Cited by 1,600Protein Kinase Regulation and GTPase SignalingMelanoma and MAPK PathwaysProtein Tyrosine Phosphatases

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Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers

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Schaeffer, Hans J., Weber, Michael J.·1999·Molecular and Cellular Biology

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Abstract

Signal transduction networks allow cells to perceive changes in the extracellular environment and to mount an appropriate response. Mitogen-activated protein kinase (MAPK) cascades are among the most thoroughly studied of signal transduction systems and have been shown to participate in a diverse array of cellular programs, including cell differentiation, cell movement, cell division, and cell death. A key question in studies of this cascade is, how does a ubiquitously activated regulatory enzume generate a specific and biologically appropriate cellular response? In this review we describe recent findings that provide insight into ways that the regulation, structure, and localization of MAPKs and the participation of adapters and scaffolds can help determine biological outcomes. MAPK cascades are evolutionarily conserved in all eucaryotes and play a key role in the regulation of gene expression as well as cytoplasmic activities. They typically are organized in a three-kinase architecture consisting of a MAPK, a MAPK activator (MEK, MKK, or MAPK kinase), and a MEK activator (MEK kinase [MEKK] or MAPK kinase kinase). Transmission of signals is achieved by sequential phosphorylation and activation of the components specific to a respective cascade. In the yeast Saccharomyces cerevisiae, five MAPK modules have been described; they regulate mating, filamentation, high-osmolarity responses, cell wall remodeling, and sporulation (Fig. (Fig.1A)1A) (reviewed in references 56 and 77). In mammalian systems five distinguishable MAPK modules have been identified so far (Fig. (Fig.1B).1B). These include the extracellular signal-regulated kinase 1 and 2 (ERK1/2) cascade, which preferentially regulates cell growth and differentiation, as well as the c-Jun N-terminal kinase (JNK) and p38 MAPK cascades, which function mainly in stress responses like inflammation and apoptosis (reviewed in references 57, 74, and 103). Moreover, MAPK pathways control several developmental programs, such as morphogenesis and spatial patterning in Dictyostelium amoebae (17, 45), eye development in Drosophila melanogaster (124), vulva induction in Caenorhabditis elegans (113), and T-cell development in mammals (31). FIG. 1 Schematic overview of MAPK modules. (A) In S. cerevisiae, five MAPK modules regulate mating, filamentation, high-osmolarity responses, cell wall remodeling, and sporulation. (B) Mammalian MAPK modules regulate cell growth, differentiation, stress responses, ... Individual MAPK modules generally can signal independently from each other, and this specificity is manifested in distinct physiologic responses. This is most obvious when studying MAPK signaling in S. cerevisiae. Here a particular extracellular event characteristically activates a specific MAPK module and initiates a unique cellular program (reviewed in references 56 and 77). For example, stimulation of cells with pheromone leads to the activation of the pheromone response pathway (STE11, STE7, and FUS3) (Fig. (Fig.2),2), which ultimately results in cell cycle arrest and the induction of mating-specific genes. However, related MAPKs whose modules share some components with the pheromone response pathway are not affected by pheromone stimulation but are activated only in response to the appropriate stimulus. For example, under conditions of high osmolarity Ste11 can lead to activation of Hog1 but does not induce mating-specific genes. Conversely, conditions that activate the filamentation pathway (which utilizes STE11 and STE7) induce only genes that regulate filamentous growth without triggering pheromone responses or responses to high osmolarity. These observations suggest that yeast cells have developed efficient mechanisms to generate pathway specificity and to successfully suppress cross talk, even when individual components participate in more than one signaling pathway. FIG. 2 Scaffold and adapter molecules in MAPK pathways. MAPK scaffolds and adapters (gray shading) are thought to promote the formation of oligomeric protein complexes with components that function in a specific MAPK module. Scaffolds have been identified in ... In metazoan cells the problem is more complex because each cell is simultaneously exposed to multiple extracellular signals and must integrate these inputs to choose an appropriate response. Thus, the biological context of a signal plays a determinative role in the way that MAPK activation is interpreted. For example, although ERKs generally regulate cell growth and cell differentiation and JNKs participate in a stress response, this is not always the case and in certain cell types activation of JNKs can induce proliferation (110). This indicates that in mammalian systems physiologic responses associated with a certain MAPK module can be cell type specific. Moreover, in PC12 cells, transient stimulation of the ERK cascade leads to proliferation whereas sustained stimulation leads to differentiation,

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Background
Mechanisms of type I interferon signaling in normal and malignant cells.
