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Mechanisms of type-I- and type-II-interferon-mediated signalling

Platanias, Leonidas C.·2005·Nature Reviews Immunology

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  1. Pestka, S., Langer, J. A., Zoon, K. C. & Samuel, C. E. Interferons and their actions. Annu. Rev. Biochem. 56, 727–777 (1987). · DOI · Paper page
  2. Pestka, S., Krause, C. D. & Walter, M. R. Interferons, interferon-like cytokines, and their receptors. Immunol. Rev. 202, 8–32 (2004). · DOI · Paper page
  3. Pestka, S. The human interferon α species and hybrid proteins. Semin. Oncol. 24, S9-4–S9-17 (1997).
  4. Chen, J., Baig, E. & Fish, E. N. Diversity and relatedness among the type I interferons. J. Interfon Cytokine Res. 24, 687–698 (2004). · DOI
  5. Platanias, L. C. & Fish, E. N. Signaling pathways activated by interferons. Exp. Hematol. 27, 1583–1592 (1999). · DOI · Paper page
  6. Parmar, S. & Platanias, L. C. Interferons: mechanisms of action and clinical applications. Curr. Opin. Oncol. 15, 431–439 (2003). · DOI
  7. Pestka, S. et al. The interferon γ (IFN-γ) receptor: a paradigm for the multichain cytokine receptor. Cytokine Growth Factor Rev. 8, 189–206 (1997). · DOI
  8. Bach, E. A., Aguet, M. & Schreiber, R. D. The IFN γ receptor: a paradigm for cytokine receptor signaling. Annu. Rev. Immunol. 15, 563–591 (1997). · DOI · Paper page
  9. Kotenko, S. V. et al. IFN-λs mediate antiviral protection through a distinct class II cytokine receptor complex. Nature Immunol. 4, 69–77 (2003). · DOI · Paper page
  10. Ihle, J. N. The Janus protein tyrosine kinase family and its role in cytokine signaling. Adv. Immunol. 60, 1–35 (1995). · DOI · Paper page
  11. Platanias, L. C. The p38 mitogen-activated protein kinase pathway and its role in interferon signaling. Pharmacol. Ther. 98, 129–142 (2003). · DOI · Paper page
  12. Der, S. D., Zhou, A., Williams, B. R. & Silverman, R. H. Identification of genes differentially regulated by interferon α, β, or γ using oligonucleotide arrays. Proc. Natl Acad. Sci. USA 95, 15623–15628 (1998). · DOI · Paper page
  13. Fu, X. Y., Schindler, C., Improta, T., Aebersold, R. & Darnell, J. E. The proteins of ISGF-3, the interferon α-induced transcriptional activator, define a gene family involved in signal transduction. Proc. Natl Acad. Sci. USA 89, 7840–7843 (1992). · DOI · Paper page
  14. Shuai, K., Schindler, C., Prezioso, V. R. & Darnell, J. E. Activation of transcription by IFN-γ: tyrosine phosphorylation of a 91-kD DNA binding protein. Science 258, 1808–1812 (1992). · DOI · Paper page
  15. Silvennoinen, O., Ihle, J. N., Schlessinger, J. & Levy, D. E. Interferon-induced nuclear signaling by Jak protein tyrosine kinases. Nature 366, 583–585 (1993). · DOI · Paper page
  16. Stark, G. R., Kerr, I. M., Williams, B. R. G., Silverman, R. H. & Schreiber, R. D. How cells respond to interferons. Annu. Rev. Biochem. 67, 227–264 (1998). · DOI · Paper page
  17. Darnell, J. E. Stats and gene regulation. Science 277, 1630–1635 (1997). An excellent review of the mechanisms of STAT activation and the regulatory effects of STATs on gene transcription. · DOI · Paper page
  18. Aaronson, D. S. & Horvath C. M. A road map for those who don't know JAK–STAT. Science 296, 1653–1655 (2002). · DOI · Paper page
  19. Meinke, A., Barahmand-Pour, F., Wohrl, S., Stoiber, D. & Decker, T. Activation of different Stat5 isoforms contributes to cell-type-restricted signaling in response to interferons. Mol. Cell. Biol. 16, 6937–6944 (1996). · DOI · Paper page
