Mitogen-activated protein kinase phosphatase-1 (MKP-1): a critical regulator of innate immune responses

References

• Kyriakis JM, Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol Rev 2001; 81: 807–69
   PubMed Web of Science ®Google Scholar
• Keyse SM. Protein phosphatases and the regulation of mitogen-activated protein kinase signalling. Curr Opin Cell Biol 2000; 12: 186–92
   PubMed Web of Science ®Google Scholar
• Camps M, Nichols A, Arkinstall S. Dual specificity phosphatases: a gene family for control of MAP kinase function. FASEB J 2000; 14: 6–16
   PubMed Web of Science ®Google Scholar
• Farooq A, Zhou M-M. Structure and regulation of MAPK phosphatases. Cell Signalling 2004; 16: 769–79
   PubMed Web of Science ®Google Scholar
• Tonks NK. Protein tyrosine phosphatases: from genes, to function, to disease. Nat Rev Mol Cell Biol 2006; 7: 833–46
   PubMed Web of Science ®Google Scholar
• Keyse SM, Emslie EA. Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase. Nature 1992; 359: 644–7
   PubMed Web of Science ®Google Scholar
• Charles CH, Abler AS, Lau LF. cDNA sequence of a growth factor-inducible immediate early gene and characterization of its encoded protein. Oncogene 1992; 7: 187–90
   PubMed Web of Science ®Google Scholar
• Sun H, Charles CH, Lau LF, Tonks NK. MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 1993; 75: 487–93
   PubMed Web of Science ®Google Scholar
• Wu JJ, Zhang L, Bennett AM. The noncatalytic amino terminus of mitogen-activated protein kinase phosphatase 1 directs nuclear targeting and serum response element transcriptional regulation. Mol Cell Biol 2005; 25: 4792–803
   PubMed Web of Science ®Google Scholar
• Franklin CC, Kraft AS. Conditional expression of the mitogen-activated protein kinase (MAPK) phosphatase MKP-1 preferentially inhibits p38 MAPK and stress-activated protein kinase in U937 cells. J Biol Chem 1997; 272: 16917–23
   PubMed Web of Science ®Google Scholar
• Akira S, Uematsu S, Takeuchi O. Pathogen recognition and innate immunity. Cell 2006; 124: 783–801
   PubMed Web of Science ®Google Scholar
• Takeda K, Kaisho T, Akira S. Toll-like receptors. Ann Rev Immunol 2003; 21: 335–76
   PubMed Web of Science ®Google Scholar
• Iwasaki A, Medzhitov R. Toll-like receptor control of the adaptive immune responses. Nat Immunol 2004; 5: 987–95
   PubMed Web of Science ®Google Scholar
• Liew FY, Xu D, Brint EK, O'Neill LAJ. Negative regulation of toll-like receptor-mediated immune responses. Nat Rev Immunol 2005; 5: 446–58
   PubMed Web of Science ®Google Scholar
• Symons A, Beinke S, Ley SC. MAP kinase kinase kinases and innate immunity. Trends Immunol 2006; 27: 40–8
   PubMed Web of Science ®Google Scholar
• Dumitru CD, Ceci JD, Tsatsanis C, Kontoyiannis D, Stamatakis K, Lin JH, et al. TNF-alpha induction by LPS is regulated posttranscriptionally via a Tpl2/ERK-dependent pathway. Cell 2000; 103: 1071–83
   PubMed Web of Science ®Google Scholar
• Shim JH, Xiao C, Paschal AE, Bailey ST, Rao P, Hayden MS, et al. TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo. Genes Dev 2005; 19: 2668–81
   PubMed Web of Science ®Google Scholar
• Sato S, Sanjo H, Takeda K, Ninomiya-Tsuji J, Yamamoto M, Kawai T, et al. Essential function for the kinase TAK1 in innate and adaptive immune responses. Nat Immunol 2005; 6: 1087–95
