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Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase
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MAP kinases phosphorylate specific groups of substrate proteins.Here we show that the amino acid sequence FXFP is an evolutionarily conserved docking site that mediates ERK MAP kinase binding to substrates in multiple protein families.FXFP and the D box, a different docking site, form a modular recognition system, as they can function independently or in combination.FXFP is specific for ERK, whereas the D box mediates binding to ERK and JNK MAP kinase, suggesting that the partially overlapping substrate specificities of ERK and JNK result from recognition of shared and unique docking sites.These findings enabled us to predict new ERK substrates and design peptide inhibitors of ERK that functioned in vitro and in vivo.
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“Moreover, the existence of FxFP (Phe-any amino acid-Phe-Pro) motifs in certain MAPK (especially ERK) substrates and a separate docking groove for such motifs on ERK suggest that in some cases two docking grooves on ERK may operate in combination: Elk1 for example contains both an FxFP and a D-motif (35-37).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [37]
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Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
Oncogenes and signal transduction
Cantley, L. C., Auger, K. R., Carpenter, C. F., Duckworth, B. C., Graziani, A., Kapeller, R., & Soltoff, S. P. (1991) · Cell · doi:10.1016/0092-8674(91)90639-g · Cited by 2,697
The mitogen-activated protein kinase signal transduction pathway
Davis, R. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82362-6 · Cited by 2,112
Hibi, M., Lin, A., Smeal, T., Minden, A., & Karin, M. (1993) · Genes & Development · doi:10.1101/gad.7.11.2135 · Cited by 1,886
Whitmarsh, A. J., & Davis, R. J. (1996) · Journal of Molecular Medicine · doi:10.1007/s001090050063 · Cited by 1,543
Regulation of transcription by MAP kinase cascades
Treisman, R. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80067-6 · Cited by 1,296
The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain
Marais, R., Wynne, J., & Treisman, R. (1993) · Cell · doi:10.1016/0092-8674(93)90237-k · Cited by 1,275
MAP kinase kinase kinase, MAP kinase kinase and MAP kinase
Marshall, C. J. (1994) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(94)90095-7 · Cited by 1,005
Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729
Ternary complex factors: growth factor regulated transcriptional activators
Treisman, R. (1994) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(94)90097-3 · Cited by 676
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Regulation of Adipogenesis by a Transcriptional Repressor That Modulates MAPK Activation
Kim, S.-W., Muise, A. M., Lyons, P. J., & Ro, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010640200 · Cited by 138
Lin, Y., & Yang, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508720200 · Cited by 137
Lin, Y., Chuang, S., & Yang, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301854200 · Cited by 134
Docking interactions in the mitogen-activated protein kinase cascades
Tanoue, T., & Nishida, E. (2002) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(02)00188-2 · Cited by 134
Opposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation
Mylona, A., Theillet, F., Foster, C., Cheng, T. M. K., Miralles, F., Bates, P. A., Selenko, P., & Treisman, R. (2016) · Science · doi:10.1126/science.aad1872 · Cited by 138
Proteome-Wide Discovery of Evolutionary Conserved Sequences in Disordered Regions
Ba, A. N. N., Yeh, B. J., van Dyk, D., Davidson, A. R., Andrews, B., Weiss, E. L., & Moses, A. M. (2012) · Science Signaling · doi:10.1126/scisignal.2002515 · Cited by 134
Arur, S., Ohmachi, M., Nayak, S., Hayes, M. E., Miranda, A., Hay, A., Golden, A., & Schedl, T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812285106 · Cited by 127
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Kong, L., Ma, X., Zhang, C., Kim, S.-I., Li, B., Xie, Y., Yeo, I., Thapa, H. R., Chen, S., Devarenne, T. P., et al. (2024) · Cell · doi:10.1016/j.cell.2023.12.030 · Cited by 125
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Holland, P. M., & Cooper, J. A. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80205-x · Cited by 125
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MUÑOZ, J. J., TÁRREGA, C., BLANCO-APARICIO, C., & PULIDO, R. (2003) · Biochemical Journal · doi:10.1042/bj20021941 · Cited by 121
Rizzo, F. M., Fernandez-Serra, M., Squarzoni, P., Archimandritis, A., & Arnone, M. I. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.08.012 · Cited by 118
