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A MAP Kinase Targeted by Endotoxin and Hyperosmolarity in Mammalian Cells

Han, J., Lee, J.-D., Bibbs, L., Ulevitch, R. J.·1994·Science

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Abstract

Mammalian cells respond to endotoxic lipopolysaccharide (LPS) by activation of protein kinase cascades that lead to new gene expression. A protein kinase, p38, that was tyrosine phosphorylated in response to LPS, was cloned. The p38 enzyme and the product of the Saccharomyces cerevisiae HOG1 gene, which are both members of the mitogen-activated protein (MAP) kinase family, have sequences at and adjacent to critical phosphorylation sites that distinguish these proteins from most other MAP kinase family members. Both HOG1 and p38 are tyrosine phosphorylated after extracellular changes in osmolarity. These findings link a signaling pathway in mammalian cells with a pathway in yeast that is responsive to physiological stress.

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Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J. (1994) · Nature · doi:10.1038/367704a0 · Cited by 592
Bacterial lipopolysaccharide induces tyrosine phosphorylation and activation of mitogen-activated protein kinases in macrophages.
Weinstein, S. L., Sanghera, J. S., Lemke, K., DeFranco, A. L., & Pelech, S. L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42133-3 · Cited by 396
Bacterial lipopolysaccharide stimulates protein tyrosine phosphorylation in macrophages.
Weinstein, S. L., Gold, M. R., & DeFranco, A. L. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.10.4148 · Cited by 311

Show all 3 references

Defective LPS Signaling in C3H/HeJ and C57BL/10ScCr Mice: Mutations in Tlr4 Gene
Poltorak, A., He, X., Smirnova, I., Liu, M.-Y., Huffel, C. V., Du, X., Birdwell, D., Alejos, E., Silva, M., Galanos, C., et al. (1998) · Science · doi:10.1126/science.282.5396.2085 · Cited by 7,631
Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
Marshall, C. J. (1995) · Cell · doi:10.1016/0092-8674(95)90401-8 · Cited by 3,906
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
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
Functional significance of cell volume regulatory mechanisms
LANG, F., BUSCH, G. L., RITTER, M., VÖLKL, H., WALDEGGER, S., GULBINS, E., & HÄUSSINGER, D. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.1.247 · Cited by 1,891
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-citation
Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways
Whitmarsh, A. J., & Davis, R. J. (1996) · Journal of Molecular Medicine · doi:10.1007/s001090050063 · Cited by 1,543
MAPK cascade signalling and synaptic plasticity
Thomas, G. M., & Huganir, R. L. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1346 · Cited by 1,454
Mitogen-activated protein kinases in apoptosis regulation
Wada, T., & Penninger, J. M. (2004) · Oncogene · doi:10.1038/sj.onc.1207556 · Cited by 1,432
Receptor-Dependent Mechanisms of Cell Stimulation by Bacterial Endotoxin
Ulevitch, R. J., & Tobias, P. S. (1995) · Annual Review of Immunology · doi:10.1146/annurev.iy.13.040195.002253 · Cited by 1,442
Self-citation
The small GTP-binding proteins Rac1 and Cdc42regulate the activity of the JNK/SAPK signaling pathway
Coso, O. A., Chiariello, M., Yu, J.-C., Teramoto, H., Crespo, P., Xu, N., Miki, T., & Silvio Gutkind, J. (1995) · Cell · doi:10.1016/s0092-8674(05)80018-2 · Cited by 1,397
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
Transcriptional Regulation by Extracellular signals: Mechanisms and Specificity
Hill, C. S., & Treisman, R. (1995) · Cell · doi:10.1016/0092-8674(95)90403-4 · Cited by 1,012
MAPKAP kinase 2 is essential for LPS-induced TNF-α biosynthesis
Kotlyarov, A., Neininger, A., Schubert, C., Eckert, R., Birchmeier, C., Volk, H.-D., & Gaestel, M. (1999) · Nature Cell Biology · doi:10.1038/10061 · Cited by 763
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
Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729
p38MAPK: stress responses from molecular mechanisms to therapeutics
Coulthard, L. R., White, D. E., Jones, D. L., McDermott, M. F., & Burchill, S. A. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.06.005 · Cited by 691
Diversity and versatility of p38 kinase signalling in health and disease
Canovas, B., & Nebreda, A. R. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00322-w · Cited by 657
The MAP kinase signaling cascades: a system of hundreds of components regulates a diverse array of physiological functions
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Ceppi, M., Pereira, P. M., Dunand-Sauthier, I., Barras, E., Reith, W., Santos, M. A., & Pierre, P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811073106 · Cited by 631
Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1
Zhang, 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
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Zhao, Q., Wang, X., Nelin, L. D., Yao, Y., Matta, R., Manson, M. E., Baliga, R. S., Meng, X., Smith, C. V., Bauer, J. A., et al. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20051794 · Cited by 370
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Shimizu, T., Kato, T., Tachibana, A., & Sasaki, M. S. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4582 · Cited by 73
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LIN, C., TSENG, H., HSIEH, H., LEE, C., WU, C., CHENG, C., & YANG, C. (2008) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2008.01.032 · Cited by 65
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Authors: Han, J., Lee, J.-D., Bibbs, L., & Ulevitch, R. J.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1994-08-05
Volume: 265
Issue: 5173
Pages: 808-811
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.7914033
OpenAlex: W2001399809
Cited by: 2,646
References: 3
FWCI: 51.72
Type: journal article
Language: en
Open access: closed

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A MAP Kinase Targeted by Endotoxin and Hyperosmolarity in Mammalian Cells

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