메뉴 건너뛰기




Volumn 178, Issue 2, 2007, Pages 986-992

Identification of CXCL11 as a STAT3-dependent gene induced by IFN

Author keywords

[No Author keywords available]

Indexed keywords

CXCL11 CHEMOKINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON; INTERFERON REGULATORY FACTOR 1; INTERFERON REGULATORY FACTOR 2; PROTEIN P50; STAT3 PROTEIN; SYNAPTOTAGMIN I; TYROSINE;

EID: 33846213580     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.178.2.986     Document Type: Article
Times cited : (43)

References (39)
  • 2
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell, J. E. J., I. M. Kerr, and G. R. Stark. 1994. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 264: 1415-1421.
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell, J.E.J.1    Kerr, I.M.2    Stark, G.R.3
  • 3
    • 0030999696 scopus 로고    scopus 로고
    • STAT3 as an adapter to couple phosphatidylinositol-3 kinase to the IFNAR-1 chain of the type I IFN receptor
    • Pfeffer, L. M., J. E. Mullersman, S. R. Pfeffer, A. Murti, W. Shi, and C. H. Yang. 1997. STAT3 as an adapter to couple phosphatidylinositol-3 kinase to the IFNAR-1 chain of the type I IFN receptor. Science 276: 1418-1420.
    • (1997) Science , vol.276 , pp. 1418-1420
    • Pfeffer, L.M.1    Mullersman, J.E.2    Pfeffer, S.R.3    Murti, A.4    Shi, W.5    Yang, C.H.6
  • 4
    • 0032510805 scopus 로고    scopus 로고
    • STAT3 complements defects in an interferon-resistant cell line: Evidence for an essential role for STAT3 in interferon signaling and biological activities
    • Yang, C. H., A. Murti, and L. M. Pfeffer. 1998. STAT3 complements defects in an interferon-resistant cell line: evidence for an essential role for STAT3 in interferon signaling and biological activities. Proc. Natl. Acad. Sci. USA 95: 5568-5572.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5568-5572
    • Yang, C.H.1    Murti, A.2    Pfeffer, L.M.3
  • 6
    • 0029960028 scopus 로고    scopus 로고
    • Dominant negative stat3 mutant inhibits interleukin-6-induced Jak-STAT signal transduction
    • Kaptein, A., V. Paillard, and M. Saunders. 1996. Dominant negative stat3 mutant inhibits interleukin-6-induced Jak-STAT signal transduction. J. Biol. Chem. 271: 5961-5964.
    • (1996) J. Biol. Chem , vol.271 , pp. 5961-5964
    • Kaptein, A.1    Paillard, V.2    Saunders, M.3
  • 7
    • 0028107016 scopus 로고
    • The role of the interferon α/β receptor chain 1 in the structure and transmembrane signaling of the interferon α/β receptor complex
    • Constantinescu, S. N., E. Croze, C. Wang, A. Murti, L. Basu, J. E. Mullersman, and L. M. Pfeffer. 1994. The role of the interferon α/β receptor chain 1 in the structure and transmembrane signaling of the interferon α/β receptor complex. Proc. Natl. Acad. Sci. USA 91: 9602-9606.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9602-9606
    • Constantinescu, S.N.1    Croze, E.2    Wang, C.3    Murti, A.4    Basu, L.5    Mullersman, J.E.6    Pfeffer, L.M.7
  • 8
    • 0025883716 scopus 로고
    • Transmembrane signaling by interferon α involves diacylglycerol production and activation of the ε isoform of protein kinase C in Daudi cells
    • Pfeffer, L. M., B. L. Eisenkraft, N. C. Reich, T. Improta, G. Baxter, S. Daniel-Issakani, and B. Strulovici. 1991. Transmembrane signaling by interferon α involves diacylglycerol production and activation of the ε isoform of protein kinase C in Daudi cells. Proc. Natl. Acad. SCi. USA 88: 7988-7992.
    • (1991) Proc. Natl. Acad. SCi. USA , vol.88 , pp. 7988-7992
    • Pfeffer, L.M.1    Eisenkraft, B.L.2    Reich, N.C.3    Improta, T.4    Baxter, G.5    Daniel-Issakani, S.6    Strulovici, B.7