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Kaffarnik, F. A. R., Müller, P., Leibundgut, M., Kahmann, R., & Feldbrügge, M. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg554 · Cited by 115
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Chevet, É., Wong, H. N., Gerber, D., Cochet, C., Fazel, A., Cameron, P. H., Gushue, J. N., Thomas, D. Y., & Bergeron, J. J. M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.13.3655 · Cited by 115
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Ohmachi, M., Rocheleau, C. E., Church, D. L., Lambie, E. J., Schedl, T., & Sundaram, M. V. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00690-5 · Cited by 111
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Xu, B.-E., Wilsbacher, J. L., Collisson, T., & Cobb, M. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.34029 · Cited by 109
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Ouatas, T., Salerno, M., Palmieri, D., & Steeg, P. S. (2003) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1023497924277 · Cited by 108
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Houle, F., Rousseau, S., MORRICE, N. A., Luc, M., Mongrain, S., Turner, C. E., Tanaka, S., Moreau, P. R., & Huot, J. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-04-0235 · Cited by 108
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Otto, I. M., Raabe, T., Rennefahrt, U. E. E., Peer Bork, B., Rapp, U. R., & Kerkhoff, E. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00388-2 · Cited by 101
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Wu, Y., Feinstein, S. I., Manevich, Y., Chowdhury, I., Pak, J. H., Kazi, A. S., Dodia, C., Speicher, D. W., & Fisher, A. B. (2009) · Biochemical Journal · doi:10.1042/bj20082061 · Cited by 95
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Nichols, A. C., Camps, M., Gilliéron, C., Chabert, C., Brunet, A., Wilsbacher, J. L., Cobb, M. H., Pouysségur, J., Shaw, J. P., & Arkinstall, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001515200 · Cited by 95
Schmidt, H., Schulz, S., Klutzny, M., Koch, T., Händel, M., & Höllt, V. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0740414.x · Cited by 95
Oh, C., & Martin, G. B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225086 · Cited by 94
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Whisenant, T. C., Ho, D. T., Benz, R. W., Rogers, J. S., Kaake, R. M., Gordon, E. A., Huang, L., Baldi, P., & Bardwell, L. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000908 · Cited by 96
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Cagnol, S., & Rivard, N. (2012) · Oncogene · doi:10.1038/onc.2012.88 · Cited by 93
Müller, J., Cacace, A. M., Lyons, W. E., McGill, C. B., & Morrison, D. K. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.15.5529-5539.2000 · Cited by 89
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Therrien, M., Morrison, D. K., Wong, A. M., & Rubin, G. M. (2000) · Genetics · doi:10.1093/genetics/156.3.1231 · Cited by 89
Cesari, F., Brecht, S., Vintersten, K., Vuong, L. G., Hofmann, M., Klingel, K., Schnorr, J., Arsenian, S., Schild, H., Herdegen, T., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.294-305.2004 · Cited by 87
Houle, F., Poirier, A., Dumaresq, J., & Huot, J. (2007) · Journal of Cell Science · doi:10.1242/jcs.003251 · Cited by 83
Klomp, J. E., Klomp, J. A., & Der, C. J. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200507 · Cited by 85
Hwang, C. Y., Lee, C., & Kwon, K. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01758-08 · Cited by 82
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Kusari, A. B., Molina, D. M., Sabbagh, W., Lau, C. S., & Bardwell, L. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200310021 · Cited by 81
Whitehurst, A. W., Robinson, F. L., Moore, M. S., & Cobb, M. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310031200 · Cited by 81
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Lavaur, J., Bernard, F., Trifilieff, P., Pascoli, V., Kappès, V., Pagès, C., Vanhoutte, P., & Caboche, J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.2279-07.2007 · Cited by 83
Waas, W. F., Lo, H., & Dalby, K. N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008787200 · Cited by 75
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Kirsch, K., Zeke, A., Tőke, O., Sok, P., Sethi, A., Sebő, A., Kumar, G. S., Egri, P., Póti, Á., Gooley, P. R., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19582-3 · Cited by 73
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Jahrling, J. B., Hernandez, C. M., Denner, L. A., & Dineley, K. T. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.4024-13.2014 · Cited by 72
Chen, Y., Wang, Y., & Chang, W. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700264200 · Cited by 71
Karim, F. D., & Rubin, G. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(01)80006-x · Cited by 71