  20. Farrar, J. D., Smith, J. D., Murphy, T. L. & Murphy, K. M. Recruitment of Stat4 to the human interferon-α/β receptor requires activated Stat2. J. Biol. Chem. 275, 2693–2697 (2000). · DOI
  21. Torpey, N., Maher, S. E., Bothwell, A. L. & Pober, J. S. Interferon α but not interleukin 12 activates STAT4 signaling in human vascular endothelial cells. J. Biol. Chem. 279, 26789–26796 (2004). · DOI
  22. Matikainen, S. et al. Interferon-α activates multiple STAT proteins and upregulates proliferation-associated IL-2Rα, c-myc, and pim-1 genes in human T cells. Blood 93, 1980–1991 (1999). · DOI · Paper page
  23. Fasler-Kan, E., Pansky, A., Wiederkehr, M., Battegay, M. & Heim, M. H. Interferon-α activates signal transducers and activators of transcription 5 and 6 in Daudi cells. Eur. J. Biochem. 254, 514–519 (1998). · DOI
  24. Nguyen, K. B. et al. Critical role for STAT4 activation by type 1 interferons in the interferon-γ response to viral infection. Science 297, 2063–2066 (2002). · DOI · Paper page
  25. Wen, Z. & Darnell, J. E. Mapping of Stat3 serine phosphorylation to a single residue (727) and evidence that serine phosphorylation has no influence on DNA binding of Stat1 and Stat3. Nucleic Acids Res. 25, 2062–2067 (1997). · DOI · Paper page
  26. Uddin, S. et al. Protein kinase C-δ (PKC-δ) is activated by type I interferons and mediates phosphorylation of Stat1 on serine 727. J. Biol. Chem. 277, 14408–14416 (2002). The first identification of PKC-δ as an IFN-activated kinase that regulates the phosphorylation of STAT1 on Ser727. · DOI · Paper page
  27. Deb, D. K. et al. Activation of protein kinase C δ by IFN-γ. J. Immunol. 171, 267–273 (2003). · DOI
  28. Kristof, A. S., Marks-Konczalik, J., Billings, E. & Moss, J. Stimulation of signal transducer and activator of transcription-1 (STAT1)-dependent gene transcription by lipopolysaccharide and interferon-γ is regulated by mammalian target of rapamycin. J. Biol. Chem. 278, 33637–33644 (2003). · DOI
  29. Choudhury, G. G. A linear signal transduction pathway involving phosphatidylinositol 3-kinase, protein kinase C-ε, and MAPK in mesangial cells regulates interferon-γ-induced STAT1α transcriptional activation. J. Biol. Chem. 279, 27399–27409 (2004). · DOI
  30. Nair, J. S. et al. Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphorylation in response to IFN-γ. Proc. Natl Acad. Sci. USA 99, 5971–5976 (2002). · DOI
  31. Zhang, J. J. et al. Two contact regions between Stat1 and CBP/p300 in interferon γ signaling. Proc. Natl Acad. Sci. USA 93, 15092–15096 (1996). · DOI · Paper page
  32. Bhattacharya, S. et al. Cooperation of Stat2 and p300/CBP in signaling induced by interferon-α. Nature 383, 344–347 (1996). · DOI · Paper page
  33. Zhang, J. J. et al. Ser727-dependent recruitment of MCM5 by Stat1α in IFN-γ-induced transcriptional activation. EMBO J. 17, 6963–6971 (1998). · DOI · Paper page
  34. DaFonseca, C. J., Shu, F. & Zhang, J. J. Identification of two residues in MCM5 critical for the assembly of MCM complexes and Stat1-mediated transcription activation in response to IFN-γ. Proc. Natl Acad. Sci. USA 98, 3034–3039 (2001). · DOI
  35. Hebbes, T. R., Thorne, A. W. & Crane-Robinson, C. A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J. 7, 1395–1402 (1988). · DOI · Paper page
  36. Paulson, M., Press, C., Smith, E., Tanese, E. & Levy, D. E. IFN-stimulated transcription through a TBP- free acetyltransferase complex escapes viral shutoff. Nature Cell Biol. 4, 140–147 (2002). · DOI
  37. Huang, M. et al. Chromatin-remodelling factor BRG1 selectively activates a subset of interferon-α-inducible genes. Nature Cell Biol. 4, 774–781 (2002). · DOI