  • 9
    • 0023236357 scopus 로고
    • Cytoskeletal association of human α-interferon-receptor complexes in interferon-sensitive and -resistant lymphoblastoid cells
    • Pfeffer, L. M., N. Stebbing, and D. B. Donner. 1987. Cytoskeletal association of human α-interferon-receptor complexes in interferon-sensitive and -resistant lymphoblastoid cells. Proc. Natl. Acad. Sci. USA 84: 3249-3253.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3249-3253
    • Pfeffer, L.M.1    Stebbing, N.2    Donner, D.B.3
  • 10
    • 0025356871 scopus 로고
    • The down-regulation of α-interferon receptors in human lymphoblastoid cells: Relation to cellular responsiveness to the antiproliferative action of α-interferon
    • Pfeffer, L. M., and D. B. Donner. 1990. The down-regulation of α-interferon receptors in human lymphoblastoid cells: relation to cellular responsiveness to the antiproliferative action of α-interferon. Cancer Res. 50: 2654-2657.
    • (1990) Cancer Res , vol.50 , pp. 2654-2657
    • Pfeffer, L.M.1    Donner, D.B.2
  • 11
    • 0024221206 scopus 로고
    • Cells resistant to interferon are defective in activation of a promoter-binding factor
    • Kessler, D. S., R. Pine, L. M. Pfeffer, D. E. Levy, and J. E. J. Darnell. 1988. Cells resistant to interferon are defective in activation of a promoter-binding factor. EMBO J. 7: 3779-3783.
    • (1988) EMBO J , vol.7 , pp. 3779-3783
    • Kessler, D.S.1    Pine, R.2    Pfeffer, L.M.3    Levy, D.E.4    Darnell, J.E.J.5
  • 14
    • 0023185543 scopus 로고
    • Interferon-α down-regulates insulin receptors in lymphoblastoid (Daudi) cells
    • Pfeffer, L. M., D. B. Donner, and I. Tamm. 1987. Interferon-α down-regulates insulin receptors in lymphoblastoid (Daudi) cells. J. Biol. Chem. 262: 3665-3670.
    • (1987) J. Biol. Chem , vol.262 , pp. 3665-3670
    • Pfeffer, L.M.1    Donner, D.B.2    Tamm, I.3
  • 15
    • 20444453281 scopus 로고    scopus 로고
    • A role of STAT3 in Rho GTPase-regulated cell migration and proliferation
    • Debidda, M., L. Wang, H. Zang, V. Poli, and Y. Zheng. 2005. A role of STAT3 in Rho GTPase-regulated cell migration and proliferation. J. Biol. Chem. 280: 17275-17285.
    • (2005) J. Biol. Chem , vol.280 , pp. 17275-17285
    • Debidda, M.1    Wang, L.2    Zang, H.3    Poli, V.4    Zheng, Y.5
  • 16
    • 3042752799 scopus 로고    scopus 로고
    • Induction of interferon-stimulated gene expression and antiviral responses require protein deacetylase activity
    • Chang, H. M., M. Paulson, M. Holko, C. M. Rice, B. R. Williams, I. Marie, and D. E. Levy. 2004. Induction of interferon-stimulated gene expression and antiviral responses require protein deacetylase activity. Proc. Natl. Acad. Sci. USA 101: 9578-9583.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9578-9583
    • Chang, H.M.1    Paulson, M.2    Holko, M.3    Rice, C.M.4    Williams, B.R.5    Marie, I.6    Levy, D.E.7
  • 17
    • 0028982917 scopus 로고
    • Interferon-α engages the insulin receptor substrate-1 to associate with the phosphatidylinositol 3′ kinase
    • Uddin, S., L. Yenush, X.-J. Sun, M. E. Sweet, M. F. White, and L. C. Platanias. 1995. Interferon-α engages the insulin receptor substrate-1 to associate with the phosphatidylinositol 3′ kinase. J. Biol. Chem. 270: 15938-15941.
    • (1995) J. Biol. Chem , vol.270 , pp. 15938-15941
    • Uddin, S.1    Yenush, L.2    Sun, X.-J.3    Sweet, M.E.4    White, M.F.5    Platanias, L.C.6
  • 18
    • 0035957951 scopus 로고    scopus 로고
    • Interferon α/β promotes cell survival by activating NF-κB through phosphatidylinositol-3 kinase and Akt