Li, Y., Srivastava, K. K., & Platanias, L. C. (2004) · PubMed · Cited by 23
Upregulation of N-acetylaspartic acid alters inflammation, transcription and contractile associated protein levels in the stomach and smooth muscle contractility
Surendran, S. (2007) · Molecular Biology Reports · doi:10.1007/s11033-007-9167-2 · Cited by 23
MAP kinase in renal development
Awazu, M. (2002) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/17.suppl_9.5 · Cited by 23
Identification of a Membrane Ig-Induced p38 Mitogen-Activated Protein Kinase Module That Regulates cAMP Response Element Binding Protein Phosphorylation and Transcriptional Activation in CH31 B Cell Lymphomas
Swart, J. M., Bergeron, D. M., & Chiles, T. C. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.5.2311 · Cited by 23
Extracellular signal-regulated kinases 1 and 2 phosphorylated neurons in the tele- and diencephalon of rat after visceral pain stimulation: an immunocytochemical study
Gioia, M., Galbiati, S., Rigamonti, L. M., Moscheni, C., & Gagliano, N. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)02008-0 · Cited by 23
Functional components of basic fibroblast growth factor signaling that inhibit lung elastin gene expression
Carreras, I., Rich, C. B., Jaworski, J. A., DiCamillo, S. J., Panchenko, M. P., Goldstein, R. H., & Foster, J. A. (2001) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2001.281.4.l766 · Cited by 23
Molecular cloning, isolation and characterisation of ERK3 gene from chewing-tobacco induced oral squamous cell carcinoma
Rai, R., Mahale, A. M., & Saranath, D. (2004) · Oral Oncology · doi:10.1016/j.oraloncology.2004.01.010 · Cited by 22
Unfolded Protein Response and Scaffold Independent Pheromone MAP Kinase Signaling Control Verticillium dahliae Growth, Development, and Plant Pathogenesis
Starke, J., Harting, R., Maurus, I., Leonard, M., Bremenkamp, R., Heimel, K., Kronstad, J. W., & Braus, G. H. (2021) · Journal of Fungi · doi:10.3390/jof7040305 · Cited by 21
Fus3, as a Critical Kinase in MAPK Cascade, Regulates Aflatoxin Biosynthesis by Controlling the Substrate Supply in Aspergillus flavus, Rather than the Cluster Genes Modulation
Ma, L., Xu, L. M., Xing, F., Ma, J., Ma, X., & Jiang, Y. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.01269-21 · Cited by 22
“The MAPK pathway, consisting of a cascade of three protein kinases, represents a highly conserved eukaryotic signal transduction system from yeast to humans (27, 28).”
Background
Extract isolated from Angelica hirsutiflora with insulin secretagogue activity
Leu, Y. L., Chen, Y. W., Yang, C., Huang, C. F., Lin, G. H., Tsai, K., Yang, R., & Liu, S. (2009) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2009.03.027 · Cited by 22
A dominant function of p38 mitogen‐activated protein kinase signaling in receptor activator of nuclear factor‐κB ligand expression and osteoclastogenesis induction by Aggregatibacter actinomycetemcomitans and Escherichia coli lipopolysaccharide
Rossa, C., Liu, M., & Kirkwood, K. L. (2007) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.2007.01013.x · Cited by 22
Relative Role of Akt, ERK and CREB in Alcohol-Induced Microglia P2X4R Receptor Expression
Gofman, L., Fernandes, N. C., & Potula, R. (2016) · Alcohol and Alcoholism · doi:10.1093/alcalc/agw009 · Cited by 22
“However, since MEK isoforms are differentially regulated (Schaeffer and Weber, 1999) and may mediate different biological responses we examined the role of MEK1 and MEK2 isoforms on ERK phosphorylation in ESdM cells.”
