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Science 11 September 1998:
Vol. 281. no. 5383, pp. 1668 - 1671
DOI: 10.1126/science.281.5383.1668
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Reports

MP1: A MEK Binding Partner That Enhances Enzymatic Activation of the MAP Kinase Cascade

Hans J. Schaeffer, * Andrew D. Catling, * Scott T. Eblen, Lara S. Collier, dagger Anke Krauss, ddagger Michael J. Weber §

Signal transduction is controlled both by regulation of enzyme activation and by organization of enzymatic complexes with nonenzymatic adapters, scaffolds, and anchor proteins. The extracellular signal-regulated kinase (ERK) cascade is one of several evolutionarily conserved mitogen-activated protein (MAP) kinase cascades important in the regulation of growth, apoptosis, and differentiation. A two-hybrid screen was conducted to identify nonenzymatic components of this signaling cascade that might be important in regulating its activity. A protein called MP1 (MEK Partner 1) was identified that bound specifically to MEK1 and ERK1 and facilitated their activation. When overexpressed in cultured cells, MP1 enhanced activation of ERK1 and activation of a reporter driven by the transcription factor Elk-1. Expression of MP1 in cells increased binding of ERK1 to MEK1. MP1 apparently functions as an adapter to enhance the efficiency of the MAP kinase cascade.

Department of Microbiology and Cancer Center, University of Virginia Health Sciences Center, Charlottesville, VA 22908, USA.
*   These authors contributed equally to this report.

dagger    Present address: Department of Developmental Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.

ddagger    Present address: European Molecular Biology Laboratory, Developmental Biology, 69012 Heidelberg, Germany.

§   To whom correspondence should be addressed. E-mail: MJW{at}Virginia.edu

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Disruption of the 14-3-3 Binding Site within the B-Raf Kinase Domain Uncouples Catalytic Activity from PC12 Cell Differentiation.
M. C. MacNicol, A. J. Muslin, and A. M. MacNicol (2000)
J. Biol. Chem. 275, 3803-3809
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Interaction of a Mitogen-Activated Protein Kinase Signaling Module with the Neuronal Protein JIP3.
N. Kelkar, S. Gupta, M. Dickens, and R. J. Davis (2000)
Mol. Cell. Biol. 20, 1030-1043
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Dimer Formation by Ternary Complex Factor ELK-1.
V. Drewett, S. Muller, J. Goodall, and P. E. Shaw (2000)
J. Biol. Chem. 275, 1757-1762
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Involvement of protein kinase A in fibroblast growth factor-2-activated transcription.
J.-P. Pursiheimo, M. Jalkanen, K. Tasken, and P. Jaakkola (2000)
PNAS 97, 168-173
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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
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Novel Membrane-Targeted ERK1 and ERK2 Chimeras Which Act as Dominant Negative, Isotype-Specific Mitogen-Activated Protein Kinase Inhibitors of Ras-Raf-Mediated Transcriptional Activation of c-fos in NIH 3T3 Cells.
F. Hochholdinger, G. Baier, A. Nogalo, B. Bauer, H. H. Grunicke, and F. Uberall (1999)
Mol. Cell. Biol. 19, 8052-8065
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Mitogen-Activated Signaling in Airway Smooth Muscle . A Central Role for Ras.
M. B. Hershenson and M. K. Abe (1999)
Am. J. Respir. Cell Mol. Biol. 21, 651-654
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The N-terminal ERK-binding Site of MEK1 Is Required for Efficient Feedback Phosphorylation by ERK2 in Vitro and ERK Activation in Vivo.
B.-e Xu, J. L. Wilsbacher, T. Collisson, and M. H. Cobb (1999)
J. Biol. Chem. 274, 34029-34035
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RIP2 Is a Raf1-activated Mitogen-activated Protein Kinase Kinase.
T. A. Navas, D. T. Baldwin, and T. A. Stewart (1999)
J. Biol. Chem. 274, 33684-33690
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JSAP1, a Novel Jun N-Terminal Protein Kinase (JNK)-Binding Protein That Functions as a Scaffold Factor in the JNK Signaling Pathway.
M. Ito, K. Yoshioka, M. Akechi, S. Yamashita, N. Takamatsu, K. Sugiyama, M. Hibi, Y. Nakabeppu, T. Shiba, and K.-I. Yamamoto (1999)
Mol. Cell. Biol. 19, 7539-7548
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Distinct, Constitutively Active MAPK Phosphatases Function in Xenopus Oocytes: Implications for p42 MAPK Regulation In Vivo.
M. L. Sohaskey and J. E. Ferrell Jr. (1999)
Mol. Biol. Cell 10, 3729-3743
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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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The JNKK2-JNK1 Fusion Protein Acts As a Constitutively Active c-Jun Kinase That Stimulates c-Jun Transcription Activity.
C. Zheng, J. Xiang, T. Hunter, and A. Lin (1999)
J. Biol. Chem. 274, 28966-28971
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