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Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers
Open accessAbstract
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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“Four main MAPK cascades have been identified: ERK1/2 (extracellular signal-regulated kinases), c-Jun N-terminal kinases (JNK), p38 (p38 kinase), and the BMK1/ERK5 (big MAP kinase 1) (Schaeffer and Weber 1999).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Schaeffer and Weber 1999
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Citations
Cites
Marshall, C. J. (1995) · Cell · doi:10.1016/0092-8674(95)90401-8 · Cited by 3,906
Dérijard, B., Hibi, M., Wu, I.-H., Barrett, T., Su, B., Deng, T., Karin, M., & Davis, R. J. (1994) · Cell · doi:10.1016/0092-8674(94)90380-8 · Cited by 3,188
Mitogen-activated protein kinase pathways
Robinson, M. J., & Cobb, M. H. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80061-0 · Cited by 2,489
Signaling Through Scaffold, Anchoring, and Adaptor Proteins
Pawson, T., & Scott, J. D. (1997) · Science · doi:10.1126/science.278.5346.2075 · Cited by 2,256
Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP
de Rooij, J., Zwartkruis, F. J. T., Verheijen, M. H. G., Cool, R. H., Nijman, S. M. B., Wittinghofer, A., & Bos, J. L. (1998) · Nature · doi:10.1038/24884 · Cited by 1,970
Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase
Kato, S., Endoh, H., Masuhiro, Y., Kitamoto, T., Uchiyama, S., Sasaki, H., Masushige, S., Gotoh, Y., Nishida, E., Kawashima, H., et al. (1995) · Science · doi:10.1126/science.270.5241.1491 · Cited by 1,964
Cowley, S. A. (1994) · Cell · doi:10.1016/0092-8674(94)90133-3 · Cited by 1,959
Mammalian Ras interacts directly with the serine/threonine kinase raf
Vojtek, A. B., Hollenberg, S. M., & Cooper, J. A. (1993) · Cell · doi:10.1016/0092-8674(93)90307-c · Cited by 1,934
Knighton, D. R., Zheng, J., Eyck, L. F. T., Ashford, V. A., Xuong, N., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862342 · Cited by 1,764
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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Chauhan, P., Sodhi, A., & Shrivastava, A. (2008) · Immunobiology · doi:10.1016/j.imbio.2008.07.012 · Cited by 41
Wojda, I., Kowalski, P., & Jakubowicz, T. (2004) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.20001 · Cited by 41
Mor, D., Bembrick, A. L., Austin, P. J., & Keay, K. A. (2011) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2011.01.004 · Cited by 40
“In addition to pivotal roles in cell differentiation, movement and division, MEK2 also plays an important role in cell death, via its role in the ERK-p38 signal cascade, which is activated during inflammation and apoptosis (Platanias, 2003; Schaeffer and Weber, 1999).”
BackgroundHansen-Schwartz, J. A., Svensson, C., Xu, C., & Edvinsson, L. I. (2002) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704838 · Cited by 41
Lee, S. A., Park, J. K., Kang, E. K., Bae, H. R., Bae, K. W., & Park, H. T. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(99)00280-6 · Cited by 41
Lee, T.-J., Sartor, O. A., Luftig, R. B., & Koochekpour, S. (2004) · Molecular Cancer · doi:10.1186/1476-4598-3-31 · Cited by 41
“GPCRs also use pathways that are very similar to those utilized by RTKs to activate survival and anti-apoptotic signaling pathways such as the prototypic Raf-MEK-MAPK and PI3K/Akt signal transduction pathways and caspase cascades [32, 34- 37 ].”
BackgroundFluvastatin inhibits growth and alters the malignant phenotype of the C6 glioma cell line
Sławińska-Brych, A., Zdzisińska, B., & Kandefer‐Szerszeń, M. (2014) · Pharmacological Reports · doi:10.1016/j.pharep.2014.01.002 · Cited by 41
“Recent evidence has suggested that modulation of several effectors of the MAPK signaling pathway that regulate diverse physiological processes such as differentiation, proliferation, oncogenic transformation, and programmed cell death [36], may be critical factors in the antiproliferative and proapoptotic action of HM…”
BackgroundPintucci, G., Yu, P., Sharony, R., Baumann, F. G., Saponara, F., Frasca, A., Galloway, A. C., Moscatelli, D., & Mignatti, P. (2003) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10721 · Cited by 41
The roles of MAPK signaling pathway in ovarian folliculogenesis
Zhao, H. L., Trang, D., Wang, Y., & Yang, Y. (2025) · Journal of Ovarian Research · doi:10.1186/s13048-025-01737-9 · Cited by 47
“The MAPK signaling pathway is a highly conserved signal transduction cascade that is widely present from yeast to humans [15].”
