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Pro-inflammatory Cytokines and Environmental Stress Cause p38 Mitogen-activated Protein Kinase Activation by Dual Phosphorylation on Tyrosine and Threonine
Open accessAbstract
Protein kinases activated by dual phosphorylation on Tyr and Thr (MAP kinases) can be grouped into two major classes: ERK and JNK. The ERK group regulates multiple targets in response to growth factors via a Ras-dependent mechanism. In contrast, JNK activates the transcription factor c-Jun in response to pro-inflammatory cytokines and exposure of cells to several forms of environmental stress. Recently, a novel mammalian protein kinase (p38) that shares sequence similarity with mitogen-activated protein (MAP) kinases was identified. Here, we demonstrate that p38, like JNK, is activated by treatment of cells with pro-inflammatory cytokines and environmental stress. The mechanism of p38 activation is mediated by dual phosphorylation on Thr-180 and Tyr-182. Immunofluorescence microscopy demonstrated that p38 MAP kinase is present in both the nucleus and cytoplasm of activated cells. Together, these data establish that p38 is a member of the mammalian MAP kinase group.
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Citations
Cites
Hibi, M., Lin, A., Smeal, T., Minden, A., & Karin, M. (1993) · Genes & Development · doi:10.1101/gad.7.11.2135 · Cited by 1,886
Independent Human MAP-Kinase Signal Transduction Pathways Defined by MEK and MKK Isoforms
Dérijard, B., Raingeaud, J., Barrett, T., Wu, I.-H., Han, J., Ulevitch, R. J., & Davis, R. J. (1995) · Science · doi:10.1126/science.7839144 · Cited by 1,555
Self-citationSun, H., Charles, C. H., Lau, L. F., & Tonks, N. K. (1993) · Cell · doi:10.1016/0092-8674(93)90383-2 · Cited by 1,156
Kallunki, T., Su, B., Tsigelny, I., Sluss, H. K., Dérijard, B., Moore, G., Davis, R., & Karin, M. (1994) · Genes & Development · doi:10.1101/gad.8.24.2996 · Cited by 642
Self-citationRotation of photoreceptor clusters in the developing drosophila eye requires the nemo gene
Choi, K.-W., & Benzer, S. (1994) · Cell · doi:10.1016/0092-8674(94)90579-7 · Cited by 339
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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
Muscle as an Endocrine Organ: Focus on Muscle-Derived Interleukin-6
Pedersen, B. K., & Febbraio, M. A. (2008) · Physiological Reviews · doi:10.1152/physrev.90100.2007 · Cited by 2,388
Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377
Carbon monoxide has anti-inflammatory effects involving the mitogen-activated protein kinase pathway
Otterbein, L. E., Bach, F. H., Alam, J., Soares, M., Tao Lu, H., Wysk, M., Davis, R. J., Flavell, R. A., & Choi, A. M. K. (2000) · Nature Medicine · doi:10.1038/74680 · Cited by 2,153
Self-citationLiu, Z.-G., Hsu, H., Goeddel, D. V., & Karin, M. (1996) · Cell · doi:10.1016/s0092-8674(00)81375-6 · Cited by 1,937
Whitmarsh, A. J., & Davis, R. J. (1996) · Journal of Molecular Medicine · doi:10.1007/s001090050063 · Cited by 1,543
Self-citationAguirre, V., Uchida, T., Yenush, L., Davis, R., & White, M. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.9047 · Cited by 1,487
Self-citationMitogen-activated protein kinases in apoptosis regulation
Wada, T., & Penninger, J. M. (2004) · Oncogene · doi:10.1038/sj.onc.1207556 · Cited by 1,432
Regulation of transcription by MAP kinase cascades
Treisman, R. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80067-6 · Cited by 1,296
Excitotoxicity and stroke: Identifying novel targets for neuroprotection