Background
Allosteric modulators of MEK1: drug design and discovery
Shang, J., Lu, S., Jiang, Y., & Zhang, J. (2016) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12780 · Cited by 23
De novo transcriptome analysis reveals insights into different mechanisms of growth and immunity in a Chinese soft-shelled turtle hybrid and the parental varieties
Zhang, H., Xu, X., He, Z., Zheng, T., & Shao, J.-Z. (2016) · Gene · doi:10.1016/j.gene.2016.12.003 · Cited by 22
The death effector domain protein PEA‐15 negatively regulates T‐cell receptor signaling
Pastorino, S., Renganathan, H., Caliva, M. J., Filbert, E. L., Opoku‐Ansah, J., Sulzmaier, F. J., Gawecka, J. E., Werlen, G., Shaw, A. S., & Ramos, J. W. (2010) · The FASEB Journal · doi:10.1096/fj.09-144295 · Cited by 22
The Activation of ERK1/2 via a Tyrosine Kinase Pathway Attenuates Trail-Induced Apoptosis in HeLa Cells
Lee, M. W., Bach, J. H., Lee, H. J., Lee, D., Joo, W. S., Kim, Y. S., Park, S. C., Kim, K. Y., Lee, W. B., & Kim, S. S. (2005) · Cancer Investigation · doi:10.1080/07357900500283036 · Cited by 22
“Mitogen-activated protein (MAP) kinases transduce extracellular signals from tyrosine kinase receptors and G proteincoupled receptors to cytoplasmic and nuclear effectors in mammalian cells.([8,9]) These are intracellular mediators that are divided into 3 classes, namely the extracellular signalregulated kinase 1/2 (E…”
Background
Stress-induced platelet-activating factor synthesis in human neutrophils
Owen, J. S., Baker, P. R. S., O’Flaherty, J. T., Thomas, M. J., Samuel, M. P., Wooten, R. E., & Wykle, R. L. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2004.12.016 · Cited by 22
Phorbol ester-induced activation of mitogen-activated protein kinase/extracellular-signal-regulated kinase kinase and extracellular-signal-regulated protein kinase decreases glucose-6-phosphatase gene expression
Schmoll, D., Grempler, R., Barthel, A., Joost, H., & Walther, R. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3570867 · Cited by 22
MEK1 and MEK2 isoforms regulate distinct functions in pancreatic cancer cells
Tan, X. (2010) · Oncology Reports · doi:10.3892/or_00000853 · Cited by 22
“The MAPK pathways are evolutionarily conserved in all eukaryotes and can be organized into a three-kinase hierarchy: a MAPK, a MAPK activator (MAP kinase kinase, MKK or MEK), and a MAP kinase kinase activator (MAP kinase kinase kinase, MAPKKK) (10).”
Differential Involvement of Cytoskeleton and Rho-Guanosine 5′-Triphosphatases in Growth-Promoting Effects of Angiotensin II in Rat Adrenal Glomerulosa Cells
Otis, M., & Gallo‐Payet, N. (2006) · Endocrinology · doi:10.1210/en.2006-0759 · Cited by 21
The Ras GDP/GTP cycle is regulated by oxidizing agents at the level of Ras regulators and effectors
Accorsi, K., Giglione, C., Vanoni, M., & Parmeggiani, A. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02251-7 · Cited by 22
Visualizing cellular heterogeneity by quantifying the dynamics of MAPK activity in live mammalian cells with synthetic fluorescent biosensors
Ma, M., Bordignon, P., Dotto, G. P., & Pelet, S. B. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e05574 · Cited by 20
“These proteins are evolutionary conserved serine/threonine kinases that mediate a wide range of cellular processes, including cellular growth, differentiation, adaptation to stress, apoptosis or motility [6, 7, 8, 9].”
Background
Comparative Transcriptome Analysis of Spleen Reveals Potential Regulation of Genes and Immune Pathways Following Administration of Aeromonas salmonicida subsp. masoucida Vaccine in Atlantic Salmon (Salmo salar)
Fu, Q., Li, Y., Zhang, H., Cao, M., Zhang, L., Gao, C., Cai, X. M., Chen, D., Yang, Z., Li, J., et al. (2022) · Marine Biotechnology · doi:10.1007/s10126-021-10089-6 · Cited by 21
“Three major groups of MAPKs, namely the extracellular signal-regulated protein kinases (ERKs), the p38 MAP kinases, and the c-Jun NH2-terminal kinases (JNKs), have been identified in mammalian cells (Schaeffer and Weber 1999; Han and Ulevitch 1999; Davis 2000, Chang and Karin 2001).”
