Positive regulation of immune cell function and inflammatory responses by phosphatase PAC-1

Nature Immunology

Volumn 7, Issue 3, 2006, Pages 274-283

  Jeffrey, Kate L ^a   Brummer, Tilman ^a   Rolph, Michael S ^a,b   Liu, Sue M ^a,b   Callejas, Nuria A ^a   Grumont, Raelene J ^c   Gillieron, Corine ^d   Mackay, Fabienne ^a   Grey, Shane ^a   Camps, Montserrat ^d   Rommel, Christian ^d   Gerondakis, Steve D ^c   Mackay, Charles R ^a,b  

^a GARVAN INSTITUTE OF MEDICAL RESEARCH   (Australia)

^b Cooperative Research Centre for Asthma ^*  (Australia)

^c WALTER AND ELIZA HALL INSTITUTE OF MEDICAL RESEARCH   (Australia)

^d SERONO PHARMACEUTICAL RES INSTITUTE   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATASE; PHOSPHATASE OF ACTIVATED CELLS 1; PROTEIN KINASE; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR ELK 1; TRANSCRIPTION FACTOR NFAT; UNCLASSIFIED DRUG; MITOGEN ACTIVATED PROTEIN KINASE KINASE 4; PAC1 PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CELL ACTIVATION; CELL FUNCTION; CONTROLLED STUDY; EFFECTOR CELL; ENZYME ACTIVITY; GENETIC CODE; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; IMMUNOCOMPETENT CELL; IMMUNOREGULATION; INFLAMMATION; INFLAMMATORY CELL; LEUKOCYTE; MICROARRAY ANALYSIS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEFICIENCY; RHEUMATOID ARTHRITIS; ANIMAL; ARTHRITIS; GENE EXPRESSION; GENE EXPRESSION PROFILING; IMMUNOLOGY; METABOLISM; POLYMERASE CHAIN REACTION; SIGNAL TRANSDUCTION;

ANIMALS; ARTHRITIS, EXPERIMENTAL; GENE EXPRESSION; GENE EXPRESSION PROFILING; HUMANS; INFLAMMATION; LEUKOCYTES; MAP KINASE KINASE 4; MICE; MITOGEN-ACTIVATED PROTEIN KINASES; POLYMERASE CHAIN REACTION; PROTEIN-TYROSINE-PHOSPHATASE; RECEPTOR CROSS-TALK; RESEARCH SUPPORT, NON-U.S. GOV'T;

EID: 33646192473     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni1310     Document Type: Article

References (53)