  38. Zhu, M., John, S., Berg, M. & Leonard, W. J. Functional association of Nmi with Stat5 and Stat1 in IL-2- and IFNγ-mediated signaling. Cell 96, 121–130 (1999). · DOI · Paper page
  39. Nusinzon, I. & Horvath, C. M. Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1. Proc. Natl Acad. Sci. USA 100, 14742–14747 (2003). The first evidence that histone-deacetylase activity is required for IFN-dependent transcription. · DOI · Paper page
  40. Chang, H. M. et al. Induction of interferon-stimulated gene expression and antiviral responses require protein deacetylase activity. Proc. Natl Acad. Sci. USA 101, 9578–9583 (2004). · DOI · Paper page
  41. Sakamoto, S., Potla, R. & Larner, A. C. Histone deacetylase activity is required to recruit RNA polymerase II to the promoters of selected interferon-stimulated early response genes. J. Biol. Chem. 279, 40362–40367 (2004). · DOI
  42. Mayer, B. J., Hamaguchi, M. & Hanafusa, H. A novel viral oncogene with structural homology to phospholipase C. Nature 332, 272–275 (1988). · DOI · Paper page
  43. Feller, S. M. Crk family adaptors — signaling complex formation and biological roles. Oncogene 20, 6348–6371 (2001). · DOI · Paper page
  44. Ahmad, S., Alsayed, Y., Druker, B. J. & Platanias, L. C. The type I interferon receptor mediates tyrosine phosphorylation of the CrkL adaptor protein. J. Biol. Chem. 272, 29991–29994 (1997). · DOI
  45. Alsayed, Y. et al. Interferon-γ activates the C3G/Rap1 signaling pathway. J. Immunol. 164, 1800–1806 (2000). · DOI
  46. Stork, P. J. Does Rap1 deserve a bad Rap? Trends Biochem. Sci. 28, 267–275 (2003). · DOI
  47. Bos, J. L., de Rooij, J. & Reedquist, K. A. Rap1 signaling: adhering to new models. Nature Rev. Mol. Cell Biol. 2, 369–377 (2001). · DOI · Paper page
  48. Kitayama, H., Sugimoto, Y., Matsuzaki, T., Ikawa, Y. & Noda, M. A ras-related gene with transformation suppressor activity. Cell 56, 77–84 (1989). · DOI · Paper page
  49. Schmitt, J. M. & Stork, P. J. Cyclic AMP-mediated inhibition of cell growth requires the small G protein Rap1. Mol. Cell. Biol. 21, 3671–3683 (2001). · DOI · Paper page
  50. Lahlou, H. et al. sst2 Somatostatin receptor inhibits cell proliferation through Ras-, Rap1-, and B-Raf-dependent ERK2 activation. J. Biol. Chem. 278, 39356–39371 (2003). · DOI
  51. Hattori, M. & Minato, N. Rap1 GTPase: functions, regulation and malignancy. J. Biochem. 134, 479–484 (2003). · DOI · Paper page
  52. Lekmine, F. et al. The CrkL adapter protein is required for type I interferon-dependent gene transcription and activation of the small G-protein Rap1. Biochem. Biophys. Res. Commun. 291, 744–750 (2002). · DOI
  53. Platanias, L. C. et al. CrkL and CrkII participate in the generation of the growth inhibitory effects of interferons on primary hematopoietic progenitors. Exp. Hematol. 27, 1315–1321 (1999). · DOI
  54. Huang, C. C., You, J. L., Wu, M. Y. & Hsu, K. S. Rap1-induced p38 mitogen-activated protein kinase activation facilitates AMPA receptor trafficking via the GDI•Rab5 complex. Potential role in (S)-3,5-dihydroxyphenylglycene-induced long-term depression. J. Biol. Chem. 279, 12286–12292 (2004). · DOI · Paper page
  55. Katagiri, K. et al. Crucial functions of the Rap1 effector molecule RAPL in lymphocyte and dendritic cell trafficking. Nature Immunol. 5, 1045–1051 (2004). · DOI · Paper page
  56. Fish, E. N. et al. Activation of a CrkL–Stat5 signaling complex by type I interferons. J. Biol. Chem. 274, 571–573 (1999). The first report that CRKL forms DNA-binding complexes with STAT5 and functions as a nuclear adaptor for STAT5 in type-I-IFN-mediated signalling. · DOI
