonsson, * Marco Muda, dagger Christian Chabert, * Ursula Boschert, * Steve Arkinstall *ddagger

MAP kinase phosphatase-3 (MKP-3) dephosphorylates phosphotyrosine and phosphothreonine and inactivates selectively ERK family mitogen-activated protein (MAP) kinases. MKP-3 was activated by direct binding to purified ERK2. Activation was independent of protein kinase activity and required binding of ERK2 to the noncatalytic amino-terminus of MKP-3. Neither the gain-of-function Sevenmaker ERK2 mutant D319N nor c-Jun amino-terminal kinase-stress-activated protein kinase (JNK/SAPK) or p38 MAP kinases bound MKP-3 or caused its catalytic activation. These kinases were also resistant to enzymatic inactivation by MKP-3. Another homologous but nonselective phosphatase, MKP-4, bound and was activated by ERK2, JNK/SAPK, and p38 MAP kinases. Catalytic activation of MAP kinase phosphatases through substrate binding may regulate MAP kinase activation by a large number of receptor systems.

Geneva Biomedical Research Institute, Glaxo Wellcome Research and Development S.A., CH-1228 Plan-les-Ouates, Geneva, Switzerland.
*   Present address: Serono Pharmaceutical Research Institute, CH-1228, Plan-les-Ouates, Geneva, Switzerland.

dagger    Present Address: Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.

ddagger    To whom correspondence should be addressed. E-mail: steve.arkinstall{at}serono.com

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   Abstract »    Full Text »    PDF »
Activation of JNK, p38 and ERK mitogen-activated protein kinases by chromium(VI) is mediated through oxidative stress but does not affect cytotoxicity.
S.-M. Chuang, G.-Y. Liou, and J.-L. Yang (2000)
Carcinogenesis 21, 1491-1500
   Abstract »    Full Text »    PDF »
A Role for the MEK-MAPK Pathway in Okadaic Acid-Induced Meiotic Resumption of Incompetent Growing Mouse Oocytes.
C. de Vantéry Arrighi, A. Campana, and S. Schorderet-Slatkine (2000)
Biol Reprod 63, 658-665
   Abstract »    Full Text »
Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium.
S.-M. Chuang, I-C. Wang, and J.-L. Yang (2000)
Carcinogenesis 21, 1423-1432
   Abstract »    Full Text »    PDF »
Mechanical stress-induced cardiac hypertrophy: mechanisms and signal transduction pathways.
C. Ruwhof and A. van der Laarse (2000)
Cardiovasc Res 47, 23-37
   Abstract »    Full Text »    PDF »
Abrogation of Nerve Growth Factor-induced Terminal Differentiation by ret Oncogene Involves Perturbation of Nuclear Translocation of ERK.
G. L. Colucci-D'Amato, A. D'Alessio, D. Califano, G. Cali, C. Rizzo, L. Nitsch, G. Santelli, and V. de Franciscis (2000)
J. Biol. Chem. 275, 19306-19314
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The Dual-Specificity Protein Phosphatase Yvh1p Regulates Sporulation, Growth, and Glycogen Accumulation Independently of Catalytic Activity in Saccharomyces cerevisiae via the Cyclic AMP-Dependent Protein Kinase Cascade.
A. E. Beeser and T. G. Cooper (2000)
J. Bacteriol. 182, 3517-3528
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Mechanistic Basis for Catalytic Activation of Mitogen-activated Protein Kinase Phosphatase 3 by Extracellular Signal-regulated Kinase.
C. C. Fjeld, A. E. Rice, Y. Kim, K. R. Gee, and J. M. Denu (2000)
J. Biol. Chem. 275, 6749-6757
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Posttranslational Modification of Bcl-2 Facilitates Its Proteasome-Dependent Degradation: Molecular Characterization of the Involved Signaling Pathway.
K. Breitschopf, J. Haendeler, P. Malchow, A. M. Zeiher, and S. Dimmeler (2000)
Mol. Cell. Biol. 20, 1886-1896
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Dual specificity phosphatases: a gene family for control of MAP kinase function.
M. CAMPS, A. NICHOLS, and S. ARKINSTALL (2000)
FASEB J 14, 6-16
   Abstract »    Full Text »
Mechanism of Mitogen-activated Protein Kinase Phosphatase-3 Activation by ERK2.
B. Zhou and Z.-Y. Zhang (1999)
J. Biol. Chem. 274, 35526-35534
   Abstract »    Full Text »    PDF »
A specific protein-protein interaction accounts for the in vivo substrate selectivity of Ptp3 towards the Fus3 MAP kinase.
X.-L. Zhan and K.-L. Guan (1999)
Genes & Dev. 13, 2811-2827
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Activation of the Saccharomyces cerevisiae Filamentation/Invasion Pathway by Osmotic Stress in High-Osmolarity Glycogen Pathway Mutants.
K. D. Davenport, K. E. Williams, B. D. Ullmann, and M. C. Gustin (1999)
Genetics 153, 1091-1103
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Identification of a Cytoplasmic-Retention Sequence in ERK2.
H. Rubinfeld, T. Hanoch, and R. Seger (1999)
J. Biol. Chem. 274, 30349-30352
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