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Atypical mitogen-activated protein kinases: Structure, regulation and functions
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Mitogen-activated protein (MAP) kinases are a family of serine/threonine kinases that play a central role in transducing extracellular cues into a variety of intracellular responses ranging from lineage specification to cell division and adaptation. Fourteen MAP kinase genes have been identified in the human genome, which define 7 distinct MAP kinase signaling pathways. MAP kinases can be classified into conventional or atypical enzymes, based on their ability to get phosphorylated and activated by members of the MAP kinase kinase (MAPKK)/MEK family. Conventional MAP kinases comprise ERK1/ERK2, p38s, JNKs, and ERK5, which are all substrates of MAPKKs. Atypical MAP kinases include ERK3/ERK4, NLK and ERK7. Much less is known about the regulation, substrate specificity and physiological functions of atypical MAP kinases.
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“Nemo-like kinase (NLK) is an evolutionary, conserved, atypical proline-directed serine/threonine mitogen-activated protein (MAP) kinase [13]”
From Nemo-Like Kinase in Development and Diseases: Insights from Mouse Studies (2020) · cites this paper as [13]
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1 retracted
ERK1b, a 46-kDa ERK Isoform That Is Differentially Regulated by MEK
Yung, Y., Yao, Z., Hanoch, T., & Seger, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910060199 · Cited by 79
RetractedSWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modeling
Guex, N., & Peitsch, M. C. (1997) · Electrophoresis · doi:10.1002/elps.1150181505 · Cited by 11,312
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
The protein kinase complement of the human genome
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145
Mammalian MAP kinase signalling cascades
Chang, L., & Karin, M. (2001) · Nature · doi:10.1038/35065000 · Cited by 5,118
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*
Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111
Mechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184
Mitogen-Activated Protein Kinase: Conservation of a Three-Kinase Module From Yeast to Human
Widmann, C., Gibson, S. B., Jarpe, M. B., & Johnson, G. L. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.1.143 · Cited by 2,707
Boulton, T. G., Nye, S. H., Robbins, D. J., Ip, N. Y., Radzlejewska, E., Morgenbesser, S. D., DePinho, R. A., Panayotatos, N., Cobb, M. H., & Yancopoulos, G. D. (1991) · Cell · doi:10.1016/0092-8674(91)90098-j · Cited by 1,876
Signal Transduction through MAP Kinase Cascades
Lewis, T. S., Shapiro, P. S., & Ahn, N. G. (1998) · Advances in cancer research · doi:10.1016/s0065-230x(08)60765-4 · Cited by 1,759
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Cargnello, M., & Roux, P. P. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00031-10 · Cited by 3,274
Physiology of cell volume regulation in vertebrates
Hoffmann, E. K., Lambert, I. H., & Pedersen, S. F. (2009) · Physiological Reviews · doi:10.1152/physrev.00037.2007 · Cited by 1,441
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Plotnikov, A. N., Zehorai, E., Procaccia, S., & Seger, R. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.12.012 · Cited by 1,021
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Rose, B. A., Force, T. L., & Wang, Y. (2010) · Physiological Reviews · doi:10.1152/physrev.00054.2009 · Cited by 730
Keshet, Y., & Seger, R. (2010) · Methods in Molecular Biology · doi:10.1007/978-1-60761-795-2_1 · Cited by 642
Boutros, T., Chevet, É., & Metrakos, P. P. (2008) · Pharmacological Reviews · doi:10.1124/pr.107.00106 · Cited by 558
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Caunt, C. J., & Keyse, S. M. (2013) · The FEBS Journal · doi:10.1111/j.1742-4658.2012.08716.x · Cited by 535
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Vinayagam, A., Stelzl, U., Foulle, R., Plaßmann, S., Zenkner, M., Timm, J., Assmus, H. E., Andrade-Navarro, M. A., & Wanker, E. E. (2011) · Science Signaling · doi:10.1126/scisignal.2001699 · Cited by 356
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Wang, Y. (2007) · Circulation · doi:10.1161/circulationaha.106.679589 · Cited by 320
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Dhanasekaran, D. N., Kashef, K., Lee, C. M., Xu, H., & Reddy, E. P. (2007) · Oncogene · doi:10.1038/sj.onc.1210411 · Cited by 288
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Greenblatt, M. B., Shim, J., & Glimcher, L. H. (2013) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101512-122347 · Cited by 256
Qin, K. H., Yu, M. S., Fan, J., Wang, H., Zhao, P., Zhao, G., Zeng, W., Chen, C., Wang, Y., Wang, A., et al. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.01.030 · Cited by 243
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Manna, P. R., & Stocco, D. M. (2011) · Journal of Signal Transduction · doi:10.1155/2011/821615 · Cited by 127
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Zacharogianni, M., Kondylis, V., Tang, Y., Farhan, H., Xanthakis, D., Fuchs, F., Boutros, M., & Rabouille, C. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.253 · Cited by 104
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Nikolic-Paterson, D. J. (2009) · Frontiers in Bioscience-Scholar · doi:10.2741/s17 · Cited by 94
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Groehler, A. L., & Lannigan, D. A. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201002124 · Cited by 60
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Luo, M., Sun, Q., Zhao, H., Tao, J., & Yan, D. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28791 · Cited by 40
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Elkhadragy, L., Alsaran, H., Morel, M., & Long, W. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003699 · Cited by 36
Wang, S., & Qi, X. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.916653 · Cited by 39
Yogendra, K. N., & Kushalappa, A. C. (2016) · Functional Plant Biology · doi:10.1071/fp16028 · Cited by 34
Jin, D., Lee, J., Kim, K. M., Kim, S., Kim, D.-H., & Park, J. (2015) · Oncotarget · doi:10.18632/oncotarget.4171 · Cited by 34
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Tanguay, P., Rodier, G., & Meloche, S. (2010) · Biochemical Journal · doi:10.1042/bj20091604 · Cited by 34
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Lee, W., Ko, K. R., Kim, H.-K., Lee, D. S., Nam, I.-J., Lim, S., & Kim, S. (2018) · Journal of Natural Products · doi:10.1021/acs.jnatprod.7b00927 · Cited by 33
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Metadata
- Authors
- Coulombe, P., & Meloche, S.
- Affiliations
- Institute for Research in Immunology and Cancer (CA)
- Corresponding author
- Meloche, Sylvain
- ORCID
- Meloche, Sylvain
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2007-08
- Volume
- 1773
- Issue
- 8
- Pages
- 1376-1387
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W1973460380
- Cited by
- 298
- References
- 87
- Citations by year
- 2026: 6 · 2025: 13 · 2024: 17 · 2023: 19 · 2022: 19 · 2021: 28 · 2020: 21 · 2019: 14 · 2018: 18 · 2017: 14 · 2016: 13 · 2015: 12 · 2014: 16 · 2013: 10 · 2012: 13
- FWCI
- 0.69
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Canada Research Chairs
- National Cancer Institute
- 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
- mitogen-activated protein kinase, Nemo-like kinase, MAPK signaling, MAP kinase kinase, kinase regulation, substrate specificity, serine/threonine kinase, signal transduction
- MeSH terms
- Amino Acid Sequence, Animals, Enzyme Activation, Humans, Models, Molecular, Molecular Sequence Data, Substrate Specificity, Sequence Homology, Amino Acid, MAP Kinase Signaling System, Extracellular Signal-Regulated MAP Kinases
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