The DOI matches its Crossref record; 121 of the 122 references it cites were found in a registry or an index.
Differential regulation and properties of MAPKs
Abstract
Mitogen-activated protein kinases (MAPKs) regulate diverse cellular programs including embryogenesis, proliferation, differentiation and apoptosis based on cues derived from the cell surface and the metabolic state and environment of the cell. In mammals, there are more than a dozen MAPK genes. The best known are the extracellular signal-regulated kinases 1 and 2 (ERK1/2), c-Jun N-terminal kinase (JNK(1-3)) and p38(alpha, beta, gamma and delta) families. ERK3, ERK5 and ERK7 are other MAPKs that have distinct regulation and functions. MAPK cascades consist of a core of three protein kinases. Despite the apparently simple architecture of this pathway, these enzymes are capable of responding to a bewildering number of stimuli to produce exquisitely specific cellular outcomes. These responses depend on the kinetics of their activation and inactivation, the subcellular localization of the kinases, the complexes in which they act, and the availability of substrates. Fine-tuning of cascade activity can occur through modulatory inputs to cascade component from the primary kinases to the scaffolding accessory proteins. Here, we describe some of the properties of the three major MAPK pathways and discuss how these properties govern pathway regulation and activity.
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“The D-motif is also found in phosphatases, substrates, and scaffold proteins (Raman et al., 2007).”
From Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases (2012) · cites this paper as Raman et al., 2007
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3 retracted
A Regulatory Role for p38δ MAPK in Keratinocyte Differentiation
Efimova, T., Broome, A., & Eckert, R. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302759200 · Cited by 135
RetractedYung, Y., Yao, Z., Aebersold, D. M., Hanoch, T., & Seger, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105995200 · Cited by 47
RetractedAoyama, K., Nagata, M., Oshima, K., Matsuda, T., & Aoki, N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100408200 · Cited by 38
RetractedMitogen-Activated Protein Kinase Pathways Mediated by ERK, JNK, and p38 Protein Kinases
Johnson, G. L., & Lapadat, R. (2002) · Science · doi:10.1126/science.1072682 · Cited by 4,295
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A central role for JNK in obesity and insulin resistance
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A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
Lee, J. C., Laydon, J. T., McDonnell, P., Gallagher, T. F., Kumar, S., Green, D., McNulty, D. E., Blumenthal, M. J., Keys, J., vatter, S. W. L., et al. (1994) · Nature · doi:10.1038/372739a0 · Cited by 3,266
Protein Tyrosine Phosphatases in the Human Genome
Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., & Mustelin, T. (2004) · Cell · doi:10.1016/j.cell.2004.05.018 · Cited by 1,886
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Signal Transduction through MAP Kinase Cascades
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Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373
Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases
Cargnello, M., & Roux, P. P. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00031-10 · Cited by 3,274
ERK1/2 MAP kinases: Structure, function, and regulation
Roskoski, R. J. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.04.005 · Cited by 1,719
Oxidative stress: the mitochondria-dependent and mitochondria-independent pathways of apoptosis
Sinha, K., Das, J., Pal, P. B., & Sil, P. C. (2013) · Archives of Toxicology · doi:10.1007/s00204-013-1034-4 · Cited by 1,643
Dhanasekaran, D. N., & Reddy, E. P. (2008) · Oncogene · doi:10.1038/onc.2008.301 · Cited by 1,558
Metadata
- Authors
- Raman, M., Chen, W., & Cobb, M. H.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Corresponding author
- Cobb, M H
- Venue
- Oncogene
- Published
- 2007-05-14
- Volume
- 26
- Issue
- 22
- Pages
- 3100-3112
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W1998809668
- Cited by
- 1,430
- References
- 122
- Citations by year
- 2026: 21 · 2025: 38 · 2024: 37 · 2023: 74 · 2022: 69 · 2021: 53 · 2020: 69 · 2019: 68 · 2018: 65 · 2017: 70 · 2016: 83 · 2015: 64 · 2014: 110 · 2013: 105 · 2012: 101
- FWCI
- 41.29
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Oncogene (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM53032, R01GM056498, R01GM053032, GM 56498)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-34128)
- 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 › Melanoma and MAPK Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- mitogen-activated protein kinase, MAPK signaling, ERK1/2, c-Jun N-terminal kinase, p38 MAPK, ERK3, ERK5, subcellular localization, scaffold proteins, signal transduction regulation
- MeSH terms
- Animals, Humans, Mitogen-Activated Protein Kinases, MAP Kinase Signaling System
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