  57. Grumbach, I. M. et al. Engagement of the CrkL adapter in interferon α signaling in BCR–ABL expressing cells. Br. J. Haematol. 112, 327–336 (2001). · doi:10.1046/j.1365-2141.2001.02556.x
  58. Takahashi, Y., Lallemand-Breitenbach, V., Zhu, J. & de The, H. PML nuclear bodies and apoptosis. Oncogene 23, 2819–2824 (2004). · DOI
  59. Uddin, S. et al. Role of Stat5 in type I interferon-signaling and transcriptional regulation. Biochem. Biophys. Res. Commun. 308, 325–330 (2003). · DOI
  60. Chang, L. & Karin, M. Mammalian MAP kinase signaling cascades. Nature 410, 37–40 (2001). · DOI · Paper page
  61. Dong, C., Davis, R. J. & Flavell, R. A. MAP kinases in the immune response. Annu. Rev. Immunol. 20, 55–72 (2002). · DOI · Paper page
  62. Hazzalin, C. A. & Mahadevan, L. C. MAPK-regulated transcription: a continuously variable gene switch? Nature Rev. Mol. Cell Biol. 3, 30–40 (2002). · DOI · Paper page
  63. Platanias, L. C. Map kinase signaling pathways and hematologic malignancies. Blood 101, 4667–4679 (2003). · DOI · Paper page
  64. Uddin, S. et al. Activation of the p38 Map kinase by type I interferons. J. Biol. Chem. 274, 30127–30131 (1999). · DOI · Paper page
  65. Goh, K. C., Haque, S. J. & Williams, B. R. p38 MAP kinase is required for STAT1 serine phosphorylation and transcriptional activation induced by interferons. EMBO J. 18, 5601–5608 (1999). · DOI · Paper page
  66. Uddin, S. et al. The Rac1/p38 Map kinase pathway is required for IFNα-dependent transcriptional activation but not serine phosphorylation of Stat-proteins. J. Biol. Chem. 275, 27634–27640 (2000). · DOI
  67. Kovarik, P. et al. Stress-induced phosphorylation of Stat1 at Ser727 requires p38 mitogen-activated protein kinase whereas IFN-γ uses a different pathway. Proc. Natl Acad. Sci. USA 96, 13956–13961 (1999). · DOI · Paper page
  68. Li, Y. et al. Role of p38α Map kinase in type I interferon signaling. J. Biol. Chem. 279, 970–979 (2004). Definitive evidence that the type-I-IFN-activated p38-signalling pathway is required for transcriptional regulation. · DOI
  69. Ramsauer, K. et al. p38 MAPK enhances STAT1-dependent transcription independently of Ser-727 phosphorylation. Proc. Natl Acad. Sci. USA 99, 12859–12864 (2002). · DOI
  70. Crespo, P., Schuebel, K. E., Ostrom, A. A., Gutkind, J. S. & Bustelo, X. R. Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product. Nature 385, 169–172 (1997). · DOI · Paper page
  71. Bustelo, X. R. Regulatory and signaling properties of the Vav family. Mol. Cell. Biol. 20, 1461–1477 (2000). · DOI · Paper page
  72. Platanias, L. C. & Sweet, M. E. Interferon α induces rapid tyrosine phosphorylation of the vav proto-oncogene product in hematopoietic cells. J. Biol. Chem. 269, 3143–3146 (1994). · DOI
  73. Micouin, A., Wietzrbin, J., Steunou, V. & Martyre, M. C. p95Vav is associated to the IFNα/β receptor and contributes to the antiproliferative effect of IFNα in megacaryocytic cell lines. Oncogene 19, 387–394 (2000). · doi:10.1038/sj.onc.1203314
  74. Uddin, S., Sweet, M. E., Colamonici, O. R., Krolewski, J. J. & Platanias, L. C. The vav proto-oncogene product interacts with the Tyk-2 tyrosine kinase. FEBS Lett. 403, 31–34 (1997). · DOI
  75. Li, Y. et al. Activation of Mkk3 and Mkk6 by type I interferons. J. Biol. Chem. 280, 10001–10010 (2005). · DOI
  76. Kotlyarov, A. & Gaestel, M. Is MK2 (mitogen-activated protein kinase-activated protein kinase 2) the key for understanding post-transcriptional regulation of gene expression? Biochem. Soc. Trans. 30, 959–963 (2002). · DOI
  77. Deak, M., Clifton A. D., Lucocq, L. M. & Alessi, D. R. Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J. 17, 4426–4441 (1998). · DOI · Paper page