Background
Resibufogenin Targets the ATP1A1 Signaling Cascade to Induce G2/M Phase Arrest and Inhibit Invasion in Glioma
Zhang, X., Yao, Z., Xue, Z., Wang, S., Liu, X., Hu, Y., Zhang, Y., Wang, J., Li, X., & Chen, A. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.855626 · Cited by 21
“It has been demonstrated that signaling mediated by mitogen-activated protein kinases (MAPKs) plays an important role in regulating the cell cycle and responding to DNA damage (Schaeffer and Weber 1999).”
Background
Divulging the potency of naturally derived photosensitizers in green PDT: an inclusive review Of mechanisms, advantages, and future prospects
Gupta, M., Sahu, A., Mukherjee, T., Mohanty, S., Das, P., Nayak, N., Kumari, S., Singh, R. P., & Pattnaik, A. K. (2024) · Photochemical & Photobiological Sciences · doi:10.1007/s43630-024-00669-5 · Cited by 22
“Combinatorial therapeutic approaches involving PDT and immune checkpoint blockade demonstrate potency in colon cancer treatment [99].”
Sphingolipids and mitochondrial function in budding yeast
Spincemaille, P., Matmati, N., Hannun, Y. A., Cammue, B. P. A., & Thevissen, K. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.06.015 · Cited by 21
“the regulation of gene expression [63].”
Gastrulation in rabbit blastocysts depends on insulin and insulin-like-growth-factor 1
Thieme, R., Ramin, N., Fischer, S., Püschel, B., Fischer, B., & Santos, A. N. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.07.044 · Cited by 21
“The MAPK-Erk1/2-signalling-pathway is well known for regulation of cell growth, cell differentiation and development in mammals (for review see (Schaeffer and Weber, 1999)).”
Background
(–)-Xanthatin induces the prolonged expression of c-Fos through an N-acetyl-L-cysteine (NAC)-sensitive mechanism in human breast cancer MDA-MB-231 cells
Takeda, S., Nishimura, H., Koyachi, K., Matsumoto, K., Yoshida, K., Okamoto, Y., Amamoto, T., Shindo, M., & Aramaki, H. (2013) · The Journal of Toxicological Sciences · doi:10.2131/jts.38.547 · Cited by 21
Low-Density Lipoprotein Induced Expression of Connective Tissue Growth Factor via Transactivation of Sphingosine 1-Phosphate Receptors in Mesangial Cells
El‐Shewy, H. M., Sohn, M., Wilson, P. C., Lee, M., Hammad, S. M., Luttrell, L. M., & Jaffa, A. A. (2012) · Molecular Endocrinology · doi:10.1210/me.2011-1261 · Cited by 21
Identification of allosteric ERK2 inhibitors through in silico biased screening and competitive binding assay
Kinoshita, T., Sugiyama, H., Mori, Y., Takahashi, N., & Tomonaga, A. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.12.056 · Cited by 21
The HamE scaffold positively regulates MpkB phosphorylation to promote development and secondary metabolism in Aspergillus nidulans
Frawley, D., Karahoda, B., Bayram, Ö. S., & Bayram, Ö. (2018) · Scientific Reports · doi:10.1038/s41598-018-34895-6 · Cited by 21
Targeting Mitogen-Activated Protein Kinases by Natural Products: A Novel Therapeutic Approach for Inflammatory Bowel Diseases
Zobeiri, M., Momtaz, S., Parvizi, F., Tewari, D., Farzaei, M. H., & Nabavi, S. M. (2019) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201021666191216122555 · Cited by 21
Epigenetic and Posttranslational Modifications in Regulating the Biology of Aspergillus Species
Nie, X., Li, B., & Wang, S. (2018) · Advances in applied microbiology · doi:10.1016/bs.aambs.2018.05.004 · Cited by 21
pRB2/p130 target genes in non-small lung cancer cells identified by microarray analysis
Russo, G., Claudio, P. P., Fu, Y., Stiegler, P., Yu, Z., Macaluso, M., & Giordano, A. (2003) · Oncogene · doi:10.1038/sj.onc.1206866 · Cited by 21
Gene expression analysis in the ventral prostate of rats exposed to vinclozolin or procymidone
Rosen, M. B., Wilson, V. S., Schmid, J. E., & Gray, L. E. (2004) · Reproductive Toxicology · doi:10.1016/j.reprotox.2004.10.005 · Cited by 24
Comparative analysis of various in vitro COT kinase assay formats and their applications in inhibitor identification and characterization
