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Volumn 186, Issue 4, 2011, Pages 1951-1962

Critical role of IRF-8 in negative regulation of TLR3 expression by Src homology 2 domain-containing protein tyrosine phosphatase-2 activity in human myeloid dendritic cells

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE 3; INTERFERON CONSENSUS SEQUENCE BINDING PROTEIN; INTERFERON REGULATORY FACTOR 1; POLYINOSINIC POLYCYTIDYLIC ACID; PROTEIN TYROSINE PHOSPHATASE SHP 2; TOLL LIKE RECEPTOR 3;

EID: 79951837401     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1000918     Document Type: Article
Times cited : (28)

References (42)
  • 1
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • DOI 10.1016/j.cell.2006.02.015, PII S0092867406001905
    • Akira, S., S. Uematsu, and O. Takeuchi. 2006. Pathogen recognition and innate immunity. Cell 124: 783-801. (Pubitemid 43261452)
    • (2006) Cell , vol.124 , Issue.4 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 2
    • 35349016235 scopus 로고    scopus 로고
    • Recognition of microorganisms and activation of the immune response
    • DOI 10.1038/nature06246, PII NATURE06246
    • Medzhitov, R. 2007. Recognition of microorganisms and activation of the immune response. Nature 449: 819-826. (Pubitemid 47598622)
    • (2007) Nature , vol.449 , Issue.7164 , pp. 819-826
    • Medzhitov, R.1
  • 3
    • 33748455338 scopus 로고    scopus 로고
    • Type I Interferons in Host Defense
    • DOI 10.1016/j.immuni.2006.08.007, PII S107476130600392X
    • Stetson, D. B., and R. Medzhitov. 2006. Type I interferons in host defense. Immunity 25: 373-381. (Pubitemid 44354218)
    • (2006) Immunity , vol.25 , Issue.3 , pp. 373-381
    • Stetson, D.B.1    Medzhitov, R.2
  • 4
    • 41349102954 scopus 로고    scopus 로고
    • TLR3: Interferon induction by double-stranded RNA including poly(I:C)
    • Matsumoto, M., and T. Seya. 2008. TLR3: interferon induction by double-stranded RNA including poly(I:C). Adv. Drug Deliv. Rev. 60: 805-812.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 805-812
    • Matsumoto, M.1    Seya, T.2
  • 5
    • 68849085894 scopus 로고    scopus 로고
    • A cell biological view of Toll-like receptor function: Regulation through compartmentalization
    • Barton, G. M., and J. C. Kagan. 2009. A cell biological view of Toll-like receptor function: regulation through compartmentalization. Nat. Rev. Immunol. 9: 535-542.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 535-542
    • Barton, G.M.1    Kagan, J.C.2
  • 6
    • 77955557963 scopus 로고    scopus 로고
    • Toll-like receptor expression and function in human dendritic cell subsets: Implications for dendritic cell-based anti-cancer immunotherapy
    • Schreibelt, G., J. Tel, K. H. Sliepen, D. Benitez-Ribas, C. G. Figdor, G. J. Adema, and I. J. de Vries. 2010. Toll-like receptor expression and function in human dendritic cell subsets: implications for dendritic cell-based anti-cancer immunotherapy. Cancer Immunol. Immunother. 59: 1573-1582.
    • (2010) Cancer Immunol. Immunother. , vol.59 , pp. 1573-1582
    • Schreibelt, G.1    Tel, J.2    Sliepen, K.H.3    Benitez-Ribas, D.4    Figdor, C.G.5    Adema, G.J.6    De Vries, I.J.7
  • 8
    • 18844415594 scopus 로고    scopus 로고
    • Viral immunity: Cross-priming with the help of TLR3
    • Salio, M., and V. Cerundolo. 2005. Viral immunity: cross-priming with the help of TLR3. Curr. Biol. 15: R336-R339.
    • (2005) Curr. Biol. , vol.15
    • Salio, M.1    Cerundolo, V.2
  • 9
    • 62649124147 scopus 로고    scopus 로고
    • Negative regulation of Toll-like receptor signaling pathway
    • Wang, J., Y. Hu, W. W. Deng, and B. Sun. 2009. Negative regulation of Toll-like receptor signaling pathway. Microbes Infect. 11: 321-327.