Neonicotinoids and Derivatives: Effects in Mammalian Cells and Mice
Tomizawa, M. (2004) · Journal of Pesticide Science · doi:10.1584/jpestics.29.177 · Cited by 40
Behren, A., Mühlen, S., Sanhueza, G. A., Schwager, C., Plinkert, P. K., Huber, P. E., Abdollahi, A., & Simon, C. (2009) · Oncogene · doi:10.1038/onc.2009.436 · Cited by 40
“Two kinases, MKK3 and MKK6, are known to activate p38 (Raingeaud et al., 1996; Schaeffer and Weber, 1999).”
BackgroundActivation of c-Jun N-terminal kinase (JNK) pathway by HSV-1 immediate early protein ICP0
Diao, L., Zhang, B., Xuan, C., Sun, S., Yang, K. S., Tang, Y., Qiao, W., Chen, Q., Geng, Y., & Wang, C. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.04.016 · Cited by 40
“Three major groups of MAPK have been identified in mammals [29], p38, the ERK (extracellular signal-regulated protein kinases) and the JNK (also known as stressactivated MAP kinases, SAPK).”
BackgroundGaldiero, S., Capasso, D., Vitiello, M., D’Isanto, M., Pedone, C., & Galdiero, M. (2003) · Infection and Immunity · doi:10.1128/iai.71.5.2798-2809.2003 · Cited by 40
“In mammalian systems, five different MAPK modules have been identified so far; single MAPK modules can signal independent of one another, and this specificity is manifest in different physiological responses (60).”
Backgroundp38 MAP Kinase Inhibits Neutrophil Development Through Phosphorylation of C/EBPα on Serine 21
Geest, C. R., Buitenhuis, M., Laarhoven, A. G., Bierings, M., Bruin, M. C. A., Vellenga, E., & Coffer, P. J. (2009) · Stem Cells · doi:10.1002/stem.152 · Cited by 40
The MAP3K ZAK, a novel modulator of ERK-dependent migration, is upregulated in colorectal cancer
Rey, C., Faustin, B., Mahouche, I., Ruggieri, R., Brulard, C., Ichas, F., Soubeyran, I., Lartigue, L., & Giorgi, F. D. (2015) · Oncogene · doi:10.1038/onc.2015.379 · Cited by 40
Lu, C., Lin, H.-I., Chen, B., & Jow, G. (2016) · The Journal of Toxicological Sciences · doi:10.2131/jts.41.429 · Cited by 40
Selected Molecular Mechanisms of Metal Toxicity and Carcinogenicity
Davidson, T. L., Ke, Q., & Costa, M. (2014) · Elsevier eBooks · doi:10.1016/b978-0-444-59453-2.00009-3 · Cited by 40
Anisomycin Affects Both Pro- and Antiapoptotic Mechanisms in PC12 Cells
Törőcsik, B., & Szeberényi, J. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3836 · Cited by 40
Contrasting signal transduction mechanisms in bacterial and eukaryotic gene transcription
Cashin, P., Goldsack, L. M., Hall, D., & O’Toole, R. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2006.00295.x · Cited by 38
Characterization of the ERK homologue CpMK2 from the chestnut blight fungus Cryphonectria parasitica
Choi, E., Chung, H., Kim, M., Park, S.-M., Cha, B., Yang, M., & Kim, D. (2005) · Microbiology · doi:10.1099/mic.0.27796-0 · Cited by 40
“This cascade, which occurs in a wide variety of organisms from yeast to humans (Herskowitz, 1995; Schaeffer & Weber, 1999), consists of three functionally interlinked protein kinases: MEEK (MAP kinase kinase kinase), MEK (MAP kinase kinase) and MAPK.”
