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Volumn 407, Issue 1, 2007, Pages 141-151

Comparable potency of IFNα2 and IFNβ on immediate JAK/STAT activation but differential down-regulation of IFNAR2

Author keywords

Interferon (IFN ); Interferon receptor; Interferon (IFN ); Internalization; Janus kinase (JAK); Signal transducer and activator of transcription (STAT)

Indexed keywords

BINDING ENERGY; BIOACTIVITY; ENZYMES; IMMUNOLOGY; SIGNAL TRANSDUCTION; TRANSCRIPTION;

EID: 35148815311     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070605     Document Type: Article
Times cited : (66)

References (44)
  • 1
    • 33748470359 scopus 로고    scopus 로고
    • Fifty years of interferon research: Aiming at a moving target
    • Vilcek, J. (2006) Fifty years of interferon research: aiming at a moving target. Immunity 25, 343-348
    • (2006) Immunity , vol.25 , pp. 343-348
    • Vilcek, J.1
  • 2
    • 9644262469 scopus 로고    scopus 로고
    • Interferons, interferon-like cytokines, and their receptors
    • Pestka, S., Krause, C. D. and Walter, M. R. (2004) Interferons, interferon-like cytokines, and their receptors. Immunol. Rev. 202, 8-32
    • (2004) Immunol. Rev , vol.202 , pp. 8-32
    • Pestka, S.1    Krause, C.D.2    Walter, M.R.3
  • 3
    • 0032863261 scopus 로고    scopus 로고
    • The Janus kinase family of protein tyrosine kinases and their role in signaling
    • Yen, T. C. and Pellegrini, S. (1999) The Janus kinase family of protein tyrosine kinases and their role in signaling. Cell. Mol. Life Sci. 55, 1523-1534
    • (1999) Cell. Mol. Life Sci , vol.55 , pp. 1523-1534
    • Yen, T.C.1    Pellegrini, S.2
  • 4
    • 33750522675 scopus 로고    scopus 로고
    • Jaks and cytokine receptors: An intimate relationship
    • Haan, C., Kreis, S., Margue, C. and Behrmann, I. (2006) Jaks and cytokine receptors: an intimate relationship. Biochem. Pharmacol. 72, 1538-1546
    • (2006) Biochem. Pharmacol , vol.72 , pp. 1538-1546
    • Haan, C.1    Kreis, S.2    Margue, C.3    Behrmann, I.4
  • 5
    • 30344483167 scopus 로고    scopus 로고
    • Alternative and accessory pathways in the regulation of IFN-β-mediated gene expression
    • Rani, M. R. and Ransohoff, R. M. (2005) Alternative and accessory pathways in the regulation of IFN-β-mediated gene expression. J. Interferon Cytokine Res. 25, 788-798
    • (2005) J. Interferon Cytokine Res , vol.25 , pp. 788-798
    • Rani, M.R.1    Ransohoff, R.M.2
  • 6
    • 33748450379 scopus 로고    scopus 로고
    • Complex modulation of cell type-specific signaling in response to type I interferons
    • van Boxel-Dezaire, A. H., Rani, M. R. and Stark, G. R. (2006) Complex modulation of cell type-specific signaling in response to type I interferons. Immunity 25, 361-372
    • (2006) Immunity , vol.25 , pp. 361-372
    • van Boxel-Dezaire, A.H.1    Rani, M.R.2    Stark, G.R.3
  • 7
    • 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 down-regulation
    • Basu, L., Yang, C. H., Murti, A., Garcia, J. V., Croze, E., Constantinescu, S. N., Mullersman, J. E. and Pfeffer, L. M. (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 down-regulation. 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
  • 9
    • 0031042220 scopus 로고    scopus 로고
    • Contributions of cloned type I interferon receptor subunits to differential ligand binding
    • Cutrone, E. C. and Langer, J. A. (1997) Contributions of cloned type I interferon receptor subunits to differential ligand binding. FEBS Lett. 404, 197-202
    • (1997) FEBS Lett , vol.404 , pp. 197-202
    • Cutrone, E.C.1    Langer, J.A.2
  • 10
    • 0032566486 scopus 로고    scopus 로고