1. Dong, C., Davis, R.J. & Flavell, R.A. MAP kinases in the immune response. Annu. Rev. Immunol. 20, 55-72 (2002).
2. Chang, L. & Karin, M. Mammalian MAP kinase signalling cascades. Nature 410, 37-40 (2001).
3. Robinson, M.J. & Cobb, M.H. Mitogen-activated protein kinase pathways. Curr. Opin. Cell Biol. 9, 180-186 (1997).
4. Mahtani, K.R. et al. Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor α mRNA stability. Mol. Cell. Biol. 21, 6461-6469 (2001).
5. Dumitru, C.D. et al. TNF-α induction by LPS is regulated posttranscriptionally via a Tpl2/ERK-dependent pathway. Cell 103, 1071-1083 (2000).
6. Camps, M., Nichols, A. & Arkinstall, S. Dual specificity phosphatases: A gene family for control of MAP kinase function. FASEB J. 14, 6-16 (2000).
7. Zhang, Y. et al. Regulation of innate and adaptive immune responses by MAP kinase phosphatase 5. Nature 430, 793-797 (2004).
8. Chu, Y., Solski, PA., Khosravi-Far, R., Der, C.J. & Kelly, K. The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation. J. Biol. Chem. 271, 6497-6501 (1996).
9. Ward, Y. et al. Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1. Nature 367, 651-654 (1994).
10. Karlsson, M., Mathers, J., Dickinson, R.J., Mandl, M. & Keyse, S.M. Both nuclear-cytoplasmic shuttling of the dual specificity phosphatase MKP-3 and its ability to anchor MAP kinase in the cytoplasm are mediated by a conserved nuclear export signal. J. Biol. Chem. 279, 41882-41891 (2004).
11. Masuda, K., Shima, H., Watanabe, M. & Kikuchi, K. MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein. J. Biol. Chem. 276, 39002-39011 (2001).
12. Theodosiou, A. & Ashworth, A. MAP kinase phosphatases. Genome Biol. 3, 3009.1-3009.10 (2002).
13. Keyse, S.M. Protein phosphatases and the regulation of mitogen-activated protein kinase signalling. Curr. Opin. Cell Biol. 12, 186-192 (2000).
14. Dorfman, K. et al. Disruption of the erp/mkp-1 gene does not affect mouse development: Normal MAP kinase activity in ERP/MKP-1-deficient fibroblasts. Oncogene 13, 925-931 (1996).
15. Zhao, Q. et al. 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. 280, 8101-8108 (2005).
16. Zhao, Q. et al. MAP kinase phosphatase 1 controls innate immune responses and suppresses endotoxic shock. J. Exp. Med. 203, 131-140 (2006).
17. Hammer, M. et al. Dual specificity phosphatase 1 (DUSP1) regulates a subset of LPS-induced genes and protects mice from lethal endotoxin shock. J. Exp. Med. 203, 15-20 (2006).
18. Christie, G.R. et al. The dual-specificity protein phosphatase DUSP9/ MKP-4 is essential for placental Function but is not required for normal embryonic development. Mol. Cell. Biol. 25, 8323-8333 (2005).
19. Rohan, PJ. et al. PAC-1: A mitogen-induced nuclear protein tyrosine phosphatase. Science 259, 1763-1766 (1993).
20. Grumont, R.J., Rasko, I.E., Strasser, A. & Gerondakis, S. Activation of the mitogen-activated protein kinase pathway induces transcription of the PAC-1 phosphatase gene. Mol. Cell. Biol. 16, 2913-2921 (1996).
21. Rohan, P.J. et al. PAC-1: A mitogen-induced nuclear protein tyrosine phosphatase. Science 259, 1763-1766 (1993).
22. Yin, Y., Liu, Y.X., Jin, Y.J., Hall, E.J. & Barrett, J.C. PAC1 phosphatase is a transcription target of p53 in signalling apoptosis and growth suppression. Nature 422, 527-531 (2003).
23. Kouskoff, V. et al. Organ-specific disease provoked by systemic autoimmunity. Cell 87, 811-822 (1996).
24. Lee, D.M. et al. Mast cells: A cellular link between autoantibodies and inflammatory arthritis. Science 297, 1689-1692 (2002).
25. Solomon, S., Rajasekaran, N., Jeisy-Walder, E., Snapper, S.B. & Illges, H. A crucial role for macrophages in the pathology of K/B × N serum-induced arthritis. Eur. J. Immunol. 35, 3064-3073 (2005).
26. Ji, H. et al. Arthritis critically dependent on innate immune system players. Immunity 16, 157-168 (2002).
27. Kouskoff, V. et al. Organ-specific disease provoked by sytemic autoimmunity. Cell 87, 811-822 (1996).
28. Farooq, A. et al. Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP. Structure (Camb) 11, 155-164 (2003).