   PubMed Web of Science ®Google Scholar
• Huang Q, Yang J, Lin Y, Walker C, Cheng J, Liu ZG, et al. Differential regulation of interleukin 1 receptor and Toll-like receptor signaling by MEKK3. Nat Immunol 2004; 5: 98–103
   PubMed Web of Science ®Google Scholar
• Matsuzawa A, Saegusa K, Noguchi T, Sadamitsu C, Nishitoh H, Nagai S, et al. ROS-dependent activation of the TRAF6-ASK1-p38 pathway is selectively required for TLR4-mediated innate immunity. Nat Immunol 2005; 6: 587–92
   PubMed Web of Science ®Google Scholar
• Ashwell JD. The many paths to p38 mitogen-activated protein kinase activation in the immune system. Nat Rev Immunol 2006; 6: 532–40
   PubMed Web of Science ®Google Scholar
• Zhang Y, Blattman JN, Kennedy NJ, Duong J, Nguyen T, Wang Y, et al. Regulation of innate and adaptive immune responses by MAP kinase phosphatase 5. Nature 2004; 430: 793–7
   PubMed Web of Science ®Google Scholar
• Jeffrey KL, Brummer T, Rolph MS, Liu SM, Callejas NA, Grumont RJ, et al. Positive regulation of immune cell function and inflammatory responses by phosphatase PAC-1. Nat Immunol 2006; 7: 274–83
   PubMed Web of Science ®Google Scholar
• Dorfman K, Carrasco D, Gruda M, Ryan C, Lira SA, Bravo R. Disruption of the erp/mkp-1 gene does not affect mouse development: normal MAP kinase activity in ERP/MKP-1-deficient fibroblasts. Oncogene 1996; 13: 925–31
   PubMed Web of Science ®Google Scholar
• Wu JJ, Bennett AM. Essential role for mitogen-activated protein (map) kinase phosphatase-1 in stress-responsive map kinase and cell survival signaling. J Biol Chem 2005; 280: 16461–6
   PubMed Web of Science ®Google Scholar
• Zhou JY, Liu Y, Wu GS. The role of mitogen-activated protein kinase phosphatase-1 in oxidative damage-induced cell death. Cancer Res 2006; 66: 4888–94
   PubMed Web of Science ®Google Scholar
• Wu JJ, Roth RJ, Anderson EJ, Hong EG, Lee MK, Choi CS, et al. Mice lacking MAP kinase phosphatase-1 have enhanced MAP kinase activity and resistance to diet-induced obesity. Cell Metab 2006; 4: 61–73
   PubMed Web of Science ®Google Scholar
• Chen P, Li J, Barnes J, Kokkonen GC, Lee JC, Liu Y. Restraint of proinflammatory cytokine biosynthesis by mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages. J Immunol 2002; 169: 6408–16
   PubMed Web of Science ®Google Scholar
• Zhao Q, Shepherd EG, Manson ME, Nelin LD, Sorokin A, Liu Y. The role of mitogen-activated protein kinase phosphatase-1 in the response of alveolar macrophages to lipopolysaccharide: attenuation of proinflammatory cytokine biosynthesis via feedback control of p38. J Biol Chem 2005; 280: 8101–8
   PubMed Web of Science ®Google Scholar
• Chi H, Barry SP, Roth RJ, Wu JJ, Jones EA, Bennett AM, et al. Dynamic regulation of pro- and anti-inflammatory cytokines by MAPK phosphatase 1 (MKP-1) in innate immune responses. Proc Natl Acad Sci U S A 2006; 103: 2274–9
   PubMed Web of Science ®Google Scholar
• Hammer M, Mages J, Dietrich H, Servatius A, Howells N, Cato AC, et al. Dual specificity phosphatase 1 (DUSP1) regulates a subset of LPS-induced genes and protects mice from lethal endotoxin shock. J Exp Med 2006; 203: 15–20
   PubMedGoogle Scholar
• Salojin KV, Owusu IB, Millerchip KA, Potter M, Platt KA, Oravecz T. Essential role of MAPK phosphatase-1 in the negative control of innate immune responses. J Immunol 2006; 176: 1899–907