Jia, Y., Quinn, C. M., Clabbers, A., Talanian, R. V., Xu, Y., Wishart, N., & Allen, H. (2005) · Analytical Biochemistry · doi:10.1016/j.ab.2005.11.010 · Cited by 21
Non-redundant Role of Shc in Erk Activation by Cytoskeletal Reorganization
Faisal, A., Kleiner, S., & Nagamine, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310010200 · Cited by 21
Strategies to design pyrazolyl urea derivatives for p38 kinase inhibition: a molecular modeling study
Kulkarni, R. G., Srivani, P., Garlapati, A., & Sastry, G. N. (2007) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-006-9092-9 · Cited by 21
MEF2C regulates c‐Jun but not TNF‐α gene expression in stimulated mast cells
Wei, X., Sun, W., Fan, R., Hahn, J., Joetham, A., Li, G., Webb, S., Garrington, T. P., Dakhama, A., Lucas, J. J., et al. (2003) · European Journal of Immunology · doi:10.1002/eji.200324127 · Cited by 21
Effects of piperine on antioxidant pathways in tissues from normal and streptozotocin-induced diabetic rats
Rauscher, F. M., Sanders, R. A., & Watkins, J. B. (2000) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/1099-0461(2000)14:6 · Cited by 105
Mercury Chloride Activates c-Jun N-Terminal Kinase and Induces c-jun Expression in LLC-PK1 Cells
Matsuoka, M. (2000) · Toxicological Sciences · doi:10.1093/toxsci/53.2.361 · Cited by 21
Protective induction of Hsp70 in heat‐stressed primary myoblasts: Involvement of MAPKs
Bironaitė, D., Brunk, U. T., & Venalis, A. (2013) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24550 · Cited by 20
Induction of cell death in RAW 264.7 cells by alpha-lactalbumin
Lin, I.-C., Su, S.-L., & Kuo, C. (2007) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.10.010 · Cited by 20
Sesamin attenuates allergic airway inflammation through the suppression of nuclear factor-kappa B activation
Li, L., Piao, H., Zheng, M., Jin, Z., Zhao, L., & Yan, G. (2016) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2016.3903 · Cited by 20
“MAPKs relay signals generated by endogenous and exogenous stimuli to the intra-cellular space through the phosphorylation of proteins (35-37).”
The gene task1 is involved in morphological development, mycoparasitism and antibiosis of Trichoderma asperellum
Yang, P. (2017) · Biocontrol Science and Technology · doi:10.1080/09583157.2017.1318824 · Cited by 20
“MAPKs regulate transcription factors by phosphorylation and are responsible for a variety of signal transmissions (Schaeffer & Weber, 1999).”
Background

Authors: Schaeffer, H. J., & Weber, M. J.
Affiliations: University of Virginia (US)
ORCID: Schaeffer, Hans J.
Weber, Michael J.
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 1999-04
Volume: 19
Issue: 4
Pages: 2435-2444
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.19.4.2435
PMC: PMC84036
OpenAlex: W1899552864
Semantic Scholar: bf5b29dd374f8bafd23fa8c6a133d764aa27c83f
Cited by: 1,600
References: 144
Citations by year: 2026: 12 · 2025: 12 · 2024: 24 · 2023: 32 · 2022: 23 · 2021: 28 · 2020: 19 · 2019: 37 · 2018: 43 · 2017: 27 · 2016: 31 · 2015: 41 · 2014: 42 · 2013: 49 · 2012: 61
FWCI: 9.18
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01gm047332-08, 1r01ca076500-01a1)
U.S. Public Health Service
National Cancer Institute (CA-39076, CA76500)
National Institute of General Medical Sciences (GM-47332)
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, signal transduction, ERK1/2, JNK, p38 MAPK, adaptor proteins, Saccharomyces cerevisiae, cell differentiation, stress response, apoptosis, cell growth and division
MeSH terms: Carrier Proteins, Cell Compartmentation, Fungal Proteins, Models, Biological, Morphogenesis, Protein Kinases, Saccharomyces cerevisiae, Substrate Specificity, Time Factors, Signal Transduction, Calcium-Calmodulin-Dependent Protein Kinases, Receptor Cross-Talk, Mitogen-Activated Protein Kinase Kinases, Saccharomyces cerevisiae Proteins, Adaptor Proteins, Signal Transducing

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Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers

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