29. Morita, S., Kojima, T. & Kitamura, T. Plat-E: An efficient and stable system for transient packaging of retroviruses. Gene Ther. 7, 1063-1066 (2000).
30. Pouyssegur, J. & Lenormand, P. Fidelity and spatio-temporal control in MAP kinase (ERKs) signalling. Eur. J. Biochem. 270, 3291-3299 (2003).
31. Franklin, C.C., Srikanth, S. & Kraft, A.S. Conditional expression of mitogen-activated protein kinase phosphatase-1, MKP-1, is cytoprotective against UV-induced apoptosis. Proc. Natl. Acad. Sci. USA 95, 3014-3019 (1998).
32. Saccani, S., Pantano, S. & Natoli, G. p38-Dependent marking of inflammatory genes for increased NF-κB recruitment. Nat. Immunol. 3, 69-75 (2002).
33. Frost, J.A. et al. Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins. EMBO J. 16, 6426-6438 (1997).
34. Avots, A. et al. CBP/p300 integrates Raf/Rac-signaling pathways in the transcriptional induction of NF-ATc during T cell activation. Immunity 10, 515-524 (1999).
35. Boise, L.H. et al. The NFAT-1 DNA binding complex in activated T cells contains Fra-1 and JunB. Mol. Cell. Biol. 13, 1911-1919 (1993).
36. Shen, Y.H. et al. Cross-talk between JNK/SAPK and ERK/MAPK pathways: sustained activation of JNK blocks ERK activation by mitogenic factors. J. Biol. Chem. 278, 26715-26721 (2003).
37. Tanoue, T., Yamamoto, T. & Nishida, E. Modular structure of a docking surface on MAPK phosphatases. J. Biol. Chem. 277, 22942-22949 (2002).
38. Firestein, G.S. Evolving concepts of rheumatoid arthritis. Nature 423, 356-361 (2003).
39. Ji, H. et al. Critical roles for interleukin 1 and tumor necrosis factor α in antibody-induced arthritis. J. Exp. Med. 196, 77-85 (2002).
40. Kohno, M., Yamasaki, S., Tybulewicz, V.L. & Saito, T. Rapid and large amount of autocrine IL-3 production is responsible for mast cell survival by IgE in the absence of antigen. Blood 105, 2059-2065 (2005).
41. Harada, H., Quearry, B., Ruiz-Vela, A. & Korsmeyer, S.J. Survival factor-induced extracellular signal-regulated kinase phosphorylates BIM, inhibiting its association with BAX and proapoptotic activity. Proc. Natl. Acad. Sci. USA 101, 15313-15317 (2004).
42. Kamata, H. et al. Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 120, 649-661 (2005).
43. 2-terminal kinase. Mol. Cell. Biol. 22, 4929-4942 (2002).
44. Xiao, Y.Q. et al. Cross-talk between ERK and p38 MAPK mediates selective suppression of pro-inflammatory cytokines by transforming growth factor-β. J. Biol. Chem. 277, 14884-14893 (2002).
45. Shen, Y. et al. Activation of the Jnk signaling pathway by a dual-specificity phosphatase, JSP-1. Proc. Natl. Acad. Sci. USA 98, 13613-13618 (2001).
46. Chen, A.J. et al. The dual specificity JKAP specifically activates the c-Jun N-terminal kinase pathway. J. Biol. Chem. 277, 36592-36601 (2002).
47. Chtanova, T. et al. T follicular helper cells express a distinctive transcriptional profile, reflecting their role as non-Th1/Th2 effector cells that provide help for B cells. J. Immunol. 173, 68-78 (2004).
48. McBurney, M.W. et al. The mouse xioa gene promoter contains an upstream activator sequence. Nucleic Acids Res. 19, 5755-5761 (1991).
49. Kontgen, F. & Stewart, C.L. Simple screening procedure to detect gene targeting events in embryonic stem cells. Methods Enzymol. 225, 878-890 (1993).
50. Ochi, H. et al. T helper cell type 2 cytokine-mediated comitogenic responses and CCR3 expression during differentiation of human mast cells in vitro. J. Exp. Med. 190, 267-280 (1999).
51. Irizarry, R.A. et al. Exploration, normalization, and summaries of high density oligonucleotide array probe level data. Biostatistics 4, 249-264 (2003).
52. Bowles, N.E., Eisensmith, R.C., Mohuiddin, R., Pyron, M. & Woo, S.L. A simple and efficient method for the concentration and purification of recombinant retrovirus for increased hepatocyte transduction in vivo. Hum. Gene Ther. 7, 1735-1742 (1996).
53. Durand, D.B. et al. Characterization of antigen receptor response elements within the interleukin-2 enhancer. Mol. Cell. Biol. 8, 1715-1724 (1988).