BackgroundFreeman, S. E., Patil, V. V., & Durham, P. L. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.09.035 · Cited by 41
Yamauchi, J., Tsujimoto, G., Kaziro, Y., & Itoh, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011752200 · Cited by 40
Retinoic Acid Inhibits Cardiac Neural Crest Migration by Blocking c-Jun N-Terminal Kinase Activation
Li, J., Molkentin, J. D., & Colbert, M. C. (2001) · Developmental Biology · doi:10.1006/dbio.2001.0203 · Cited by 40
Tajti, J., Kuris, A., Vécsei, L., Xu, C., & Edvinsson, L. I. (2010) · Cephalalgia · doi:10.1177/0333102410382796 · Cited by 39
“Specific antibodies against CGRP, phosphorylated ERK1/2 (pERK1/2), total ERK1/2 (tERK1/2), phosphorylated p38 (pp38), phosphorylated C-Jun-N-terminal protein kinase (pJNK), pro-calcitonin (pro-CT), CGRP receptor activity modifying protein 1 (RAMP1), glutamine synthetase (GS) and pro-CT were used.”
BackgroundInfluentialMitochondrial Impairment Mediates Cytolysis in Anthrax Lethal Toxin-Treated Murine Macrophages
Alileche, A., Squires, R. C., Muehlbauer, S. M., Lisanti, M. P., & Brojatsch, J. (2006) · Cell Cycle · doi:10.4161/cc.5.1.2283 · Cited by 39
Mikuzuki, L., Saito, H., Katagiri, A., Okada, S., Sugawara, S., Kubo, A., Ohara, K., Lee, J., Toyofuku, A., & Iwata, K. (2017) · European Journal of Neuroscience · doi:10.1111/ejn.13667 · Cited by 40
Yeung, Y. T., Yin, S., Lu, B., Fan, S., Yang, R., Bai, R., Zhang, C., Bode, A. M., Liu, K., & Dong, Z. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.01.017 · Cited by 39
“The p38 MAPK belongs to the mitogen activated protein kinase (MAPK) superfamily and is a major cellular signal transducer of extracellular stress (Han et al., 1994; Schaeffer and Weber, 1999).”
BackgroundMitogen-Activated Protein Kinase Inhibitors and T-Cell-Dependent Immunotherapy in Cancer
Kumar, S., Principe, D. R., Singh, S. K., Viswakarma, N., Sondarva, G. V., Rana, B., & Rana, A. (2020) · Pharmaceuticals · doi:10.3390/ph13010009 · Cited by 38
“Mitogen-activated protein kinase (MAPK) signaling is mediated by several MAPK family members, sharing several evolutionary-conserved domains [1].”
BackgroundNew Insights into the Mechanism of JNK1 Inhibition by Glutathione Transferase P1-1
Luca, A. D., Federici, L., Canio, M. D., Stella, L., & Caccuri, A. M. (2012) · Biochemistry · doi:10.1021/bi300559m · Cited by 40
Ulisse, S., Cinque, B., Silvano, G., Rucci, N., Biordi, L. A., Cifone, M. G., & D’Armiento, M. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400716 · Cited by 39
Ham, Y., Choi, J., Chun, K., Joo, S.-H., & Lee, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302997200 · Cited by 39
Takeda, S., Matsuo, K., Yaji, K., Okajima-Miyazaki, S., Harada, M., Miyoshi, H., Okamoto, Y., Amamoto, T., Shindo, M., Omiecinski, C. J., et al. (2011) · Chemical Research in Toxicology · doi:10.1021/tx200046s · Cited by 38
Thomas, R., Gohlke, J. M., Stopper, G. F., Parham, F., & Portier, C. J. (2009) · Genome biology · doi:10.1186/gb-2009-10-4-r44 · Cited by 38
“Alterna-tively, intermediate kinase components are shared by numerous pathways and, in general, do not convey specificity nor do they directly dictate the ultimate response (see [39] for a review).”
BackgroundH2S‐induced pancreatic acinar cell apoptosis is mediated via JNK and p38 MAP kinase
Adhikari, S., & Bhatia, M. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00318.x · Cited by 38
“Each of these MAPKs has unique role in the regulation of cellular metabolism and gene expression related to growth, apoptosis and cellular responses to external stresses [44].”