  78. Soloaga, A. et al. MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14. EMBO J. 22, 2788–2797 (2003). · DOI · Paper page
  79. Clayton, A. L. & Mahadevan, L. C. MAP kinase-mediated phosphoacetylation of histone H3 and inducible gene regulation. FEBS Lett. 546, 51–58 (2003). · DOI · Paper page
  80. Waskiewicz, A. J., Flynn, A., Proud, C. G. & Cooper, J. A. Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J. 16, 1909–1920 (1997). · DOI · Paper page
  81. Knauf, U., Tschopp, C. & Gram, H. Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2. Mol. Cell. Biol. 21, 5500–5511 (2001). · DOI
  82. Mayer, I. A. et al. The p38 MAPK pathway mediates the growth inhibitory effects of interferon-α in BCR–ABL-expressing cells. J. Biol. Chem. 276, 28570–28577 (2001). · DOI
  83. Verma, A. et al. Activation of the p38 Map kinase pathway mediates the suppressive effects of type I interferons and transforming growth factor β on normal hematopoiesis. J. Biol. Chem. 277, 7726–7735 (2002). · DOI · Paper page
  84. Ishida, H. et al. Involvement of p38 signaling pathway in interferon-α-mediated antiviral activity towards hepatitis C virus. Biochem. Biophys. Res. Commun. 321, 722–727 (2004). · DOI
  85. David, M. et al. Requirement for MAP kinase (ERK2) activity in interferon α- and interferon β-stimulated gene expression through STAT proteins. Science 269, 1721–1723 (1995). · DOI · Paper page
  86. Hu, J. et al. ERK1 and ERK2 activate CCAAAT/enhancer-binding protein-β-dependent gene transcription in response to interferon-γ. J. Biol. Chem. 276, 287–297 (2001). · DOI
  87. Wang, F. et al. Disruption of Erk-dependent type I interferon induction breaks the myxoma virus species barrier. Nature Immunol. 5, 1266–1274 (2004). · DOI
  88. Roy, S. K. et al. MEKK1 plays a critical role in activating the transcription factor C/EBP-β-dependent gene expression in response to IFN-γ. Proc. Natl Acad. Sci. USA 99, 7945–7950 (2002). · DOI
  89. Roy, S. K., Wachira, S. J., Weihua, X., Hu, J. & Kalvakolanu, D. V. CCAAT/enhancer-binding protein-β regulates interferon-induced transcription through a novel element. J. Biol. Chem. 275, 12626–12632 (2000). · DOI
  90. Floyd, Z. E. & Stephens, J. M. Interferon-γ-mediated activation and ubiquitin-proteasome-dependent degradation of PPARγ in adipocytes. J. Biol. Chem. 277, 4062–4068 (2002). · DOI
  91. Li, C. et al. IFNα induces Fas expression and apoptosis in hedgehog pathway activated BCC cells through inhibiting Ras–Erk signaling. Oncogene 23, 1608–1617 (2004). · DOI
  92. Li, G., Xiang, Y., Sabapathy, K. & Silverman, R. H. An apoptotic signaling pathway in the interferon antiviral response mediated by RNase L and c-Jun NH2-terminal kinase. J. Biol. Chem. 279, 1123–1131 (2004). · DOI
  93. Uddin, S. et al. Interferon-α engages the insulin receptor substrate-1 to associate with the phosphatidylinositol 3′-kinase. J. Biol. Chem. 270, 15938–159341 (1995). · DOI
  94. Platanias, L. C. et al. The type I interferon receptor mediates tyrosine phosphorylation of insulin receptor substrate 2. J. Biol. Chem. 271, 278–282 (1996). · DOI
  95. Burfoot, M. S. et al. Janus kinase-dependent activation of insulin receptor substrate 1 in response to interleukin-4, oncostatin M, and the interferons. J. Biol. Chem. 272, 24183–24190 (1997). · DOI
  96. Uddin, S. et al. The IRS-pathway operates distinctively from the Stat-pathway in hematopoietic cells and transduces common and distinct signals during engagement of the insulin or interferon-α receptors. Blood 90, 2574–2582 (1997).