Lai, T. W., Zhang, S., & Wang, Y. T. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.11.006 · Cited by 1,106
Regulatory interactions between muscle and the immune system during muscle regeneration
Tidball, J. G., & Villalta, S. A. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00735.2009 · Cited by 1,105
JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis
Lei, K., & Davis, R. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0438011100 · Cited by 1,068
Self-citationThe Role of c-Jun N-terminal Kinase (JNK) in Apoptosis Induced by Ultraviolet C and γ Radiation
Chen, Y.-R., Wang, X., Templeton, D., Davis, R. J., & Tan, T.-H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.50.31929 · Cited by 867
Self-citationPhosphatase‐mediated crosstalk between MAPK signaling pathways in the regulation of cell survival
Junttila, M. R., Li, S., & Westermarck, J. (2008) · The FASEB Journal · doi:10.1096/fj.06-7859rev · Cited by 826
Mitogen-activated protein kinase cascades and regulation of gene expression
Su, B., & Karin, M. (1996) · Current Opinion in Immunology · doi:10.1016/s0952-7915(96)80131-2 · Cited by 747
Cytokine Stimulation of Energy Expenditure through p38 MAP Kinase Activation of PPARγ Coactivator-1
Puigserver, P., Rhee, J., Lin, J., Wu, Z., Yoon, J. C., Zhang, C.-Y., Krauss, S., Mootha, V. K., Lowell, B. B., & Spiegelman, B. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00390-2 · Cited by 732
A Cytoplasmic Inhibitor of the JNK Signal Transduction Pathway
Dickens, M., Rogers, J. S., Cavanagh, J., Raitano, A., Xia, Z., Halpern, J. R., Greenberg, M. E., Sawyers, C. L., & Davis, R. J. (1997) · Science · doi:10.1126/science.277.5326.693 · Cited by 675
Self-citationPain, T., Yang, X.-M., Critz, S. D., Yue, Y., Nakano, A., Liu, G. S., Heusch, G., Cohen, M. V., & Downey, J. M. (2000) · Circulation Research · doi:10.1161/01.res.87.6.460 · Cited by 662
Oxidative Stress, Molecular Inflammation and Sarcopenia
Meng, S.-J., & Yu, L.-J. (2010) · International Journal of Molecular Sciences · doi:10.3390/ijms11041509 · Cited by 637
CX3CR1 deficiency leads to impairment of hippocampal cognitive function and synaptic plasticity
Rogers, J. T., Morganti, J. M., Bachstetter, A. D., Hudson, C. E., Peters, M. M., Grimmig, B. A., Weeber, E. J., Bickford, P. C., & Gemma, C. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3667-11.2011 · Cited by 624
Self-citationZhang, S., Han, J., Sells, M. A., Chernoff, J., Knaus, U. G., Ulevitch, R. J., & Bokoch, G. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.23934 · Cited by 614
Self-citationTNF receptor subtype signalling: Differences and cellular consequences
MacEwan, D. J. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00262-5 · Cited by 610
Luo, L., Li, D.-Q., Doshi, A., Farley, W., Corrales, R. M., & Pflugfelder, S. C. (2004) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.03-1145 · Cited by 595
Dual‐specificity MAP kinase phosphatases (MKPs): Shaping the outcome of MAP kinase signalling
Caunt, C. J., & Keyse, S. M. (2013) · The FEBS Journal · doi:10.1111/j.1742-4658.2012.08716.x · Cited by 535
Hsu, H.-Y., & Wen, M.-H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111883200 · Cited by 519
Schäfers, M., Svensson, C. I., Sommer, C., & Sorkin, L. S. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-07-02517.2003 · Cited by 519
Heme oxygenase/carbon monoxide signaling pathways: Regulation and functional significance
Ryter, S. W., Otterbein, L. E., Morse, D., & Choi, A. M. K. (2002) · Molecular and Cellular Biochemistry · doi:10.1023/a:1015957026924 · Cited by 497