    • Shared receptor components but distinct complexes for α and β interferons
    • Lewerenz, M., Mogensen, K. E. and Uzé, G. (1998) Shared receptor components but distinct complexes for α and β interferons. J. Mol. Biol. 282, 585-599
    • (1998) J. Mol. Biol , vol.282 , pp. 585-599
    • Lewerenz, M.1    Mogensen, K.E.2    Uzé, G.3
  • 11
    • 1642432084 scopus 로고    scopus 로고
    • The Class II cytokine receptor (CRF2) family: Overview and patterns of receptor-ligand interactions
    • Langer, J. A., Cutrone, E. C. and Kotenko, S. (2004) The Class II cytokine receptor (CRF2) family: overview and patterns of receptor-ligand interactions. Cytokine Growth Factor Rev. 15, 33-48
    • (2004) Cytokine Growth Factor Rev , vol.15 , pp. 33-48
    • Langer, J.A.1    Cutrone, E.C.2    Kotenko, S.3
  • 12
    • 4143062575 scopus 로고    scopus 로고
    • Ligand-induced assembling of the type I interferon receptor on supported lipid bilayers
    • Lamken, P., Lata, S., Gavutis, M. and Piehler, J. (2004) Ligand-induced assembling of the type I interferon receptor on supported lipid bilayers. J. Mol. Biol. 341, 303-318
    • (2004) J. Mol. Biol , vol.341 , pp. 303-318
    • Lamken, P.1    Lata, S.2    Gavutis, M.3    Piehler, J.4
  • 13
    • 33644522358 scopus 로고    scopus 로고
    • Inquiring into the differential action of interferons (IFNs): An IFN-α2 mutant with enhanced affinity to IFNAR1 is functionally similar to IFN-β
    • Jaitin, D. A., Roisman, L. C., Jaks, E., Gavutis, M., Piehler, J., Van der Heyden, J., Uzé, G. and Schreiber, G. (2006) Inquiring into the differential action of interferons (IFNs): an IFN-α2 mutant with enhanced affinity to IFNAR1 is functionally similar to IFN-β. Mol. Cell. Biol. 26, 1888-1897
    • (2006) Mol. Cell. Biol , vol.26 , pp. 1888-1897
    • Jaitin, D.A.1    Roisman, L.C.2    Jaks, E.3    Gavutis, M.4    Piehler, J.5    Van der Heyden, J.6    Uzé, G.7    Schreiber, G.8
  • 14
    • 25144452720 scopus 로고    scopus 로고
    • Mutational analysis of the IFNAR1 binding site on IFNα2 reveals the architecture of a weak ligand-receptor binding-site
    • Roisman, L. C., Jaitin, D. A., Baker, D. P. and Schreiber, G. (2005) Mutational analysis of the IFNAR1 binding site on IFNα2 reveals the architecture of a weak ligand-receptor binding-site. J. Mol. Biol. 353, 271-281
    • (2005) J. Mol. Biol , vol.353 , pp. 271-281
    • Roisman, L.C.1    Jaitin, D.A.2    Baker, D.P.3    Schreiber, G.4
  • 15
    • 0037415720 scopus 로고    scopus 로고
    • The tyrosine kinase Tyk2 controls IFNAR1 cell surface expression
    • Ragimbeau, J., Dondi, E., Alcover, A., Eid, P., Uzé, G. and Pellegrini, S. (2003) The tyrosine kinase Tyk2 controls IFNAR1 cell surface expression. EMBO J. 22, 537-547
    • (2003) EMBO J , vol.22 , pp. 537-547
    • Ragimbeau, J.1    Dondi, E.2    Alcover, A.3    Eid, P.4    Uzé, G.5    Pellegrini, S.6
  • 17
    • 8744247500 scopus 로고    scopus 로고
    • Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor
    • Kumar, K. G., Krolewski, J. J. and Fuchs, S. Y. (2004) Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor. J. Biol. Chem. 279, 46614-46620
    • (2004) J. Biol. Chem , vol.279 , pp. 46614-46620
    • Kumar, K.G.1    Krolewski, J.J.2    Fuchs, S.Y.3
  • 18
    • 0029786754 scopus 로고    scopus 로고
    • Interferon-α-dependent activation of Tyk2 requires phosphorylation of positive regulatory tyrosines by another kinase
    • Gauzzi, M. C., Velazquez, L., McKendry, R., Mogensen, K. E., Fellous, M. and Pellegrini, S. (1996) Interferon-α-dependent activation of Tyk2 requires phosphorylation of positive regulatory tyrosines by another kinase. J. Biol. Chem. 271, 20494-20500
