Cited by 1,430Protein Kinase Regulation and GTPase SignalingMelanoma and MAPK PathwaysProtein Tyrosine Phosphatases

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Differential regulation and properties of MAPKs

Raman, M, Chen, W, Cobb, M H·2007·Oncogene

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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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Altered Regulation of ERK1b by MEK1 and PTP-SL and Modified Elk1 Phosphorylation by ERK1b Are Caused by Abrogation of the Regulatory C-terminal Sequence of ERKs
Yung, Y., Yao, Z., Aebersold, D. M., Hanoch, T., & Seger, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105995200 · Cited by 47
Retracted
Molecular Cloning and Characterization of a Novel Dual Specificity Phosphatase, LMW-DSP2, That Lacks the Cdc25 Homology Domain
Aoyama, K., Nagata, M., Oshima, K., Matsuda, T., & Aoki, N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100408200 · Cited by 38
Retracted
Mitogen-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
Mammalian Mitogen-Activated Protein Kinase Signal Transduction Pathways Activated by Stress and Inflammation
Kyriakis, J. M., & Avruch, J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.807 · Cited by 3,400
A central role for JNK in obesity and insulin resistance
Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359
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
Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.
Hibi, M., Lin, A., Smeal, T., Minden, A., & Karin, M. (1993) · Genes & Development · doi:10.1101/gad.7.11.2135 · Cited by 1,886
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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Authors: Raman, M., Chen, W., & Cobb, M. H.
Affiliations: The University of Texas Southwestern Medical Center (US)
Corresponding author: Cobb, M H
ORCID: Raman, M
Cobb, M H
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 2007-05-14
Volume: 26
Issue: 22
Pages: 3100-3112
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/sj.onc.1210392
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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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Differential regulation and properties of MAPKs

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