p38 Mitogen-activated Protein Kinase Pathway Promotes Skeletal Muscle Differentiation
Zetser, A., Gredinger, E., & Bengal, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.5193 · Cited by 461
The p38 MAPK inhibitors for the treatment of inflammatory diseases and cancer
Yong, H.-Y., Koh, M.-S., & Moon, A. (2009) · Expert Opinion on Investigational Drugs · doi:10.1517/13543780903321490 · Cited by 422
Fisher, G. J., Talwar, H. S., Lin, J., Lin, P., McPhillips, F., Wang, Z., Li, X., Wan, Y., Kang, S., & Voorhees, J. J. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2153 · Cited by 392
Glucose or diabetes activates p38 mitogen-activated protein kinase via different pathways
Igarashi, M., Wakasaki, H., Takahara, N., Ishii, H., Jiang, Z.-Y., Yamauchi, T., Kuboki, K., Meier, M., Rhodes, C. J., & King, G. L. (1999) · Journal of Clinical Investigation · doi:10.1172/jci3326 · Cited by 386
Wang, W., Chen, J. X., Liao, R., Deng, Q., Zhou, J. J., Huang, S., & Sun, P. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.10.3389-3403.2002 · Cited by 376
p38 Kinase Is Activated in the Alzheimer's Disease Brain
Hensley, K., Floyd, R. A., Zheng, N., Nael, R., Robinson, K. A., Nguyen, X., Pye, Q. N., Stewart, C. A., Geddes, J., Markesbery, W. R., et al. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722053.x · Cited by 373
Nuclear Accumulation of NFAT4 Opposed by the JNK Signal Transduction Pathway
Chow, C.-W., Rincón, M., Cavanagh, J., Dickens, M., & Davis, R. J. (1997) · Science · doi:10.1126/science.278.5343.1638 · Cited by 357
Self-citationVillalta, S. A., Rinaldi, C., Deng, B., Liu, G., Fedor, B., & Tidball, J. G. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddq523 · Cited by 299
Antagonism of glucocorticoid receptor transcriptional activation by the c-Jun N-terminal kinase
Rogatsky, I., Logan, S. K., & Garabedian, M. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2050 · Cited by 297
Vandevyver, S., Dejager, L., Tuckermann, J., & Libert, C. (2013) · Endocrinology · doi:10.1210/en.2012-2045 · Cited by 296
The 70 kDa S6 Kinase Complexes with and Is Activated by the Rho Family G Proteins Cdc42 and Rac1
Chou, M. M., & Blenis, J. (1996) · Cell · doi:10.1016/s0092-8674(00)81257-x · Cited by 292
The structure of mitogen-activated protein kinase p38 at 2.1-Å resolution
Wang, Z., Harkins, P. C., Ulevitch, R. J., Han, J., Cobb, M. H., & Goldsmith, E. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2327 · Cited by 275
Self-citationInflammation induced loss of skeletal muscle
Londhe, P., & Guttridge, D. C. (2015) · Bone · doi:10.1016/j.bone.2015.03.015 · Cited by 276
Neuronal death/survival signaling pathways in cerebral ischemia
Sugawara, T., Fujimura, M., Noshita, N., Kim, G. W., Saito, A., Hayashi, T., Narasimhan, P., Maier, C. M., & Chan, P. H. (2004) · NeuroRX · doi:10.1602/neurorx.1.1.17 · Cited by 270
Reactive Oxygen Species as Mediators of Signal Transduction in Cardiovascular Disease
Abe, J.-I., & Berk, B. C. (1998) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(97)00133-3 · Cited by 260
Targeting of p38 Mitogen-Activated Protein Kinases to MEF2 Transcription Factors
Yang, S.-H., Galanis, A., & Sharrocks, A. D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4028 · Cited by 244
Requirement of the JIP1 scaffold protein for stress-induced JNK activation
Whitmarsh, A. J., Kuan, C.-Y., Kennedy, N. J., Kelkar, N., Haydar, T. F., Mordes, J. P., Appel, M., Rossini, A. A., Jones, S. N., Flavell, R. A., et al. (2001) · Genes & Development · doi:10.1101/gad.922801 · Cited by 238
