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A conserved docking motif in MAP kinases common to substrates, activators and regulators
Abstract
Mitogen-activated protein kinases (MAPKs) are specifically phosphorylated and activated by the MAPK kinases, phosphorylate various targets such as MAPK-activated protein kinases and transcription factors, and are inactivated by specific phosphatases. Recently, docking interactions via the non-catalytic regions of MAPKs have been suggested to be important in regulating these reactions. Here we identify docking sites in MAPKs and in MAPK-interacting enzymes. A docking domain in extracellular-signal-regulated kinase (ERK), a MAPK, serves as a common site for binding to the MAPK kinase MEK1, the MAPK-activated protein kinase MNK1 and the MAPK phosphatase MKP3. Two aspartic acids in this domain are essential for docking, one of which is mutated in the sevenmaker mutant of Drosophila ERK/Rolled. A corresponding domain in the MAPKs p38 and JNK/SAPK also serves as a common docking site for their MEKs, MAPK-activated protein kinases and MKPs. These docking interactions increase the efficiency of the enzymatic reactions. These findings reveal a hitherto unidentified docking motif in MAPKs that is used in common for recognition of their activators, substrates and regulators.
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“The majority of MAPK regulatory proteins investigated thus far contain KIMs.”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [21]
Citations
Cites
Marshall, C. J. (1995) · Cell · doi:10.1016/0092-8674(95)90401-8 · Cited by 3,906
Cobb, M. H., & Goldsmith, E. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.25.14843 · Cited by 1,718
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 MAP kinase cascade is essential for diverse signal transduction pathways
Nishida, E., & Gotoh, Y. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90019-j · Cited by 1,087
Self-citationBmi-1 collaborates with c-Myc in tumorigenesis by inhibiting c-Myc-induced apoptosis via INK4a/ARFPreprint
Jacobs, J. J. L., Scheijen, B., Voncken, J. W., Kieboom, K., Berns, A. J. M., & van Lohuizen, M. (1999) · Genes & Development · doi:10.1101/gad.13.20.2678 · Cited by 1,069
Proteolytic Inactivation of MAP-Kinase-Kinase by Anthrax Lethal Factor
Duesbery, N. S., Webb, C. P., Leppla, S. H., Gordon, V. M., Klimpel, K. R., Copeland, T. D., Ahn, N. G., Oskarsson, M. K., Fukasawa, K., Paull, K. D., et al. (1998) · Science · doi:10.1126/science.280.5364.734 · Cited by 1,007
Mitogen‐activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
Waskiewicz, A. J., Flynn, A., Proud, C. G., & Cooper, J. A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.8.1909 · Cited by 951
MAPKs: new JNK expands the group
Davis, R. J. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90132-5 · Cited by 944
Protein kinase cascades activated by stress and inflammatory cytokines
Kyriakis, J. M., & Avruch, J. (1996) · BioEssays · doi:10.1002/bies.950180708 · Cited by 709
Phosphorylation of the MAP Kinase ERK2 Promotes Its Homodimerization and Nuclear Translocation
Khokhlatchev, A. V., Canagarajah, B. J., Wilsbacher, J. L., Robinson, M. J., Atkinson, M. A., Goldsmith, E. J., & Cobb, M. H. (1998) · Cell · doi:10.1016/s0092-8674(00)81189-7 · Cited by 675
Fukunaga, R., & Hunter, T. (1997) · The EMBO Journal · doi:10.1093/emboj/16.8.1921 · Cited by 666
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J. (1994) · Nature · doi:10.1038/367704a0 · Cited by 592
Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase.
Camps, M., Nichols, A., Gilliéron, C., Antonsson, B., Muda, M., Chabert, C., Boschert, U., & Arkinstall, S. (1998) · Science · doi:10.1126/science.280.5367.1262 · Cited by 523
Characterization of the Structure and Function of a Novel MAP Kinase Kinase (MKK6)
Han, J., Lee, J., Jiang, Y., Li, Z., Feng, L., & Ulevitch, R. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.6.2886 · Cited by 512
c-Jun Can Recruit JNK to Phosphorylate Dimerization Partners via Specific Docking Interactions
Kallunki, T., Deng, T., Hibi, M., & Karin, M. (1996) · Cell · doi:10.1016/s0092-8674(00)81999-6 · Cited by 492
Chu, Y., Solski, P. A., Khosravi‐Far, R., Der, C. J., & Kelly, K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.11.6497 · Cited by 442
Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., & Kornfeld, K. (1999) · Genes & Development · doi:10.1101/gad.13.2.163 · Cited by 439
Sturgill, T. W., & Wu, J. (1991) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(97)90012-4 · Cited by 430
Brunner, D., Oellers, N., Szabad, J., Biggs, W., Zipursky, S. L., & Hafen, E. (1994) · Cell · doi:10.1016/0092-8674(94)90362-x · Cited by 409
Fukuda, M., Gotoh, Y., & Nishida, E. (1997) · The EMBO Journal · doi:10.1093/emboj/16.8.1901 · Cited by 385
Self-citationPulido, R., Zúñiga, Á., & Ullrich, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7337 · Cited by 320
Differential targeting of MAP kinases to the ETS‐domain transcription factor Elk‐1