    • Yang, C. H., A. Murti, S. R. Pfeffer, J. G. Kim, D. B. Donner, and L. M. Pfeffer. 2001. Interferon α/β promotes cell survival by activating NF-κB through phosphatidylinositol-3 kinase and Akt. J. Biol. Chem. 276: 13756-13761.
    • (2001) J. Biol. Chem , vol.276 , pp. 13756-13761
    • Yang, C.H.1    Murti, A.2    Pfeffer, S.R.3    Kim, J.G.4    Donner, D.B.5    Pfeffer, L.M.6
  • 19
    • 0032561211 scopus 로고    scopus 로고
    • Amino-terminal signal transducer and activator of transcription (STAT) domains regulate nuclear translocation and STAT deactivation
    • Strehlow, I., and C. Schindler. 1998. Amino-terminal signal transducer and activator of transcription (STAT) domains regulate nuclear translocation and STAT deactivation. J. Biol. Chem. 273: 28049-28056.
    • (1998) J. Biol. Chem , vol.273 , pp. 28049-28056
    • Strehlow, I.1    Schindler, C.2
  • 20
    • 0033621066 scopus 로고    scopus 로고
    • A nuclear protein tyrosine phosphatase is required for the inactivation of Stat1
    • Haspel, R. L., and J. E. Darnell, Jr. 1999. A nuclear protein tyrosine phosphatase is required for the inactivation of Stat1. Proc. Natl. Acad. Sci. USA 96: 10188-10193.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10188-10193
    • Haspel, R.L.1    Darnell Jr., J.E.2
  • 21
    • 33744961633 scopus 로고    scopus 로고
    • NFκB negatively regulates interferon-induced gene expression and anti-influenza activity
    • Wei, L., M. R. Sandbulte, P. G. Thomas, R. J. Webby, R. Homayouni, and L. M. Pfeffer. 2006. NFκB negatively regulates interferon-induced gene expression and anti-influenza activity. J. Biol. Chem. 281: 11678-11684.
    • (2006) J. Biol. Chem , vol.281 , pp. 11678-11684
    • Wei, L.1    Sandbulte, M.R.2    Thomas, P.G.3    Webby, R.J.4    Homayouni, R.5    Pfeffer, L.M.6
  • 22
    • 0028303977 scopus 로고
    • Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway
    • Akira, S., Y. Nishio, M. Inoue, X.-J. Wang, S. Wei, T. Matsusaka, K. Yoshida, T. Sudo, M. Naruto, and T. Kishimoto. 1994. Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway. Cell 77: 63-71.
    • (1994) Cell , vol.77 , pp. 63-71
    • Akira, S.1    Nishio, Y.2    Inoue, M.3    Wang, X.-J.4    Wei, S.5    Matsusaka, T.6    Yoshida, K.7    Sudo, T.8    Naruto, M.9    Kishimoto, T.10
  • 23
    • 0028349735 scopus 로고
    • Stat3: A STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6
    • Zhong, Z., Z. Wen, and J. E. J. Darnell. 1994. Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6. Science 264: 95-98.
    • (1994) Science , vol.264 , pp. 95-98
    • Zhong, Z.1    Wen, Z.2    Darnell, J.E.J.3
  • 25
    • 0036731485 scopus 로고    scopus 로고
    • Stats: Transcriptional control and biological impact
    • Levy, D. E., and J. E. Darnell, Jr. 2002. Stats: transcriptional control and biological impact. Nat. Rev. Mol. Cell Biol. 3: 651-662.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 651-662
    • Levy, D.E.1    Darnell Jr., J.E.2
  • 26
    • 1042302005 scopus 로고    scopus 로고
    • The STATs of cancer: New molecular targets come of age
    • Yu, H., and R. Jove. 2004. The STATs of cancer: new molecular targets come of age. Nat. Rev. Cancer 4: 97-105.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 97-105
    • Yu, H.1    Jove, R.2
  • 29
    • 0028931604 scopus 로고
    • Choice of STATs and other substrates by modular tyrosine-based motifs in cytokine receptors
    • Stahl, N., T. J. Farruggella, T. G. Boulton, Z. Zhong, J. E. J. Darnell, and G. D. Yancopoulos. 1995. Choice of STATs and other substrates by modular tyrosine-based motifs in cytokine receptors. Science 267: 1349-1353.
    • (1995) Science , vol.267 , pp. 1349-1353