Self-citationSignaling mechanisms in skeletal muscle: acute responses and chronic adaptations to exercise
Röckl, K. S. C., Witczak, C. A., & Goodyear, L. J. (2008) · IUBMB Life · doi:10.1002/iub.21 · Cited by 222
Nagata, Y., & Todokoro, K. (1999) · Blood · doi:10.1182/blood.v94.3.853.415a12_853_863 · Cited by 218
Vereker, E., O'Donnell, E., & Lynch, M. A. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-18-06811.2000 · Cited by 214
Zhao, Q., Shepherd, E. G., Manson, M. E., Nelin, L. D., Sorokin, A., & Liu, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411760200 · Cited by 207
Kikuchi, M., Tenneti, L., & Lipton, S. A. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-13-05037.2000 · Cited by 197
LPS and TNFα induce SOCS3 mRNA and inhibit IL‐6‐induced activation of STAT3 in macrophages
Bode, J. G., Nimmesgern, A., Schmitz, J., Schaper, F., Schmitt, M., Frisch, W., Häussinger, D., Heinrich, P. C., & Graeve, L. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01662-2 · Cited by 196
Giovannini, M. G., Scali, C., Prosperi, C., Bellucci, A., Vannucchi, M. G., Rosi, S., Pepeu, G., & Casamenti, F. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0538 · Cited by 190
Sheng, J. G., Jones, R. A., Zhou, X. Q., McGinness, J. M., Van Eldik, L. J., Mrak, R. E., & Griffin, W. S. T. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(01)00041-9 · Cited by 176
López-Camarillo, C., Aréchaga Ocampo, E., López Casamichana, M., Pérez-Plasencia, C., Álvarez-Sánchez, E., & Marchat, L. A. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms13010142 · Cited by 165
Hashimoto, S., Gon, Y., Takeshita, I., Maruoka, S., & Horie, T. (2001) · Journal of Allergy and Clinical Immunology · doi:10.1067/mai.2001.114702 · Cited by 151
Coogan, A. N., O'Neill, L. A. J., & O'Connor, J. J. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00100-1 · Cited by 129
Wang, X., Wu, H., & Miller, A. H. (2004) · Molecular Psychiatry · doi:10.1038/sj.mp.4001339 · Cited by 128
Yokota, T., & Wang, Y. (2016) · Gene · doi:10.1016/j.gene.2015.09.030 · Cited by 127
Caffrey, D. R., O'Neill, L. A. J., & Shields, D. C. (1999) · Journal of Molecular Evolution · doi:10.1007/pl00006578 · Cited by 124
Carter, A. B., & Hunninghake, G. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003599200 · Cited by 119
De Cesaris, P., Starace, D., Riccioli, A., Padula, F., Filippini, A., & Ziparo, E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7566 · Cited by 116
IL-1 and TNF-induced bone resorption is mediated by p38 mitogen activated protein kinase.
Kumar, S., Votta, B. J., Rieman, D. J., Badger, A. M., Gowen, M., & Lee, J. C. (2001) · Journal of Cellular Physiology · doi:10.1002/jcp.1082 · Cited by 107
The response of c-Jun/AP-1 to chronic hypoxia is hypoxia-inducible factor 1α dependent
Laderoute, K. R., Calaoagan, J. M., Gustafson-Brown, C., Knapp, A. M., Li, G.-C., Mendonca, H. L., Ryan, H. E., Wang, Z., & Johnson, R. S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.8.2515-2523.2002 · Cited by 105
Hypochlorous Acid Stimulation of the Mitogen-Activated Protein Kinase Pathway Enhances Cell Survival
Midwinter, R. G., Vissers, M. C. M., & Winterbourn, C. C. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2530 · Cited by 90
COLOGNATO, R., LAURENZA, I., FONTANA, I., COPPEDE, F., SICILIANO, G., COECKE, S., ARUOMA, O., BENZI, L., & MIGLIORE, L. (2006) · Clinical Nutrition · doi:10.1016/j.clnu.2005.10.005 · Cited by 81
Lisnock, J., Griffin, P., Calaycay, J., Frantz, B., Parsons, J., O'Keefe, S. J., & LoGrasso, P. (2000) · Biochemistry · doi:10.1021/bi992410+ · Cited by 79