    • (2009) Microbes Infect. , vol.11 , pp. 321-327
    • Wang, J.1    Hu, Y.2    Deng, W.W.3    Sun, B.4
  • 10
    • 0036679732 scopus 로고    scopus 로고
    • Of mice and men: Species variations of Toll-like receptor expression
    • DOI 10.1016/S1471-4906(02)02259-7, PII S1471490602022597
    • Rehli, M. 2002. Of mice and men: species variations of Toll-like receptor expression. Trends Immunol. 23: 375-378. (Pubitemid 34804626)
    • (2002) Trends in Immunology , vol.23 , Issue.8 , pp. 375-378
    • Rehli, M.1
  • 13
    • 26844577143 scopus 로고    scopus 로고
    • Increased expression of TLR3 in lymph nodes during simian immunodeficiency virus infection: Implications for inflammation and immunodeficiency
    • Sanghavi, S. K., and T. A. Reinhart. 2005. Increased expression of TLR3 in lymph nodes during simian immunodeficiency virus infection: implications for inflammation and immunodeficiency. J. Immunol. 175: 5314-5323.
    • (2005) J. Immunol. , vol.175 , pp. 5314-5323
    • Sanghavi, S.K.1    Reinhart, T.A.2
  • 14
    • 14044267522 scopus 로고    scopus 로고
    • Involvement of toll-like receptor 3 in the immune response of lung epithelial cells to double-stranded RNA and influenza A virus
    • Guillot, L., R. Le Goffic, S. Bloch, N. Escriou, S. Akira, M. Chignard, and M. Si-Tahar. 2005. Involvement of toll-like receptor 3 in the immune response of lung epithelial cells to double-stranded RNA and influenza A virus. J. Biol. Chem. 280: 5571-5580.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5571-5580
    • Guillot, L.1    Le Goffic, R.2    Bloch, S.3    Escriou, N.4    Akira, S.5    Chignard, M.6    Si-Tahar, M.7
  • 15
    • 42649114059 scopus 로고    scopus 로고
    • The IRF family transcription factors in immunity and oncogenesis
    • Tamura, T., H. Yanai, D. Savitsky, and T. Taniguchi. 2008. The IRF family transcription factors in immunity and oncogenesis. Annu. Rev. Immunol. 26: 535-584.
    • (2008) Annu. Rev. Immunol. , vol.26 , pp. 535-584
    • Tamura, T.1    Yanai, H.2    Savitsky, D.3    Taniguchi, T.4
  • 16
    • 0037011021 scopus 로고    scopus 로고
    • ICSBP is essential for the development of mouse type I interferon-producing cells and for the generation and activation of CD8alpha(+) dendritic cells
    • Schiavoni, G., F. Mattei, P. Sestili, P. Borghi, M. Venditti, H. C. Morse, III, F. Belardelli, and L. Gabriele. 2002. ICSBP is essential for the development of mouse type I interferon-producing cells and for the generation and activation of CD8alpha(+) dendritic cells. J. Exp. Med. 196: 1415-1425.
    • (2002) J. Exp. Med. , vol.196 , pp. 1415-1425
    • Schiavoni, G.1    Mattei, F.2    Sestili, P.3    Borghi, P.4    Venditti, M.5    Morse III, H.C.6    Belardelli, F.7    Gabriele, L.8
  • 22
    • 0036178254 scopus 로고    scopus 로고
    • ICSBP/IRF-8: Its regulatory roles in the development of myeloid cells
    • DOI 10.1089/107999002753452755
    • Tamura, T., and K. Ozato. 2002. ICSBP/IRF-8: its regulatory roles in the development of myeloid cells. J. Interferon Cytokine Res. 22: 145-152. (Pubitemid 34161292)
    • (2002) Journal of Interferon and Cytokine Research , vol.22 , Issue.1 , pp. 145-152
    • Tamura, T.1    Ozato, K.2
  • 23
    • 0035851121 scopus 로고    scopus 로고
    • SHP1 protein-tyrosine phosphatase inhibits gp91PHOX and p67PHOX expression by inhibiting interaction of PU.1, IRF1, interferon consensus sequence-binding protein, and CREB-binding protein with homologous Cis elements in the CYBB and NCF2 genes
    • Kautz, B., R. Kakar, E. David, and E. A. Eklund. 2001. SHP1 protein-tyrosine phosphatase inhibits gp91PHOX and p67PHOX expression by inhibiting interaction of PU.1, IRF1, interferon consensus sequence-binding protein, and CREB-binding protein with homologous Cis elements in the CYBB and NCF2 genes. J. Biol. Chem. 276: 37868-37878.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37868-37878
    • Kautz, B.1    Kakar, R.2    David, E.3    Eklund, E.A.4
  • 24
    • 34250320958 scopus 로고    scopus 로고
    • PU.1, interferon regulatory factor (IRF) 2, and the interferon consensus sequence-binding protein (ICSBP/ IRF8) cooperate to activate NF1 transcription in differentiating myeloid cells
    • Huang, W., E. Horvath, and E. A. Eklund. 2007. PU.1, interferon regulatory factor (IRF) 2, and the interferon consensus sequence-binding protein (ICSBP/ IRF8) cooperate to activate NF1 transcription in differentiating myeloid cells. J. Biol. Chem. 282: 6629-6643.