    • Stahl, N.1    Farruggella, T.J.2    Boulton, T.G.3    Zhong, Z.4    Darnell, J.E.J.5    Yancopoulos, G.D.6
  • 30
    • 0028819186 scopus 로고
    • A novel cytoplasmic homology domain in interferon receptors
    • Mullersman, J. E., and L. M. Pfeffer. 1994. A novel cytoplasmic homology domain in interferon receptors. Trends Biochem. Sci. 20: 55-56.
    • (1994) Trends Biochem. Sci , vol.20 , pp. 55-56
    • Mullersman, J.E.1    Pfeffer, L.M.2
  • 31
    • 0032030169 scopus 로고    scopus 로고
    • The antiviral action of interferon is potentiated by removal of the conserved IRTAM domain of the IFNAR1 chain of the interferon α/β receptor: Effects on JAK-STAT activation and receptor downregulation
    • Basu, L., C. H. Yang, A. Murti, J. V. Garcia, E. Croze, S. N. Constantinescu, J. E. Mullersman, and L. M. Pfeffer. 1998. The antiviral action of interferon is potentiated by removal of the conserved IRTAM domain of the IFNAR1 chain of the interferon α/β receptor: effects on JAK-STAT activation and receptor downregulation. Virology 242: 14-21.
    • (1998) Virology , vol.242 , pp. 14-21
    • Basu, L.1    Yang, C.H.2    Murti, A.3    Garcia, J.V.4    Croze, E.5    Constantinescu, S.N.6    Mullersman, J.E.7    Pfeffer, L.M.8
  • 32
    • 0025356737 scopus 로고
    • Shared architecture of hormone binding domains in type I and II interferon receptors
    • Bazan, J. F. 1990. Shared architecture of hormone binding domains in type I and II interferon receptors. Cell 61: 753-754.
    • (1990) Cell , vol.61 , pp. 753-754
    • Bazan, J.F.1
  • 33
    • 0037064119 scopus 로고    scopus 로고
    • Requirement of phosphoinositide 3-kinase and Akt for interferon-β- mediated induction of the β-R1 (SCYB11) gene
    • Rani, M. R., L. Hibbert, N. Sizemore, G. R. Stark, and R. M. Ransohoff. 2002. Requirement of phosphoinositide 3-kinase and Akt for interferon-β- mediated induction of the β-R1 (SCYB11) gene. J. Biol. Chem. 277: 38456-38461.
    • (2002) J. Biol. Chem , vol.277 , pp. 38456-38461
    • Rani, M.R.1    Hibbert, L.2    Sizemore, N.3    Stark, G.R.4    Ransohoff, R.M.5
  • 34
    • 0010136245 scopus 로고    scopus 로고
    • Characterization of β-R1, a gene that is selectively induced by interferon β (IFN-β) compared with IFN-α
    • Rani, M. R., G. R. Foster, S. Leung, D. Leaman, G. R. Stark, and R. M. Ransohoff. 1996. Characterization of β-R1, a gene that is selectively induced by interferon β (IFN-β) compared with IFN-α. J. Biol. Chem. 271: 22878-22884.
    • (1996) J. Biol. Chem , vol.271 , pp. 22878-22884
    • Rani, M.R.1    Foster, G.R.2    Leung, S.3    Leaman, D.4    Stark, G.R.5    Ransohoff, R.M.6
  • 36
    • 33646591224 scopus 로고    scopus 로고
    • Stat3 activation of NF-κB p100 processing involves CBP/p300-mediated acetylation
    • Nadiminty, N., W. Lou, S. O. Lee, X. Lin, D. L. Trump, and A. C. Gao. 2006. Stat3 activation of NF-κB p100 processing involves CBP/p300-mediated acetylation. Proc. Natl. Acad. Sci. USA 103: 7264-7269.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7264-7269
    • Nadiminty, N.1    Lou, W.2    Lee, S.O.3    Lin, X.4    Trump, D.L.5    Gao, A.C.6
  • 37
  • 38
    • 0024380583 scopus 로고
    • Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes
    • Harada, H., T. Fujita, M. Miyamoto, Y. Kimura, M. Maruyama, A. Furia, T. Miyata, and T. Taniguchi. 1989. Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes. Cell 58: 729-739.
    • (1989) Cell , vol.58 , pp. 729-739
    • Harada, H.1    Fujita, T.2    Miyamoto, M.3    Kimura, Y.4    Maruyama, M.5    Furia, A.6    Miyata, T.7    Taniguchi, T.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.