BackgroundIsoforms of JSAP1 scaffold protein generated through alternative splicing
Ito, M., Akechi, M., Hirose, R., Ichimura, M., Takamatsu, N., Xu, P., Nakabeppu, Y., Shiba, T., Yamamoto, K.-I., & Yoshioka, K. (2000) · Gene · doi:10.1016/s0378-1119(00)00335-8 · Cited by 38
Teraishi, F., Zhang, L., Guo, W., Dong, F., Davis, J. J., Lin, A., & Fang, B. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.10.064 · Cited by 38
Hayashi, H., Matsuzaki, O., Muramatsu, S., Tsuchiya, Y., Harada, T., Suzuki, Y., Sugano, S., Matsuda, A., & Nishida, E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505905200 · Cited by 38
Kooter, I. M., Pennings, J. L. A., Opperhuizen, A., & Cassee, F. R. (2004) · Inhalation Toxicology · doi:10.1080/08958370590885717 · Cited by 38
“The ERK pathway is activated by growth factors and oxidative stress in a Ras/Raf/MEK1-dependent fashion, and it is important in cellular proliferation and differentiation (Schaeffer & Weber, 1999).”
BackgroundFocal adhesion kinase (FAK), une protéine aux fonctions multiples
Cornillon, J., Campos, L., & Guyotat, D. (2003) · médecine/sciences · doi:10.1051/medsci/20031967743 · Cited by 48
Effects of Heavy Metals on Mitogen-Activated Protein Kinase Pathways.
Matsuoka, M., & Igisu, H. (2002) · Environmental Health and Preventive Medicine · doi:10.1007/bf02897972 · Cited by 37
Gailhouste, L., Ezan, F., Bessard, A., Frémin, C., Rageul, J., Langouët, S., & Baffet, G. (2009) · International Journal of Cancer · doi:10.1002/ijc.24950 · Cited by 38
“phorylation from the membrane receptors to downstream cytoplasmic and nuclear substrates.(3,4) The MEK/ERK path-”
BackgroundNunes, P. H. C., Calaza, K. D. C., Albuquerque, L. M., Madeira, L. F., Sholl‐Franco, A., & Ventura, A. L. M. (2007) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2007.09.007 · Cited by 37
“The ERK pathway is a membrane-to-nucleus signaling module involved in multiple physiological processes, including cell proliferation, cell differentiation and apoptosis (Schaeffer and Weber, 1999; Peyssonnaux and Eychène, 2001).”
BackgroundOncogenic Signaling in Tumorigenesis and Applications of siRNA Nanotherapeutics in Breast Cancer
Kamaruzman, N. I., Abd-Aziz, N., Poh, C. L., & Chowdhury, E. H. (2019) · Cancers · doi:10.3390/cancers11050632 · Cited by 37
The Calcium-Sensing Receptor as a Regulator of Cellular Fate in Normal and Pathological Conditions
Diez‐Fraile, A., Lammens, T., Benoit, Y., & D'Herde, K. G. M. A. (2013) · Current Molecular Medicine · doi:10.2174/1566524011313020005 · Cited by 37
Activation of Mitogen-activated Protein Kinase Kinase (MKK) 3 and MKK6 by Type I Interferons
Li, Y., Batra, S., Sassano, A., Majchrzak, B., Levy, D. E., Gaestel, M., Fish, E. N., Davis, R. J., & Platanias, L. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410972200 · Cited by 37
Involvement of MAPK proteins in bystander effects induced by chemicals and ionizing radiation
Asur, R. S., Balasubramaniam, M., Marples, B., Thomas, R. A., & Tucker, J. D. (2009) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2009.12.007 · Cited by 38
Goldberg-Bittman, L., Sagi‐Assif, O., Meshel, T., Nevo, I., Levy‐Nissenbaum, O., Yron, I., Witz, I. P., & Ben‐Baruch, A. (2004) · Cytokine · doi:10.1016/j.cyto.2004.10.003 · Cited by 37
Crystal structure of human ERK2 complexed with a pyrazolo[3,4-c]pyridazine derivative
Kinoshita, T., Warizaya, M., Ohori, M., Sato, K., Neya, M., & Fujii, T. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.09.055 · Cited by 37