    • (2007) J. Biol. Chem. , vol.282 , pp. 6629-6643
    • Huang, W.1    Horvath, E.2    Eklund, E.A.3
  • 26
    • 0032762860 scopus 로고    scopus 로고
    • Interferon consensus sequence binding protein and interferon regulatory factor-4/Pip form a complex that represses the expression of the interferon-stimulated gene-15 in macrophages
    • Rosenbauer, F., J. F. Waring, J. Foerster, M. Wietstruk, D. Philipp, and I. Horak. 1999. Interferon consensus sequence binding protein and interferon regulatory factor-4/Pip form a complex that represses the expression of the interferon-stimulated gene-15 in macrophages. Blood 94: 4274-4281.
    • (1999) Blood , vol.94 , pp. 4274-4281
    • Rosenbauer, F.1    Waring, J.F.2    Foerster, J.3    Wietstruk, M.4    Philipp, D.5    Horak, I.6
  • 27
    • 43149090541 scopus 로고    scopus 로고
    • The interferon consensus sequence-binding protein (ICSBP/IRF8) represses PTPN13 gene transcription in differentiating myeloid cells
    • Huang,W., C. Zhu, H.Wang, E. Horvath, and E. A. Eklund. 2008. The interferon consensus sequence-binding protein (ICSBP/IRF8) represses PTPN13 gene transcription in differentiating myeloid cells. J. Biol. Chem. 283: 7921-7935.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7921-7935
    • Huang, W.1    Zhu, C.2    Wang, H.3    Horvath, E.4    Eklund, E.A.5
  • 28
    • 40549094646 scopus 로고    scopus 로고
    • Constitutive activation of SHP2 in mice cooperates with ICSBP deficiency to accelerate progression to acute myeloid leukemia
    • Konieczna, I., E. Horvath, H. Wang, S. Lindsey, G. Saberwal, L. Bei, W. Huang, L. Platanias, and E. A. Eklund. 2008. Constitutive activation of SHP2 in mice cooperates with ICSBP deficiency to accelerate progression to acute myeloid leukemia. J. Clin. Invest. 118: 853-867.
    • (2008) J. Clin. Invest. , vol.118 , pp. 853-867
    • Konieczna, I.1    Horvath, E.2    Wang, H.3    Lindsey, S.4    Saberwal, G.5    Bei, L.6    Huang, W.7    Platanias, L.8    Eklund, E.A.9
  • 29
    • 0030899516 scopus 로고    scopus 로고
    • Phosphorylation events modulate the ability of interferon consensus sequence binding protein to interact with interferon regulatory factors and to bind DNA
    • Sharf, R., D. Meraro, A. Azriel, A. M. Thornton, K. Ozato, E. F. Petricoin, A. C. Larner, F. Schaper, H. Hauser, and B. Z. Levi. 1997. Phosphorylation events modulate the ability of interferon consensus sequence binding protein to interact with interferon regulatory factors and to bind DNA. J. Biol. Chem. 272: 9785-9792.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9785-9792
    • Sharf, R.1    Meraro, D.2    Azriel, A.3    Thornton, A.M.4    Ozato, K.5    Petricoin, E.F.6    Larner, A.C.7    Schaper, F.8    Hauser, H.9    Levi, B.Z.10
  • 30
    • 38349004658 scopus 로고    scopus 로고
    • The molecular functions of Shp2 in the Ras/Mitogen-activated protein kinase (ERK1/2) pathway
    • Dance, M., A. Montagner, J. P. Salles, A. Yart, and P. Raynal. 2008. The molecular functions of Shp2 in the Ras/Mitogen-activated protein kinase (ERK1/2) pathway. Cell. Signal. 20: 453-459.