    • (1996) J. Biol. Chem , vol.271 , pp. 20494-20500
    • Gauzzi, M.C.1    Velazquez, L.2    McKendry, R.3    Mogensen, K.E.4    Fellous, M.5    Pellegrini, S.6
  • 19
    • 0038394715 scopus 로고    scopus 로고
    • Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
    • Haglund, K., Sigismund, S., Polo, S., Szymkiewicz, I., Di Fiore, P. P. and Dikic, I. (2003) Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat. Cell Biol. 5, 461-466
    • (2003) Nat. Cell Biol , vol.5 , pp. 461-466
    • Haglund, K.1    Sigismund, S.2    Polo, S.3    Szymkiewicz, I.4    Di Fiore, P.P.5    Dikic, I.6
  • 21
    • 11244273938 scopus 로고    scopus 로고
    • Both proteasomes and lysosomes degrade the activated erythropoietin receptor
    • Walraten, P., Verdier, F., Kadri, Z., Chretien, S., Lacombe, C. and Mayeux, P. (2005) Both proteasomes and lysosomes degrade the activated erythropoietin receptor. Blood 105, 600-608
    • (2005) Blood , vol.105 , pp. 600-608
    • Walraten, P.1    Verdier, F.2    Kadri, Z.3    Chretien, S.4    Lacombe, C.5    Mayeux, P.6
  • 22
    • 0019427474 scopus 로고
    • Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts
    • Basu, S. K., Goldstein, J. L., Anderson, R. G. and Brown, M. S. (1981) Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts. Cell 24, 493-502
    • (1981) Cell , vol.24 , pp. 493-502
    • Basu, S.K.1    Goldstein, J.L.2    Anderson, R.G.3    Brown, M.S.4
  • 23
    • 0000241799 scopus 로고
    • pH and the recycling of transferrin during receptor-mediated endocytosis
    • Dautry-Varsat, A., Ciechanover, A. and Lodish, H. F. (1983) pH and the recycling of transferrin during receptor-mediated endocytosis. Proc. Natl. Acad. Sci. U.S.A. 80, 2258-2262
    • (1983) Proc. Natl. Acad. Sci. U.S.A , vol.80 , pp. 2258-2262
    • Dautry-Varsat, A.1    Ciechanover, A.2    Lodish, H.F.3
  • 25
    • 0036204683 scopus 로고    scopus 로고
    • Comparison of gene expression patterns induced by treatment of human umbilical vein endothelial cells with IFN-α2b vs. IFN-β1a: Understanding the functional relationship between distinct type I interferons that act through a common receptor
    • da Silva, A. J., Brickelmaier, M., Majeau, G. R., Lukashin, A. V., Peyman, J., Whitty, A. and Hochman, P. S. (2002) Comparison of gene expression patterns induced by treatment of human umbilical vein endothelial cells with IFN-α2b vs. IFN-β1a: understanding the functional relationship between distinct type I interferons that act through a common receptor. J. Interferon Cytokine Res. 22, 173-188
    • (2002) J. Interferon Cytokine Res , vol.22 , pp. 173-188
    • da Silva, A.J.1    Brickelmaier, M.2    Majeau, G.R.3    Lukashin, A.V.4    Peyman, J.5    Whitty, A.6    Hochman, P.S.7
  • 27
  • 28
    • 0036260742 scopus 로고    scopus 로고
    • Mechanisms for regulation of cellular responsiveness to human IFN-β1a
    • Dupont, S. A., Goelz, S., Goyal, J. and Green, M. (2002) Mechanisms for regulation of cellular responsiveness to human IFN-β1a. J. Interferon Cytokine Res. 22, 491-501
    • (2002) J. Interferon Cytokine Res , vol.22 , pp. 491-501
    • Dupont, S.A.1    Goelz, S.2    Goyal, J.3    Green, M.4
  • 29
    • 1842855210 scopus 로고    scopus 로고
    • Interferon-γ inhibits interferon-α signalling in hepatic cells: Evidence for the involvement of STAT1 induction and hyperexpression of STAT1 in chronic hepatitis C
    • Radaeva, S., Jaruga, B., Kim, W. H., Heller, T., Liang, T. J. and Gao, B. (2004) Interferon-γ inhibits interferon-α signalling in hepatic cells: evidence for the involvement of STAT1 induction and hyperexpression of STAT1 in chronic hepatitis C. Biochem. J. 379, 199-208
    • (2004) Biochem. J , vol.379 , pp. 199-208