Positive Regulation of Apoptosis Signal-regulating Kinase 1 by hD53L1
Cho, S., Ko, H.-M., Kim, J., Lee, J.-A., Park, J.-E., Jang, M.-S., Park, S. G., Lee, D. H., Ryu, S.-E., & Park, B.-C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m305758200 · Cited by 37
Paolis, P. D., Porcellini, A., Savoia, C., Lombardi, A., Gigante, B., Frati, G., Rubattu, S., Musumeci, B., & Volpe, M. (2002) · Journal of Hypertension · doi:10.1097/00004872-200204000-00027 · Cited by 37
Expression of the β4 integrin subunit induces monocytic differentiation of 32D/v-Abl cells
Morena, A. R., Riccioni, S., Marchetti, A., Polcini, A. T., Mercurio, A. M., Blandino, G., Sacchi, A., & Falcioni, R. (2002) · Blood · doi:10.1182/blood.v100.1.96 · Cited by 37
miR-506 regulates breast cancer cell metastasis by targeting IQGAP1
Sun, G., Liu, Y., Wang, K., & Xu, Z. (2015) · International Journal of Oncology · doi:10.3892/ijo.2015.3161 · Cited by 36
Regulatory roles of phosphorylation in model and pathogenic fungi
Bataineh, M. T. A., & Kadosh, D. (2015) · Medical Mycology · doi:10.1093/mmy/myv098 · Cited by 37
Huth, H. W., Albarnaz, J. D., Torres, A. A., Bonjardim, C. A., & Ropert, C. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.05.009 · Cited by 36
Xie, M., Bai, N., Yang, J., Jiang, K., Zhou, D., Zhao, Y., Li, D., Niu, X., Zhang, K., & Yang, J. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.03065 · Cited by 36
Wang, S., Uchi, H., Hayashida, S., Urabe, K., Moroi, Y., & Furue, M. (2009) · The Journal of Dermatology · doi:10.1111/j.1346-8138.2009.00696.x · Cited by 36
IKVAV regulates ERK1/2 and Akt signalling pathways in BMMSC population growth and proliferation
Li, B., Qiu, T., Zhang, P., Wang, X., Yin, Y., & Li, S. (2014) · Cell Proliferation · doi:10.1111/cpr.12094 · Cited by 36
XAF1 mediates apoptosis through an extracellular signal‐regulated kinase pathway in colon cancer
Yu, L., Wang, J., Zou, B., Lin, M. C. M., Wu, Y., Xia, H. H., Sun, Y. W., Gu, Q., He, H., Lam, S. K., et al. (2007) · Cancer · doi:10.1002/cncr.22624 · Cited by 36
“M itogen-activated protein kinases (MAPKs) or extracellular signal-regulated protein kinases (ERKs) comprise a family of serine/threonine protein kinases that mediate intracellular phosphorylation events linking receptor activation to the control of cell proliferation, chemotaxis, differentiation, and stress response.…”
BackgroundAnisotropic regulation of Ankrd2 gene expression in skeletal muscle by mechanical stretch
Mohamed, J. S., Lopez, M. A., Cox, G. A., & Boriek, A. M. (2010) · The FASEB Journal · doi:10.1096/fj.10-158386 · Cited by 36
Hofmann, M., Ivosevic-Zaper, J., Bernd, A., Bereiter‐Hahn, J., Kaufmann, R., & Kippenberger, S. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.02.101 · Cited by 36
Zhang, W., Chen, T., Wan, T. Y., He, L., Li, N., Yuan, Z., & Cao, X. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3244 · Cited by 36
Souza, R. F., Shewmake, K., Shen, Y., Ramirez, R. D., Bullock, J. S., Hladik, C. L., Lee, E. L., Terada, L. S., & Spechler, S. J. (2005) · The American Journal of Gastroenterology · doi:10.1111/j.1572-0241.2005.41122.x · Cited by 35
“The ability of ERK1/2-mediated signaling to promote either growth arrest and cellular differentiation or cellular proliferation depends both on the duration of the ERK1/2 signal and the cell type involved (6, 10, 25).”