    • (2008) Cell. Signal. , vol.20 , pp. 453-459
    • Dance, M.1    Montagner, A.2    Salles, J.P.3    Yart, A.4    Raynal, P.5
  • 31
    • 33845438110 scopus 로고    scopus 로고
    • SHP-2 Phosphatase Negatively Regulates the TRIF Adaptor Protein-Dependent Type I Interferon and Proinflammatory Cytokine Production
    • DOI 10.1016/j.immuni.2006.10.014, PII S1074761306005127
    • An, H., W. Zhao, J. Hou, Y. Zhang, Y. Xie, Y. Zheng, H. Xu, C. Qian, J. Zhou, Y. Yu, et al. 2006. SHP-2 phosphatase negatively regulates the TRIF adaptor protein-dependent type I interferon and proinflammatory cytokine production. Immunity 25: 919-928. (Pubitemid 44894946)
    • (2006) Immunity , vol.25 , Issue.6 , pp. 919-928
    • An, H.1    Zhao, W.2    Hou, J.3    Zhang, Y.4    Xie, Y.5    Zheng, Y.6    Xu, H.7    Qian, C.8    Zhou, J.9    Yu, Y.10    Liu, S.11    Feng, G.12    Cao, X.13
  • 32
    • 33747788689 scopus 로고    scopus 로고
    • Leukemia-associated, constitutively active mutants of SHP2 protein tyrosine phosphatase inhibit NF1 transcriptional activation by the interferon consensus sequence binding protein
    • Huang, W., G. Saberwal, E. Horvath, C. Zhu, S. Lindsey, and E. A. Eklund. 2006. Leukemia-associated, constitutively active mutants of SHP2 protein tyrosine phosphatase inhibit NF1 transcriptional activation by the interferon consensus sequence binding protein. Mol. Cell. Biol. 26: 6311-6332.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 6311-6332
    • Huang, W.1    Saberwal, G.2    Horvath, E.3    Zhu, C.4    Lindsey, S.5    Eklund, E.A.6
  • 36
    • 0034235928 scopus 로고    scopus 로고
    • An IFN-gamma-inducible transcription factor, IFN consensus sequence binding protein (ICSBP), stimulates IL-12 p40 expression in macrophages
    • Wang, I. M., C. Contursi, A. Masumi, X. Ma, G. Trinchieri, and K. Ozato. 2000. An IFN-gamma-inducible transcription factor, IFN consensus sequence binding protein (ICSBP), stimulates IL-12 p40 expression in macrophages. J. Immunol. 165: 271-279. (Pubitemid 30429516)
    • (2000) Journal of Immunology , vol.165 , Issue.1 , pp. 271-279
    • Wang, I.-M.1    Contursi, C.2    Masumi, A.3    Ma, X.4    Trinchieri, G.5    Ozato, K.6
  • 39
    • 0037032471 scopus 로고    scopus 로고
    • IRF-8/ICSBP and IRF-1 cooperatively stimulate mouse IL-12 promoter activity in macrophages
    • DOI 10.1016/S0014-5793(02)03556-1, PII S0014579302035561
    • Masumi, A., S. Tamaoki, I. M. Wang, K. Ozato, and K. Komuro. 2002. IRF-8/ ICSBP and IRF-1 cooperatively stimulate mouse IL-12 promoter activity in macrophages. FEBS Lett. 531: 348-353. (Pubitemid 35341222)
    • (2002) FEBS Letters , vol.531 , Issue.2 , pp. 348-353
    • Masumi, A.1    Tamaoki, S.2    Wang, I.-M.3    Ozato, K.4    Komuro, K.5
  • 40
    • 28544437589 scopus 로고    scopus 로고
    • Characterization of two candidate genes, NCoA3 and IRF8, potentially involved in the control of HIV-1 latency
    • Munier, S., D. Delcroix-Genête, L. Carthagéna, A. Gumez, and U. Hazan. 2005. Characterization of two candidate genes, NCoA3 and IRF8, potentially involved in the control of HIV-1 latency. Retrovirology 2: 73.
    • (2005) Retrovirology , vol.2 , pp. 73
    • Munier, S.1    Delcroix-Genête, D.2    Carthagéna, L.3    Gumez, A.4    Hazan, U.5
  • 41
    • 67349262527 scopus 로고    scopus 로고
    • The extrinsic RNA-sensing pathway for adjuvant immunotherapy of cancer
    • Seya, T., and M. Matsumoto. 2009. The extrinsic RNA-sensing pathway for adjuvant immunotherapy of cancer. Cancer Immunol. Immunother. 58: 1175-1184.
    • (2009) Cancer Immunol. Immunother. , vol.58 , pp. 1175-1184
    • Seya, T.1    Matsumoto, M.2
  • 42
    • 70449717532 scopus 로고    scopus 로고
    • TLR3 ligand polyinosinic:polycytidylic acid induces IL-17A and IL-21 synthesis in human Th cells
    • Holm, C. K., C. C. Petersen, M. Hvid, L. Petersen, S. R. Paludan, B. Deleuran, and M. Hokland. 2009. TLR3 ligand polyinosinic:polycytidylic acid induces IL-17A and IL-21 synthesis in human Th cells. J. Immunol. 183: 4422-4431.
    • (2009) J. Immunol. , vol.183 , pp. 4422-4431
    • Holm, C.K.1    Petersen, C.C.2    Hvid, M.3    Petersen, L.4    Paludan, S.R.5    Deleuran, B.6    Hokland, M.7


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