    • Radaeva, S.1    Jaruga, B.2    Kim, W.H.3    Heller, T.4    Liang, T.J.5    Gao, B.6
  • 30
    • 31544476539 scopus 로고    scopus 로고
    • Modulation of STAT1 protein levels: A mechanism shaping CD8 T-cell responses in vivo
    • Gil, M. P., Salomon, R., Louten, J. and Biron, C. A. (2006) Modulation of STAT1 protein levels: a mechanism shaping CD8 T-cell responses in vivo. Blood 107, 987-993
    • (2006) Blood , vol.107 , pp. 987-993
    • Gil, M.P.1    Salomon, R.2    Louten, J.3    Biron, C.A.4
  • 31
    • 33846871508 scopus 로고    scopus 로고
    • Dendritic cell maturation alters intracellular signaling networks, enabling differential effects of IFNα/β on antigen cross-presentation
    • Longman, R. S., Braun, D., Pellegrini, S., Rice, C., Darnell, R. and Albert, M. L. (2006) Dendritic cell maturation alters intracellular signaling networks, enabling differential effects of IFNα/β on antigen cross-presentation. Blood 109, 1113-1122
    • (2006) Blood , vol.109 , pp. 1113-1122
    • Longman, R.S.1    Braun, D.2    Pellegrini, S.3    Rice, C.4    Darnell, R.5    Albert, M.L.6
  • 32
    • 0030945179 scopus 로고    scopus 로고
    • Functional subdomains of STAT2 required for preassociation with the α interferon receptor and for signaling
    • Li, X., Leung, S., Kerr, I. M. and Stark, G. R. (1997) Functional subdomains of STAT2 required for preassociation with the α interferon receptor and for signaling. Mol. Cell. Biol. 17, 2048-2056
    • (1997) Mol. Cell. Biol , vol.17 , pp. 2048-2056
    • Li, X.1    Leung, S.2    Kerr, I.M.3    Stark, G.R.4
  • 33
    • 0028605245 scopus 로고
    • Differential tyrosine phosphorylation of the IFNAR chain of the type I interferon receptor and of an associated surface protein in response to IFN-α and IFN-β
    • Abramovich, C., Shulman, L. M., Ratovitski, E., Harroch, S., Tovey, M., Eid, P. and Revel, M. (1994) Differential tyrosine phosphorylation of the IFNAR chain of the type I interferon receptor and of an associated surface protein in response to IFN-α and IFN-β. EMBO J. 13, 5871-5877
    • (1994) EMBO J , vol.13 , pp. 5871-5877
    • Abramovich, C.1    Shulman, L.M.2    Ratovitski, E.3    Harroch, S.4    Tovey, M.5    Eid, P.6    Revel, M.7
  • 34
    • 0030468346 scopus 로고    scopus 로고
    • The human type I interferon receptor: Identification of the interferon β-specific receptor-associated phosphoprotein
    • Croze, E., Russell-Harde, D., Wagner, T. C., Pu, H., Pfefter, L. M. and Perez, H. D. (1996) The human type I interferon receptor: identification of the interferon β-specific receptor-associated phosphoprotein. J. Biol. Chem. 271, 33165-33168
    • (1996) J. Biol. Chem , vol.271 , pp. 33165-33168
    • Croze, E.1    Russell-Harde, D.2    Wagner, T.C.3    Pu, H.4    Pfefter, L.M.5    Perez, H.D.6
  • 35
    • 0029846515 scopus 로고    scopus 로고
    • Differences in interferon α and β signaling: Interferon β selectively induces the interaction of the α and βL subunits of the type I interferon receptor
    • Platanias, L. C., Uddin, S., Domanski, P. and Colamonici, O, R. (1996) Differences in interferon α and β signaling: interferon β selectively induces the interaction of the α and βL subunits of the type I interferon receptor. J. Biol. Chem. 271, 23630-23633
    • (1996) J. Biol. Chem , vol.271 , pp. 23630-23633
    • Platanias, L.C.1    Uddin, S.2    Domanski, P.3    Colamonici, O.R.4
  • 37
    • 0033573957 scopus 로고    scopus 로고
    • Formation of a uniquely stable type I interferon receptor complex by interferon β is dependent upon particular interactions between interferon β and its receptor and independent of tyrosine phosphorylation