BackgroundDifferential localization of MAPK-activated protein kinases RSK1 and MSK1 in mouse brain
Heffron, D. S., & Mandell, J. W. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2005.01.014 · Cited by 36
Ozaki, I. (2003) · Hepatology Research · doi:10.1016/s1386-6346(03)00268-7 · Cited by 36
Protein kinase A balances the growth factor‐induced Ras/ERK signaling
Pursiheimo, J., Kieksi, A., Jalkanen, M., & Salmivirta, M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02864-8 · Cited by 36
Slomiany, B. L., & Slomiany, A. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00463-1 · Cited by 36
Roy, J., Kazi, M., Hedin, U., & Thyberg, J. (2001) · Differentiation · doi:10.1046/j.1432-0436.2001.067001050.x · Cited by 36
PGE2stimulates human brain natriuretic peptide expression via EP4and p42/44 MAPK
Qian, J.-Y., Leung, A., Harding, P., & LaPointe, M. C. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00904.2005 · Cited by 35
Ferland‐Beckham, C., Harris, E. P., Lam, M., & Schrader, L. A. (2014) · Endocrinology · doi:10.1210/en.2013-1918 · Cited by 36
Frawley, D., & Bayram, Ö. (2020) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2020.103469 · Cited by 34
P2Y2 nucleotide receptors inhibit trauma‐induced death of astrocytic cells
Burgos, M., Neary, J. T., & González, F. A. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04872.x · Cited by 35
Hornigold, D. C., Mistry, R., Raymond, P. D., Blank, J. L., & Challiss, R. A. J. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705178 · Cited by 35
“…both the M1/M3/M5 and M2/M4 subfamilies (Winitz et al., 1993; Crespo et al., 1994; Mitchell et al., 1995), suggesting the potential for mACh receptor cross-talk in the regulation of extracellular signal- regulated kinase (ERK) and c-Jun N-terminal kinase (JNK) cascades (Schaeffer & Weber, 1999).”
BackgroundKo, J., Liu, Y., Yanai, R., Chikama, T.-I., Takezawa, T., & Nishida, T. (2008) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.07-0353 · Cited by 35
Analysis of Ecstasy (MDMA)‐induced transcriptional responses in the rat cortex
Thiriet, N., Ladenheim, B., McCoy, M. T., & Cadet, J. L. (2002) · The FASEB Journal · doi:10.1096/fj.02-0502com · Cited by 35
ERK phosphorylation is required for retention of trace fear memory
Villarreal, J. S., & Barea-Rodrı́guez, E. J. (2005) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2005.08.005 · Cited by 34
Single‐molecule pull‐down (SiMPull) for new‐age biochemistry
Aggarwal, V., & Ha, T. (2014) · BioEssays · doi:10.1002/bies.201400090 · Cited by 34
Pulsed electromagnetic fields promote survival and neuronal differentiation of human BM-MSCs
Urnukhsaikhan, E., Cho, H., Mishig‐Ochir, T., Seo, Y., & Park, J.-K. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.02.066 · Cited by 35
Molecular ‘palpation’ of BPH: a tale of MAPK signalling?
Papatsoris, A., & Papavassiliou, A. G. (2001) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02015-9 · Cited by 35
Colorectal tumors frequently express phosphorylated mitogen‐activated protein kinase
Lee, S. H., Lee, J. W., Soung, Y. H., Kim, S. Y., Nam, S. W., Park, W. S., Kim, S. H., Yoo, N. J., & Lee, J. Y. (2004) · Apmis · doi:10.1111/j.1600-0463.2004.apm11204-0502.x · Cited by 36
“Mitogen-activated protein (MAP) kinase is activated in response to a variety of cellular stimuli and controls the proliferation, differentiation and development of the cells (1, 2).”
BackgroundLania, A. G., Filopanti, M., Corbetta, S., Losa, M., Ballarè, E., Beck‐Peccoz, P., & Spada, A. (2003) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2002-021207 · Cited by 35
A synthetic peptide mimic kills Candida albicans and synergistically prevents infection
Schaefer, S., Vij, R., Sprague, J. L., Austermeier, S., Dinh, H., Judzewitsch, P. R., Müller‐Loennies, S., Silva, T. L., Seemann, E. A., Qualmann, B., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50491-x · Cited by 41
“An upregulation of genes in the MAPK signalling pathway is typical for cell wall and osmotic stress or star-vation and leads to cell cycle arrest and cell wall remodelling 48,49 .”
Regulatory roles of conserved phosphorylation sites in the activation T-loop of the MAP kinase ERK1
Lai, S., & Pelech, S. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-07-0527 · Cited by 36
“Mitogen-activated protein kinases (MAPKs) play fundamental roles in the regulation of a broad diversity of functions, including meiosis, cell cycle progression, and stress responses, from yeast to humans (Schaeffer and Weber, 1999; Raman et al., 2007).”
BackgroundDong, W., Xie, W., Liu, Y., Sui, B., Zhang, H., Liu, L., Tan, Y., Tong, X., Fu, Z. F., Yin, P., et al. (2019) · Antiviral Research · doi:10.1016/j.antiviral.2019.104651 · Cited by 34
“Antibodies against p38, Jun-N-terminal kinases (JNKs), phosphorylated p38 (p-p38) and phosphorylated JNKs (p-JNKs) were purchased from Cell Signaling Technology (Washington, DC, USA).”
