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Science 16 April 1993:
Vol. 260. no. 5106, pp. 315 - 319
DOI: 10.1126/science.8385802
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Articles

Science, Vol 260, Issue 5106, 315-319
Copyright © 1993 by American Association for the Advancement of Science

articles

A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf

CA Lange-Carter, CM Pleiman, AM Gardner, KJ Blumer, and GL Johnson

Division of Basic Sciences, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206.

Mitogen-activated protein kinases (MAPKs) are rapidly phosphorylated and activated in response to various extracellular stimuli in many different cell types. Such regulation of MAPK results from sequential activation of a series of protein kinases. The kinases that phosphorylate MAPKs, the MAP kinase kinases (MEKs) are also activated by phosphorylation. MEKs are related in sequence to the yeast protein kinases Byr1 (from Schizosaccharomyces pombe) and Ste7 (from Saccharomyces cerevisiae), which function in the pheromone-induced signaling pathway that results in mating. Byr1 and Ste7 are in turn regulated by the protein kinases Byr2 and Ste11. The amino acid sequence of the mouse homolog of Byr2 and Ste11, denoted MEKK (MEK kinase), was elucidated from a complementary DNA sequence encoding a protein of 672 amino acid residues (73 kilodaltons). MEKK was expressed in all mouse tissues tested, and it phosphorylated and activated MEK. Phosphorylation and activation of MEK by MEKK was independent of Raf, a growth factor-regulated protein kinase that also phosphorylates MEK. Thus, MEKK and Raf converge at MEK in the protein kinase network mediating the activation of MAPKs by hormones, growth factors, and neurotransmitters.


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Differential Involvement of MEK Kinase 1 (MEKK1) in the Induction of Apoptosis in Response to Microtubule-targeted Drugs versus DNA Damaging Agents.
S. Gibson, C. Widmann, and G. L. Johnson (1999)
J. Biol. Chem. 274, 10916-10922
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Mitogen-activated Protein Kinase/ERK Kinase Kinases 2 and 3 Activate Nuclear Factor-kappa B through Ikappa B Kinase-alpha and Ikappa B Kinase-beta.
Q. Zhao and F. S. Lee (1999)
J. Biol. Chem. 274, 8355-8358
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Fas activates the JNK pathway in human colonic epithelial cells: lack of a direct role in apoptosis.
M. T. Abreu-Martin, A. A. Palladino, M. Faris, N. M. Carramanzana, A. E. Nel, and S. R. Targan (1999)
Am J Physiol Gastrointest Liver Physiol 276, G599-G605
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Hepatitis C Virus Core Protein Enhances NF-kappa B Signal Pathway Triggering by Lymphotoxin-beta Receptor Ligand and Tumor Necrosis Factor Alpha.
L.-R. You, C.-M. Chen, and Y.-H. W. Lee (1999)
J. Virol. 73, 1672-1681
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The MKK7 Gene Encodes a Group of c-Jun NH2-Terminal Kinase Kinases.
C. Tournier, A. J. Whitmarsh, J. Cavanagh, T. Barrett, and R. J. Davis (1999)
Mol. Cell. Biol. 19, 1569-1581
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A Novel Human STE20-related Protein Kinase, HGK, That Specifically Activates the c-Jun N-terminal Kinase Signaling Pathway.
Z. Yao, G. Zhou, X. S. Wang, A. Brown, K. Diener, H. Gan, and T.-H. Tan (1999)
J. Biol. Chem. 274, 2118-2125
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Functional Role for Protein Kinase Cbeta as a Regulator of Stress-Activated Protein Kinase Activation and Monocytic Differentiation of Myeloid Leukemia Cells.
M. Kaneki, S. Kharbanda, P. Pandey, K. Yoshida, M. Takekawa, J.-R. Liou, R. Stone, and D. Kufe (1999)
Mol. Cell. Biol. 19, 461-470
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