   PubMed Web of Science ®Google Scholar
• Zhao Q, Wang X, Nelin LD, Yao Y, Matta R, Manson ME, et al. MAP kinase phosphatase 1 controls innate immune responses and suppresses endotoxic shock. J Exp Med 2006; 203: 131–40
   PubMed Web of Science ®Google Scholar
• Dong C, Davis RJ, Flavell RA. MAP kinases in immune response. Annu Rev Immunol 2002; 20: 55–72
   PubMed Web of Science ®Google Scholar
• Shepherd EG, Zhao Q, Welty SE, Hansen TN, Smith CV, Liu Y. The function of mitogen-activated protein kinase phosphatase-1 in peptidoglycan-stimulated macrophages. J Biol Chem 2004; 279: 54023–31
   Google Scholar
• Moore KW, de Waal Malefyt R, Coffman RL, O'Garra A. Interleukin-10 and the interleukin-10 receptor. Annu Rev Immunol 2001; 19: 683–765
   PubMed Web of Science ®Google Scholar
• Hacker H, Redecke V, Blagoev B, Kratchmarova I, Hsu LC, Wang GG, et al. Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6. Nature 2006; 439: 204–7
   PubMed Web of Science ®Google Scholar
• Ma W, Lim W, Gee K, Aucoin S, Nandan D, Kozlowski M, et al. The p38 mitogen-activated kinase pathway regulates the human interleukin-10 promoter via the activation of Sp1 transcription factor in lipopolysaccharide-stimulated human macrophages. J Biol Chem 2001; 276: 13664–74
   PubMed Web of Science ®Google Scholar
• Cross AS. Endotoxin tolerance—current concepts in historical perspective. J Endotoxin Res 2002; 8: 83–98
   PubMedGoogle Scholar
• Nimah M, Zhao B, Denenberg AG, Bueno O, Molkentin J, Wong HR, et al. Contribution of MKP-1 regulation of p38 to endotoxin tolerance. Shock 2005; 23: 80–7
   PubMed Web of Science ®Google Scholar
• Hu JH, Chen T, Zhuang ZH, Kong L, Yu MC, Liu Y, et al. Feedback control of MKP-1 expression by p38.Cell Signal 2006; Jul 25 [Epub ahead of print].
   Google Scholar
• Cohen J. The immunopathogenesis of sepsis. Nature 2002; 420: 885–91
   PubMed Web of Science ®Google Scholar
• Lopez-Bojorquez LN, Dehesa AZ, Reyes-Teran G. Molecular mechanisms involved in the pathogenesis of septic shock. Arch Med Res 2004; 35: 465–79
   Google Scholar
• Martin GS, Mannino DM, Eaton S, Moss M. The epidemiology of sepsis in the United States from 1979 through 2000. N Engl J Med 2003; 348: 1546–54
   PubMed Web of Science ®Google Scholar
• Brand DD, Kang AH, Rosloniec EF. Immunopathogenesis of collagen arthritis. Springer Semin Immunopathol 2003; 25: 3–18
   PubMed Web of Science ®Google Scholar
• Valledor AF, Xaus J, Comalada M, Soler C, Celada A. Protein kinase C epsilon is required for the induction of mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages. J Immunol 2000; 164: 29–37
   PubMedGoogle Scholar
• Sanchez-Tillo E, Comalada M, Farrera C, Valledor AF, Lloberas J, Celada A. Macrophage-colony-stimulating factor-induced proliferation and lipopolysaccharide-dependent activation of macrophages requires Raf-1 phosphorylation to induce mitogen kinase phosphatase-1 expression. J Immunol 2006; 176: 6594–602
   PubMed Web of Science ®Google Scholar
• Li J, Gorospe M, Hutter D, Barnes J, Keyse SM, Liu Y. Transcriptional induction of MKP-1 in response to stress is associated with histone H3 phosphorylation-acetylation. Mol Cell Biol 2001; 21: 8213–24