  97. Uddin, S. et al. Interferon-dependent activation of the serine kinase PI 3′-kinase requires engagement of the IRS pathway but not the Stat pathway. Biochem. Biophys. Res. Commun. 270, 158–162 (2000). · DOI
  98. Uddin, S. et al. Activation of the phosphatidylinositol 3-kinase serine kinase by IFN-α. J. Immunol. 158, 2390–2397 (1997). · DOI
  99. Cengel, K. A. & Freund, G. G. JAK1-dependent phosphorylation of insulin receptor substrate-1 (IRS-1) is inhibited by IRS-1 serine phosphorylation. J. Biol. Chem. 274, 27969–27974 (1999). · DOI
  100. Nguyen, H., Ramana, C. V., Bayes, J. & Stark, G. R. Roles of phosphatidylinositol 3-kinase in interferon-γ-dependent phosphorylation of STAT1 on serine 727 and activation of gene expression. J. Biol. Chem. 276, 33361–33368 (2001). · DOI
  101. DeVries, T. A., Rachelle, L., Kalkofen, A., Matassa, A. & Reyland, M. E. Protein kinase Cδ regulates apoptosis via activation of STAT1. J. Biol. Chem. 279, 45603–45612 (2004). · DOI
  102. Lu, Z. et al. Tumor promotion by depleting cells of protein kinase C-δ. Mol. Cell. Biol. 17, 3418–3428 (1997). · DOI · Paper page
  103. Redding, P. J. et al. Transgenic mice overexpressing protein kinase C δ in the epidermis are resistant to skin tumor promotion by 12-O-tetradecanoylphorbol-13-acetate. Cancer Res. 59, 5710–5718 (1999).
  104. Srivastava, K. K. et al. Engagement of protein kinase C-θ in interferon signaling in T-cells. J. Biol. Chem. 279, 29911–29920 (2004). · DOI
  105. Vivanco, I. & Sawyers, C. L. The phosphatidylinositol 3-kinase AKT pathway in human cancer. Nature Rev. Cancer 2, 489–501 (2002). · DOI · Paper page
  106. Barca, O. et al. Interferon β promotes survival in primary astrocytes through phosphatidylinositol 3-kinase. J. Neuroimmunol. 139, 155–159 (2003). · DOI
  107. Ruuth, K., Carlsson, L., Hallberg, B. & Lundgren, E. Interferon-α promotes survival of human primary B-lymphocytes via phosphatidylinositol 3-kinase. Biochem. Biophys. Res. Commun. 284, 583–586 (2001). · DOI
  108. Wang, K. et al. Inhibition of neutrophil apoptosis by type 1 IFN depends on cross-talk between phosphoinositol 3-kinase, protein kinase C-δ, and NF-κB signaling pathways. J. Immunol. 171, 1035–1041 (2003). · DOI
  109. Yang, C. H. et al. Interferon α/β promotes cell survival by activating nuclear factor κB through phosphatidylinositol 3-kinase and Akt. J. Biol. Chem. 276, 13756–13761 (2001). · DOI
  110. Thyrell, L. et al. Interferon α-induced apoptosis in tumor cells is mediated through the phosphoinositide 3-kinase/mammalian target of rapamycin signaling pathway. J. Biol. Chem. 279, 24152–24162 (2004). · DOI
  111. Hwang, S. Y. et al. LY294002 inhibits interferon-γ-stimulated inducible nitric oxide synthase expression in BV2 microglial cells. Biochem. Biophys. Res. Commun. 318, 691–697 (2004). · DOI
  112. Navarro, A., Anand-Apte, B., Tanabe, Y., Feldman, G. & Larner, A. C. A PI-3 kinase-dependent, Stat1-independent signaling pathway regulates interferon-stimulated monocyte adhesion. J. Leukoc. Biol. 73, 540–545 (2003). · DOI
  113. Rani, M. R., Hibbert, L., Sizemore, N., Stark, G. R. & Ransohoff, R. M. 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). · DOI
  114. Marcus, P. I. & Salb, J. M. Molecular basis of interferon action: inhibition of viral RNA translation. Virology 30, 502–516 (1966). · doi:10.1016/0042-6822(66)90126-7