Shimizu, T., Kato, T., Tachibana, A., & Sasaki, M. S. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4582 · Cited by 73
Dynamic Regulation of Proinflammatory Cytokines
Watkins, L. R., Nguyen, K. T., Lee, J. E., & Maier, S. F. (1999) · Advances in Experimental Medicine and Biology · doi:10.1007/978-0-585-37970-8_10 · Cited by 67
Lanna, A., Coutavas, E., Levati, L., Seidel, J., Rustin, M. H. A., Henson, S. M., Akbar, A. N., & Franzese, O. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301409 · Cited by 62
Onyango, I. G., Bennett, J. P., & Tuttle, J. B. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.01.026 · Cited by 56
Contribution of mitogen-activated protein kinases to NMDA-induced neurotoxicity in the rat retina
Munemasa, Y., Ohtani-kaneko, R., Kitaoka, Y., Kuribayashi, K., Isenoumi, K., Kogo, J., Yamashita, K., Kumai, T., Kobayashi, S., Hirata, K., et al. (2005) · Brain Research · doi:10.1016/j.brainres.2005.03.014 · Cited by 52
Zhuang, Z.-H., Zhou, Y., Yu, M.-C., Silverman, N., & Ge, B.-X. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2005.05.013 · Cited by 45
Shin, S. M., Baek, E. J., Kim, K. H., Kim, K. J., & Park, E. J. (2023) · Molecular Medicine Reports · doi:10.3892/mmr.2023.13035 · Cited by 45
Mathiasen, D. P., Egebjerg, C., Andersen, S. H., Rafn, B., Puustinen, P., Khanna, A., Daugaard, M., Valo, E., Tuomela, S., Bøttzauw, T., et al. (2012) · Oncogene · doi:10.1038/onc.2011.230 · Cited by 44
Thompson, D. A., Zacny, V., Belinsky, G. S., Classon, M., Jones, D. L., Schlegel, R., & Münger, K. (2001) · Oncogene · doi:10.1038/sj.onc.1204483 · Cited by 44
Matsuzaki, T., Aisaki, K.-I., Yamamura, Y., Noda, M., & Ikawa, Y. (2000) · Oncogene · doi:10.1038/sj.onc.1203461 · Cited by 40
Gao, F., Li, F., Miao, Y., Xu, L.-J., Zhao, Y., Li, Q., Zhang, S.-H., Wu, J., Sun, X.-H., & Wang, Z. (2017) · Scientific Reports · doi:10.1038/s41598-017-01557-y · Cited by 34
Ehyai, S., Dionyssiou, M. G., Gordon, J. W., Williams, D., Siu, K. W. M., & McDermott, J. C. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00832-15 · Cited by 32
Rouget, R., Auclair, Y., Loignon, M., Affar, E. B., & Drobetsky, E. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706257200 · Cited by 30
Sugiura, H., Tanaka, H., Yasuda, S., Takemiya, T., & Yamagata, K. (2009) · The Neuroscientist · doi:10.1177/1073858408324024 · Cited by 27
Irnaten, M., Duff, A., Clark, A., & O’Brien, C. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm10010062 · Cited by 27
Van Proeyen, K., De Bock, K., & Hespel, P. (2011) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1753-7 · Cited by 24
COL1A2 is a TBX3 target that mediates its impact on fibrosarcoma and chondrosarcoma cell migration
Omar, R., Cooper, A., Maranyane, H. M., Zerbini, L., & Prince, S. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.06.004 · Cited by 21
Molecular characterization of a zebrafish TCF ETS-domain transcription factor
Brown, L. A., Yang, S.-H., Hair, A., Galanis, A., & Sharrocks, A. D. (1999) · Oncogene · doi:10.1038/sj.onc.1203197 · Cited by 10
Metadata
- Authors
- Raingeaud, J., Gupta, S., Rogers, J. S., Dickens, M., Han, J., Ulevitch, R. J., & Davis, R. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-03
- Volume
- 270
- Issue
- 13
- Pages
- 7420-7426
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2007986629
- Cited by
- 2,241
- References
- 5
- FWCI
- 43.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
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