   PubMed Web of Science ®Google Scholar
• Brondello J-M, Pouyssegur J, McKenzie FR. Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation. Science 1999; 286: 2514–17
   PubMed Web of Science ®Google Scholar
• Lin YW, Chuang SM, Yang JL. ERK1/2 achieves sustained activation by stimulating MAPK phosphatase-1 degradation via the ubiquitin-proteasome pathway. J Biol Chem 2003; 278: 21534–41
   PubMed Web of Science ®Google Scholar
• De Waal Malefyt R, Abrams J, Bennett B, Figdor CG, de Vries JE. Interleukin 10(IL-10) inhibits cytokine synthesis by human monocytes: an autoregulatory role of IL-10 produced by monocytes. J Exp Med 1991; 174: 1209–20
   PubMed Web of Science ®Google Scholar
• Abraham SM, Lawrence T, Kleiman A, Warden P, Medghalchi M, Tuckermann J, et al. Antiinflammatory effects of dexamethasone are partly dependent on induction of dual specificity phosphatase 1. J Exp Med 2006; 203: 1883–9
   PubMed Web of Science ®Google Scholar
• Kassel O, Sancono A, Kratzschmar J, Kreft B, Stassen M, Cato ACB. Glucocorticoids inhibit MAP kinase via increased expression and decreased degradation of MKP-1. EMBO J 2001; 20: 7108–16
   PubMed Web of Science ®Google Scholar
• Lasa M, Abraham SM, Boucheron C, Saklatvala J, Clark AR. Dexamethasone causes sustained expression of mitogen-activated protein kinase (MAPK) phosphatase 1 and phosphatase-mediated inhibition of MAPK p38. Mol Cell Biol 2002; 22: 7802–11
   PubMed Web of Science ®Google Scholar
• Hammer M, Mages J, Dietrich H, Schmitz F, Striebel F, Murray PJ, et al. Control of dual-specificity phosphatase-1 expression in activated macrophages by IL-10. Eur J Immunol 2005; 35: 2991–3001
   PubMedGoogle Scholar
• Xiao YQ, Malcolm K, Worthen GS, Gardai S, Schiemann WP, Fadok VA, et al. Cross-talk between ERK and p38 MAPK mediates selective suppression of pro-inflammatory cytokines by transforming growth factor-beta. J Biol Chem 2002; 277: 14884–93
   PubMed Web of Science ®Google Scholar
• Eljaschewitsch E, Witting A, Mawrin C, Lee T, Schmidt PM, Wolf S, et al. The endocannabinoid anandamide protects neurons during CNS inflammation by induction of MKP-1 in microglial cells. Neuron 2006; 49: 67–79
   PubMed Web of Science ®Google Scholar
• Sanlorenzo L, Zhao B, Spight D, Denenberg AG, Page K, Wong HR, et al. Heat shock inhibition of lipopolysaccharide-mediated tumor necrosis factor expression is associated with nuclear induction of MKP-1 and inhibition of mitogen-activated protein kinase activation. Crit Care Med 2004; 32: 2284–92
   PubMed Web of Science ®Google Scholar
• Roger T, Chanson AL, Knaup-Reymond M, Calandra T. Macrophage migration inhibitory factor promotes innate immune responses by suppressing glucocorticoid-induced expression of mitogen-activated protein kinase phosphatase-1. Eur J Immunol 2005; 35: 3405–13
   PubMed Web of Science ®Google Scholar
• Shen YH, Godlewski J, Zhu J, Sathyanarayana P, Leaner V, Birrer MJ, et al. Cross-talk between JNK/SAPK and ERK/MAPK pathways: sustained activation of JNK blocks ERK activation by mitogenic factors. J Biol Chem 2003; 278: 26715–21
   PubMedGoogle Scholar
• Zhang H, Shi X, Hampong M, Blanis L, Pelech S. Stress-induced inhibition of ERK1 and ERK2 by direct interaction with p38 MAP kinase. J Biol Chem 2001; 276: 6905–8
   PubMedGoogle Scholar