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Déléris, P., Rousseau, J., Coulombe, P., Rodier, G., Tanguay, P., & Meloche, S. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21560 · Cited by 69
Vomastek, T., Iwanicki, M., Burack, R., Tiwari, D., Kumar, D., Parsons, J. T., Weber, M. J., & Nandicoori, V. K. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00925-08 · Cited by 69
Frijns, E., Sachs, N., Kreft, M., Wilhelmsen, K., & Sonnenberg, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.138818 · Cited by 69
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Zeke, A., Bastys, T., Alexa, A., Garai, Á., Mészáros, B., Kirsch, K., Dosztányi, Z., Kalinina, O. V., & Reményi, A. (2015) · Molecular Systems Biology · doi:10.15252/msb.20156269 · Cited by 70
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Villanueva, A., Lozano, J., Morales, A., Lin, X.-H., Deng, X.-Z., Hengartner, M., & Kolesnick, R. (2001) · EMBO Journal · doi:10.1093/emboj/20.18.5114 · Cited by 75
Zhou, B., & Zhang, Z. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200377200 · Cited by 63
Wolf, G., Reinking, R. R., Zahner, G., Stahl, R. A. K., & Shankland, S. J. (2003) · Diabetologia · doi:10.1007/s00125-003-1163-z · Cited by 62
Wei, F., Yan, J. J., & Tang, D. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711798194388 · Cited by 63
Barr, R. K., Boehm, I., Attwood, P. V., Watt, P. M., & Bogoyevitch, M. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402181200 · Cited by 61
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Yang, S., Bumpass, D. C., Perkins, N. D., & Sharrocks, A. D. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.14.5036-5046.2002 · Cited by 59
Hendus-Altenburger, R., Pedraz‐Cuesta, E., Olesen, C. W., Papaleo, E., Schnell, J. A., Hopper, J. T. S., Robinson, C. V., Pedersen, S. F., & Kragelund, B. B. (2016) · BMC Biology · doi:10.1186/s12915-016-0252-7 · Cited by 59
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Leight, E. R., Glossip, D., & Kornfeld, K. (2005) · Development · doi:10.1242/dev.01664 · Cited by 58
Self-citationLigand-specific sequential regulation of transcription factors for differentiation of MCF-7 cells
Saeki, Y., Endo, T. A., Ide, K., Nagashima, T., Yumoto, N., Toyoda, T., Suzuki, H., Hayashizaki, Y., Sakaki, Y., & Okada, M. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-545 · Cited by 58
Bell, B., Xing, H., Yan, K., Gautam, N., & Muslin, A. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.7982 · Cited by 58
Self-citationYang, T. T. C., Xiong, Q., Graef, I. A., Crabtree, G. R., & Chow, C.-W. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.3.907-920.2005 · Cited by 59
Eblen, S. T., Catling, A. D., Assanah, M. C., & Weber, M. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.1.249-259.2001 · Cited by 58
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Zhou, B., Zhang, J., Liu, S., Reddy, S., Wang, F., & Zhang, Z. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608916200 · Cited by 56
Kim, D. W., & Cochran, B. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.4.1140-1148.2000 · Cited by 56
Zhan, X.-L., & Guan, K. (1999) · Genes & Development · doi:10.1101/gad.13.21.2811 · Cited by 56
Liu, X., Zhang, C., Lu, C., Lin, S., Wu, J., & Wang, Z. (2016) · Nature Communications · doi:10.1038/ncomms10879 · Cited by 58
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Muslin, A. J. (2005) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2005.06.008 · Cited by 55
Self-citationDucret, C., Maira, S.-M., Lutz, Y., & Wasylyk, B. (2000) · Oncogene · doi:10.1038/sj.onc.1203892 · Cited by 55
Waas, W. F., & Dalby, K. N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110523200 · Cited by 48
Regulation of ROMK Channel and K+ Homeostasis by Kidney-specific WNK1 Kinase
Liu, Z., Wang, H.-R., & Huang, C.-L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806551200 · Cited by 54
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Metadata
- Authors
- Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., & Kornfeld, K.
- Affiliations
- Washington University in St. Louis (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1999-01-15
- Volume
- 13
- Issue
- 2
- Pages
- 163-175
- ISSN
- 0890-9369 (ISSN-L)
- OpenAlex
- W4239714346
- Cited by
- 439
- References
- 49
- Citations by year
- 2026: 8 · 2025: 6 · 2024: 4 · 2023: 9 · 2022: 16 · 2021: 12 · 2020: 13 · 2019: 7 · 2018: 13 · 2017: 13 · 2016: 16 · 2015: 15 · 2014: 10 · 2013: 13 · 2012: 15
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- Funders
- Burroughs Wellcome Fund
- Foundation for Barnes-Jewish Hospital
- Edward Mallinckrodt, Jr. Foundation
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- ERK MAP kinase, docking site, D-box, substrate specificity, JNK MAP kinase, phosphorylation, peptide inhibitors
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