Yang, S., Whitmarsh, A. J., Davis, R. J., & Sharrocks, A. D. (1998) · The EMBO Journal · doi:10.1093/emboj/17.6.1740 · Cited by 299
The mitogen-activated protein kinase activator
Ahn, N. G., Seger, R., & Krebs, E. G. (1992) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(92)90131-u · Cited by 284
Smith, J. A., Poteet-Smith, C. E., Malarkey, K., & Sturgill, T. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.5.2893 · Cited by 283
The structure of mitogen-activated protein kinase p38 at 2.1-Å resolution
Wang, Z., Harkins, P. C., Ulevitch, R. J., Han, J., Cobb, M. H., & Goldsmith, E. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2327 · Cited by 275
Crystal Structure of p38 Mitogen-activated Protein Kinase
Wilson, K. P., Fitzgibbon, M. J., Caron, P. R., Griffith, J. P., Chen, W., McCaffrey, P. G., Chambers, S. P., & Su, M. S. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27696 · Cited by 262
Targeting of p38 Mitogen-Activated Protein Kinases to MEF2 Transcription Factors
Yang, S.-H., Galanis, A., & Sharrocks, A. D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4028 · Cited by 244
Molecular Cloning and Characterization of a Novel Dual Specificity Phosphatase, MKP-5
Tanoue, T., Moriguchi, T., & Nishida, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19949 · Cited by 224
Self-citationPritchard, C. A., Samuels, M. L., Bosch, E., & McMahon, M. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.11.6430 · Cited by 224
Xia, Y., Wu, Z., Su, B., Murray, B. W., & Karin, M. (1998) · Genes & Development · doi:10.1101/gad.12.21.3369 · Cited by 203
Crystal structure of JNK3: a kinase implicated in neuronal apoptosis
Xie, X., Gu, Y., Fox, T., Coll, J. T., Fleming, M. A., Markland, W., Caron, P. R., Wilson, K. P., & Su, M. S.-S. (1998) · Structure · doi:10.1016/s0969-2126(98)00100-2 · Cited by 198
The MKK7 Gene Encodes a Group of c-Jun NH 2 -Terminal Kinase Kinases
Tournier, C., Whitmarsh, A. J., Cavanagh, J., Barrett, T., & Davis, R. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1569 · Cited by 173
Purification and Identification of a Major Activator for p38 from Osmotically Shocked Cells
Moriguchi, T., Toyoshima, F., Gotoh, Y., Iwamatsu, A., Irie, K., Mori, E., Kuroyanagi, N., Hagiwara, M., Matsumoto, K., & Nishida, E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.26981 · Cited by 165
Self-citationA MAP kinase docking site is required for phosphorylation and activation of p90rsk/MAPKAP kinase-1
Gavin, A.-C., & Nebreda, A. R. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80120-1 · Cited by 158
Rouault, J.-P., Kuwabara, P. E., Sinilnikova, O. M., Duret, L., Thierry‐Mieg, D., & Billaud, M. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80143-2 · Cited by 144
Bardwell, L., & Thorner, J. W. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)30032-7 · Cited by 141
Zúñiga, Á., Torres, J., Úbeda, J., & Pulido, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21900 · Cited by 131
Protein modification: Docking sites for kinases
Holland, P. M., & Cooper, J. A. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80205-x · Cited by 125
Identification of MAP Kinase Domains by Redirecting Stress Signals into Growth Factor Responses
Brunet, A., & Pouysségur, J. (1996) · Science · doi:10.1126/science.272.5268.1652 · Cited by 125
Bott, C. M., Thorneycroft, S. G., & Marshall, C. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00958-9 · Cited by 104
Karim, F. D., & Rubin, G. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(01)80006-x · Cited by 71
Phosphorylation of MAP Kinases by MAP/ERK Involves Multiple Regions of MAP Kinases
Wilsbacher, J. L., Goldsmith, E. J., & Cobb, M. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.24.16988 · Cited by 65
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Metadata
- Authors
- Tanoue, T., Adachi, M., Moriguchi, T., & Nishida, E.
- Affiliations
- Kyoto University (JP)
- Corresponding author
- Nishida, Eisuke
- Venue
- Nature Cell Biology
- Published
- 2000-01-17
- Volume
- 2
- Issue
- 2
- Pages
- 110-116
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2083117403
- Cited by
- 816
- References
- 42
- Citations by year
- 2026: 13 · 2025: 16 · 2024: 15 · 2023: 25 · 2022: 26 · 2021: 17 · 2020: 16 · 2019: 24 · 2018: 20 · 2017: 25 · 2016: 23 · 2015: 27 · 2014: 19 · 2013: 28 · 2012: 32
- FWCI
- 19.91
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
- Keywords
- mitogen-activated protein kinase, extracellular signal-regulated kinase, MEK1, MKP-3, MAPK phosphatase, p38 MAPK, SAPK/JNK, MAPK kinase, aspartic acid residues, protein-protein interaction, kinase activation, substrate recognition
- MeSH terms
- Amino Acid Sequence, Binding Sites, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Tyrosine Phosphatases, Conserved Sequence, Protein Serine-Threonine Kinases, Calcium-Calmodulin-Dependent Protein Kinases, Mitogen-Activated Protein Kinase 1, Amino Acid Motifs, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase Kinases, p38 Mitogen-Activated Protein Kinases, MAP Kinase Kinase 1, Dual Specificity Phosphatase 6
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