  115. Doualla-Bell, F. & Koromilas, A. E. Induction of PG G/H synthase-2 in bovine myometrial cells by interferon-τ requires the activation of the p38 MAPK pathway. Endocrinology 142, 5107–5115 (2001). · DOI
  116. Lekmine, F. et al. Activation of the p70 S6 kinase and phosphorylation of the 4E-BP1 repressor of mRNA translation by type I interferons. J. Biol. Chem. 278, 27772–27780 (2003). The first report that type I IFNs activate pathways for the initiation of mRNA translation that are downstream of MTOR. · DOI
  117. Lekmine, F. et al. Interferon-γ engages the p70 S6 kinase to regulate phosphorylation of the 40S S6 ribosomal protein. Exp. Cell Res. 295, 173–182 (2004). · DOI
  118. Hay, N. & Sonenberg, N. Upstream and downstream of mTOR. Genes Dev. 18, 1926–1945 (2004). A comprehensive review of MTOR and the regulation of signals for mRNA translation. · DOI · Paper page
  119. Bjornsti, M. A. & Houghton, P. J. The TOR pathway: a target for cancer therapy. Nature Rev. Cancer 4, 335–348 (2004). · DOI · Paper page
  120. Gingras, A. C. et al. Hierarchical phosphorylation of the translation inhibitor 4E-BP1. Genes Dev. 15, 2852–2864 (2001). · DOI · Paper page
  121. Lal, L. et al. Activation of the p70 S6 kinase by all-trans-retinoic acid in acute promyelocytic leukemia cells. Blood 105, 1669–1677 (2005). · DOI
  122. Garber, K. Rapamycin's resurrection: a new way to target the cancer cell cycle. J. Natl Cancer Inst. 93, 1517–1519 (2001). · DOI · Paper page
  123. Ramana, C. V., Gil, P. M., Schreiber, R. D. & Stark, G. R. Stat1-dependent and -independent pathways in IFNγ-dependent signaling. Trends Immunol. 23, 96–101 (2002). · DOI · Paper page
  124. Sizemore, N. et al. Inhibitor of κB kinase is required to activate a subset of interferon γ-stimulated genes. Proc. Natl Acad. Sci. USA 101, 7994–7998 (2004). · doi:10.1073/pnas.0401593101
  125. Deane, J. A. & Fruman, D. A. Phosphoinositide 3-kinase: diverse roles in immune cell activation. Annu. Rev. Immunol. 22, 563–598 (2004). · DOI · Paper page
  126. Malik, A. H. & Lee, W. M. Chronic hepatitis B virus infection: treatment strategies for the next millennium. Ann. Intern. Med. 132, 723–731 (2000). · DOI
  127. Liang, T. J., Rehermann, B., Seeff, L. B. & Hoofnagle, J. H. Pathogenesis, natural history, treatment, and prevention of hepatitis C. Ann. Intern. Med. 132, 296–305 (2000). · DOI · Paper page
  128. Loutfy, M. R. et al. Interferon alfacon-1 plus corticosteroids in severe acute respiratory syndrome: a preliminary study. JAMA 290, 3222–3228 (2003). · DOI · Paper page

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Metadata

Authors
Platanias, L. C.
Venue
Nature Reviews Immunology
Published
2005-05-01
Volume
5
Issue
5
Pages
375-386
ISSN
  • 1474-1733 (ISSN-L)
  • 1474-1741
OpenAlex
W2078844752
Cited by
3,491
References
11
FWCI
4.83
Type
journal article
Language
en
Open access
closed
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Mechanisms of type-I- and type-II-interferon-mediated signalling. https://app.cochat.ai/papers/10.1038/nri1604
The paper
Platanias, L. C. (2005). Mechanisms of type-I- and type-II-interferon-mediated signalling. Nature Reviews Immunology. https://doi.org/10.1038/nri1604

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.