    • Russell-Harde, D., Wagner, T. C., Perez, H. D. and Croze, E. (1999) Formation of a uniquely stable type I interferon receptor complex by interferon β is dependent upon particular interactions between interferon β and its receptor and independent of tyrosine phosphorylation. Biochem. Biophys. Res. Commun. 255, 539-544
    • (1999) Biochem. Biophys. Res. Commun , vol.255 , pp. 539-544
    • Russell-Harde, D.1    Wagner, T.C.2    Perez, H.D.3    Croze, E.4
  • 38
    • 0028969961 scopus 로고
    • Intracellular trafficking of epidermal growth factor family ligands is directly influenced by the pH sensitivity of the receptor/ligand interaction
    • French, A. R., Tadaki, D. K., Niyogi, S. K. and Lauffenburger, D. A. (1995) Intracellular trafficking of epidermal growth factor family ligands is directly influenced by the pH sensitivity of the receptor/ligand interaction. J. Biol. Chem. 270, 4334-4340
    • (1995) J. Biol. Chem , vol.270 , pp. 4334-4340
    • French, A.R.1    Tadaki, D.K.2    Niyogi, S.K.3    Lauffenburger, D.A.4
  • 39
    • 0032577487 scopus 로고    scopus 로고
    • Alternative intracellular routing of ErbB receptors may determine signaling potency
    • Waterman, H., Sabanai, I., Geiger, B. and Yarden, Y. (1998) Alternative intracellular routing of ErbB receptors may determine signaling potency. J. Biol. Chem. 273, 13819-13827
    • (1998) J. Biol. Chem , vol.273 , pp. 13819-13827
    • Waterman, H.1    Sabanai, I.2    Geiger, B.3    Yarden, Y.4
  • 41
    • 0242351936 scopus 로고    scopus 로고
    • The odd couple: Signal transduction and endocytosis
    • Teis, D. and Huber, L. A. (2003) The odd couple: signal transduction and endocytosis. Cell. Mol. Life Sci. 60, 2020-2033
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 2020-2033
    • Teis, D.1    Huber, L.A.2
  • 42
    • 0037598870 scopus 로고    scopus 로고
    • Distinct endocytic pathways regulate TGF-β receptor signalling and turnover
    • Di Guglielmo, G. M., Le Roy, C., Goodfellow, A. F. and Wrana, J. L. (2003) Distinct endocytic pathways regulate TGF-β receptor signalling and turnover. Nat. Cell. Biol. 5, 410-421
    • (2003) Nat. Cell. Biol , vol.5 , pp. 410-421
    • Di Guglielmo, G.M.1    Le Roy, C.2    Goodfellow, A.F.3    Wrana, J.L.4
  • 43
    • 0034733672 scopus 로고    scopus 로고
    • Cross talk between interferon-γ and -α/β signaling components in caveolar membrane domains
    • Takaoka, A., Mitani, Y., Suemori, H., Sato, M., Yokochi, T., Noguchi, S., Tanaka, N. and Taniguchi, T. (2000) Cross talk between interferon-γ and -α/β signaling components in caveolar membrane domains. Science 288, 2357-2360
    • (2000) Science , vol.288 , pp. 2357-2360
    • Takaoka, A.1    Mitani, Y.2    Suemori, H.3    Sato, M.4    Yokochi, T.5    Noguchi, S.6    Tanaka, N.7    Taniguchi, T.8
  • 44
    • 33745626171 scopus 로고    scopus 로고
    • Stat-mediated signaling induced by type I and type II interferons (IFNs) is differentially controlled through lipid microdomain association and clathrin-dependent endocytosis of IFN receptors
    • Marchetti, M., Monier, M. N., Fradagrada, A., Mitchell, K., Baychelier, F., Eid, P., Johannes, L. and Lamaze, C. (2006) Stat-mediated signaling induced by type I and type II interferons (IFNs) is differentially controlled through lipid microdomain association and clathrin-dependent endocytosis of IFN receptors. Mol. Biol. Cell 17, 2896-2909
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2896-2909
    • Marchetti, M.1    Monier, M.N.2    Fradagrada, A.3    Mitchell, K.4    Baychelier, F.5    Eid, P.6    Johannes, L.7    Lamaze, C.8


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