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MP1: A MEK Binding Partner That Enhances Enzymatic Activation of the MAP Kinase Cascade
Abstract
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.
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Cites
Rotation of photoreceptor clusters in the developing drosophila eye requires the nemo gene
Choi, K.-W., & Benzer, S. (1994) · Cell · doi:10.1016/0092-8674(94)90579-7 · Cited by 339
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Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237
Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464
“Previous work indicates that these three small proteins interact with each other, localize to endosomes and lysosomes, and play positive roles in the MAPK pathway (Lunin et al., 2004; Nada et al., 2009; Schaeffer et al., 1998; Teis et al., 2006; Teis et al., 2002; Wunderlich et al., 2001).”
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Schaeffer, H. J., & Weber, M. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2435 · Cited by 1,600
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Phosphatase‐mediated crosstalk between MAPK signaling pathways in the regulation of cell survival
Junttila, M. R., Li, S., & Westermarck, J. (2008) · The FASEB Journal · doi:10.1096/fj.06-7859rev · Cited by 826
Redox signaling and the MAP kinase pathways
Torres, M., & Forman, H. J. (2003) · BioFactors · doi:10.1002/biof.5520170128 · Cited by 580
The ERK Cascade: Distinct Functions within Various Subcellular Organelles
Wortzel, I., & Seger, R. (2011) · Genes & Cancer · doi:10.1177/1947601911407328 · Cited by 563
Nada, S., Hondo, A., Kasai, A., Koike, M., Saito, K., Uchiyama, Y., & Okada, M. (2009) · The EMBO Journal · doi:10.1038/emboj.2008.308 · Cited by 341
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Yao, Y., Li, W., Wu, J., Germann, U. A., Su, M. S. S., Kuida, K., & Boucher, D. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2134254100 · Cited by 323
Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3
Kelkar, N., Gupta, S., Dickens, M., & Davis, R. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.1030-1043.2000 · Cited by 281
Ito, M., Yoshioka, K., Akechi, M., Yamashita, S., Takamatsu, N., Sugiyama, K., Hibi, M., Nakabeppu, Y., Shiba, T., & Yamamoto, K.-I. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7539 · Cited by 279
KSR is a scaffold required for activation of the ERK/MAPK module
Roy, F., Laberge, G., Douziech, M., Ferland-McCollough, D., & Therrien, M. (2002) · Genes & Development · doi:10.1101/gad.962902 · Cited by 217
Kolli, S., Zito, C. I., Mossink, M. H., Wiemer, E. A. C., & Bennett, A. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313955200 · Cited by 154
Signaling dynamics of the KSR1 scaffold complex
McKay, M. M., Ritt, D. A., & Morrison, D. K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901590106 · Cited by 163
Kelkar, N., Standen, C. L., & Davis, R. J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.7.2733-2743.2005 · Cited by 157
ERK2 Contributes to the Control of Social Behaviors in Mice
Satoh, Y., Endo, S., Nakata, T., Kobayashi, Y., Yamada, K., Ikeda, T., Takeuchi, A., Hiramoto, T., Watanabe, Y., & Kazama, T. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2349-11.2011 · Cited by 145
ERK2 is required for efficient terminal differentiation of skeletal myoblasts
Li, J., & Johnson, S. E. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.051 · Cited by 137
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Fehrenbacher, N., Bar-Sagi, D., & Philips, M. (2009) · Molecular Oncology · doi:10.1016/j.molonc.2009.06.004 · Cited by 131
Caffrey, D. R., O'Neill, L. A. J., & Shields, D. C. (1999) · Journal of Molecular Evolution · doi:10.1007/pl00006578 · Cited by 124
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Filipek, P. A., de Araujo, M. E. G., Vogel, G. F., De Smet, C. H., Eberharter, D., Rebsamen, M., Rudashevskaya, E. L., Kremser, L., Yordanov, T., Tschaikner, P., et al. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201703061 · Cited by 119
Mitogen-Activated Protein Kinases Promote WNT/β-Catenin Signaling via Phosphorylation of LRP6
Červenka, I., Wolf, J., Mašek, J., Krejci, P., Wilcox, W. R., Kozubík, A., Schulte, G., Gutkind, J. S., & Bryja, V. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.00550-10 · Cited by 117
Zheng, C., Xiang, J., Hunter, T., & Lin, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.28966 · Cited by 110
Kurzbauer, R., Teis, D., de Araujo, M. E. G., Maurer-Stroh, S., Eisenhaber, F., Bourenkov, G. P., Bartunik, H. D., Hekman, M., Rapp, U. R., Huber, L. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403435101 · Cited by 95
Kogan, K., Spear, E. D., Kaiser, C. A., & Fass, D. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.07.034 · Cited by 56
R-Ras3, a brain-specific Ras-related protein, activates Akt and promotes cell survival in PC12 cells
Kimmelman, A. C., Osada, M., & Chan, A. M.-L. (2000) · Oncogene · doi:10.1038/sj.onc.1203530 · Cited by 50
Genetic Targeting of ERK1 Suggests a Predominant Role for ERK2 in Murine Pain Models
Alter, B. J., Zhao, C., Karim, F., Landreth, G. E., & Gereau, R. W. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.6103-09.2010 · Cited by 47
Exploiting Conformational Ensembles in Modeling Protein–Protein Interactions on the Proteome Scale
Kuzu, G., Gursoy, A., Nussinov, R., & Keskin, O. (2013) · Journal of Proteome Research · doi:10.1021/pr400006k · Cited by 47
Metadata
- Authors
- Schaeffer, H. J., Catling, A. D., Eblen, S. T., Collier, L. S., Krauss, A., & Weber, M. J.
- Venue
- Science
- Published
- 1998-09-11
- Volume
- 281
- Issue
- 5383
- Pages
- 1668-1671
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2072243374
- Cited by
- 471
- References
- 1
- FWCI
- 14.18
- Type
- journal article
- Language
- en
- Open access
- closed
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