BackgroundDysregulation of cellular membrane homeostasis as a crucial modulator of cancer risk
Erazo‐Oliveras, A., Muñoz‐Vega, M., Salinas, M. L., Wang, X., & Chapkin, R. S. (2022) · FEBS Journal · doi:10.1111/febs.16665 · Cited by 38
Differences in activation of ERK1/2 and p38 kinase in Jnk3 null mice following KA treatment
de Lemos, L., Junyent, F., Verdaguer, E., Folch, J., Romero, R., Pallàs, M., Ferrer, I., Auladell, C., & Camins, A. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06853.x · Cited by 34
Lee, Y. S., Yoon, S., Yoon, H.-J., Lee, K., Yoon, H. K., Lee, J., & Song, C. W. (2009) · Toxicology Letters · doi:10.1016/j.toxlet.2009.05.019 · Cited by 34
Lin, J., Chang, S., Hsieh, D.-S., Lee, C.-F., & Yü, D. (2005) · The Journal of Urology · doi:10.1097/01.ju.0000176476.14572.39 · Cited by 34
Targeting Raf/MEK/ERK pathway in pituitary adenomas
Zhang, S., Feng, W., Dongsheng, G., & Lei, T. (2011) · European Journal of Cancer · doi:10.1016/j.ejca.2011.11.002 · Cited by 35
Neuroprotective and procognitive effects of sertraline: In vitro and in vivo studies
Taler, M., Miron, O., Gil‐Ad, I., & Weizman, A. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.06.033 · Cited by 35
Zhou, Q., Zhang, H., Lu, Y., Wang, X., & Su, S. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2009.01297.x · Cited by 34
Determinants That Control the Specific Interactions between TAB1 and p38α
Zhou, H., Zheng, M., Chen, J., Xie, C., Kolatkar, A. R., Zarubin, T., Ye, Z., Akella, R., Lin, S., Goldsmith, E. J., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.10.3824-3834.2006 · Cited by 34
“MAPKs catalyze the phosphorylation of their targets, which include transcription factors and protein kinases (9, 15, 22, 25, 34, 37).”
BackgroundHuang, W., Mishra, V., Batra, S., Dillon, I., & Mehta, K. D. (2004) · Journal of Lipid Research · doi:10.1194/jlr.m400088-jlr200 · Cited by 34
Cañadillas, S., Canalejo, R., Rodríguez-Ortiz, M. E., Martinez-Moreno, J. M., Estepa, J. C., Zafra, R., Pérez, J., Muñoz-Castañeda, J. R., Canalejo, A., Rodríguez, M., et al. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00529.2009 · Cited by 34
“Activated PLA2 is also associated with phosphorylation of MAPK, as ERK 1/2 and p38-MAPK (12, 34).”
BackgroundKim, S.-H., Kwon, H., Kim, Y. S., Ryu, J.-H., Kim, K., Ahn, Y., Lee, W., & Choi, K. (2001) · Biochemical Journal · doi:10.1042/bj3610143 · Cited by 34
Bhattacharjya, S., Xu, P., Gingras, R., Shaykhutdinov, R. A., Wu, C., Whiteway, M. S., & Ni, F. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.09.018 · Cited by 34
The human stress-activated protein kinase-interacting 1 gene encodes JNK-binding proteins
Schroder, W. A., Bushell, G. R., & Sculley, T. B. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.10.015 · Cited by 34
Hall, J. P., & Davis, R. J. (2002) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10187 · Cited by 34
Fumagalli, F., Frasca, A., Spartà, M., Drago, F., Racagni, G., & Riva, M. A. (2006) · Molecular Pharmacology · doi:10.1124/mol.105.019828 · Cited by 34
Nakajima, M., Negishi, Y., Tanaka, H., & Kawashima, K. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.057 · Cited by 34
ATM-dependent activation of the gene encoding MAP kinase phosphatase 5 by radiomimetic DNA damage
Bar‐Shira, A., Rashi‐Elkeles, S., Zlochover, L., Moyal, L., Smorodinsky, N. I., Seger, R., & Shiloh, Y. (2002) · Oncogene · doi:10.1038/sj.onc.1205127 · Cited by 34
Metadata
- Authors
- Schaeffer, H. J., & Weber, M. J.
- Affiliations
- University of Virginia (US)
- 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
- 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
- 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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