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Volumn 242, Issue 1, 1998, Pages 14-21

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

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA INTERFERON RECEPTOR; INTERFERON;

EID: 0032030169     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1997.9002     Document Type: Article
Times cited : (25)

References (27)
  • 1
    • 0020412790 scopus 로고
    • Interaction of interferon with cellular receptors: Internalization and degradation of cell-bound interferon
    • Branca A. A., Faltynek C. R., D'Alessandro S. B., Baglioni C. Interaction of interferon with cellular receptors: Internalization and degradation of cell-bound interferon. J. Biol. Chem. 257:1982;13291-13296.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13291-13296
    • Branca, A.A.1    Faltynek, C.R.2    D'Alessandro, S.B.3    Baglioni, C.4
  • 2
    • 0028225872 scopus 로고
    • Knockout and reconstitution of a functional human type I interferon receptor complex
    • Cleary C. M., Donnelly R. J., Soh J., Mariano T. M., Pestka S. Knockout and reconstitution of a functional human type I interferon receptor complex. J. Biol. Chem. 269:1994;18747-18749.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18747-18749
    • Cleary, C.M.1    Donnelly, R.J.2    Soh, J.3    Mariano, T.M.4    Pestka, S.5
  • 4
    • 0028277910 scopus 로고
    • Complementation of the IFNα response in resistant cells by expression of the cloned subunit of the IFNα receptor: Central role of this subunit in IFNα signalling
    • Colamonici O. R., Porterfield B., Domanski P., Constantinescu S. N., Pfeffer L. M. Complementation of the IFNα response in resistant cells by expression of the cloned subunit of the IFNα receptor: Central role of this subunit in IFNα signalling. J. Biol. Chem. 269:1994b;9598-9602.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9598-9602
    • Colamonici, O.R.1    Porterfield, B.2    Domanski, P.3    Constantinescu, S.N.4    Pfeffer, L.M.5
  • 5
    • 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., Croze E., Wang C., Murti A., Basu L., Mullersman J. E., Pfeffer L. M. 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. 91:1994;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
  • 7
    • 0029148972 scopus 로고
    • Cloning and expression of a long form of the β subunit of the interferon αβ receptor that is required for signaling
    • Domanski P., Witte M., Kellum M., Rubinstein M., Hackett R., Pitha P., Colamonici O. R. Cloning and expression of a long form of the β subunit of the interferon αβ receptor that is required for signaling. J. Biol. Chem. 270:1995;21606-21611.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21606-21611
    • Domanski, P.1    Witte, M.2    Kellum, M.3    Rubinstein, M.4    Hackett, R.5    Pitha, P.6    Colamonici, O.R.7
  • 8
    • 0026723419 scopus 로고
    • A transcription factor with SH2 and SH3 domains is directly activated by an interferon α-induced cytoplasmic protein tyrosine kinase(s)
    • Fu X.-Y. A transcription factor with SH2 and SH3 domains is directly activated by an interferon α-induced cytoplasmic protein tyrosine kinase(s). Cell. 70:1992;323-335.
    • (1992) Cell , vol.70 , pp. 323-335
    • Fu, X.-Y.1
  • 9
    • 0029961502 scopus 로고    scopus 로고
    • A negative regulatory region in the intracellular domain of the human interferon-α receptor
    • Gibbs V. C., Takahashi M., Aguet M., Chuntharapal A. A negative regulatory region in the intracellular domain of the human interferon-α receptor. J. Biol. Chem. 271:1996;28710-28716.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28710-28716
    • Gibbs, V.C.1    Takahashi, M.2    Aguet, M.3    Chuntharapal, A.4
  • 10
    • 0027055658 scopus 로고
    • Interferon-γ potentiates the antiviral actvity and the expression of interferon-stimulated genes induced by interferon-α in U-937 cells
    • Improta T., Pine R., Pfeffer L. M. Interferon-γ potentiates the antiviral actvity and the expression of interferon-stimulated genes induced by interferon-α in U-937 cells. J. Interferon Res. 12:1992;87-94.
    • (1992) J. Interferon Res. , vol.12 , pp. 87-94
    • Improta, T.1    Pine, R.2    Pfeffer, L.M.3
  • 11
    • 0027243120 scopus 로고
    • The use of retroviral vectors for gene transfer and expression
    • Miller A. D., Miller D. G., Garcia J. V., Lynch C. M. The use of retroviral vectors for gene transfer and expression. Methods Enzymol. 217:1993;581-599.
    • (1993) Methods Enzymol. , vol.217 , pp. 581-599
    • Miller, A.D.1    Miller, D.G.2    Garcia, J.V.3    Lynch, C.M.4
  • 12
    • 0026474672 scopus 로고
    • Specific antiviral activities of the human alpha interferons are determined at the level of receptor (IFNAR) structure
    • Mouchel-Viehl E., Lutfalla G., Mogensen K. E., Uze G. Specific antiviral activities of the human alpha interferons are determined at the level of receptor (IFNAR) structure. FEBS Lett. 313:1992;255-259.
    • (1992) FEBS Lett. , vol.313 , pp. 255-259
    • Mouchel-Viehl, E.1    Lutfalla, G.2    Mogensen, K.E.3    Uze, G.4
  • 14
    • 0028819186 scopus 로고
    • A novel cytoplasmic homology domain in interferon receptors
    • Mullersman J. E., Pfeffer L. M. A novel cytoplasmic homology domain in interferon receptors. Trends Biochem. Sci. 20:1994;55-56.
    • (1994) Trends Biochem. Sci. , vol.20 , pp. 55-56
    • Mullersman, J.E.1    Pfeffer, L.M.2
  • 15
    • 0028299340 scopus 로고
    • The human interferon α/β receptor: Characterization and molecular cloning
    • Novick D., Cohen B., Rubinstein M. The human interferon α/β receptor: Characterization and molecular cloning. Cell. 77:1994;391-400.
    • (1994) Cell , vol.77 , pp. 391-400
    • Novick, D.1    Cohen, B.2    Rubinstein, M.3
  • 16
    • 0025114430 scopus 로고
    • Interferon-α selectively activates the β isoform of protein kinase C through phosphatidylcholine hydrolysis
    • Pfeffer L. M., Strulovici B., Saltiel A. R. Interferon-α selectively activates the β isoform of protein kinase C through phosphatidylcholine hydrolysis. Proc. Natl. Acad. Sci. USA. 87:1990;6537-6541.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6537-6541
    • Pfeffer, L.M.1    Strulovici, B.2    Saltiel, A.R.3
  • 17
    • 0030977225 scopus 로고    scopus 로고
    • The short form of the interferon α/β receptor chain acts as a dominant negative for type I interferon action
    • Pfeffer L. M., Basu L., Pfeffer S. R., Yang C. H., Murti A., Russell-Harde D., Croze E. The short form of the interferon α/β receptor chain acts as a dominant negative for type I interferon action. J. Biol. Chemc. 272:1997a;11002-11005.
    • (1997) J. Biol. Chemc. , vol.272 , pp. 11002-11005
    • Pfeffer, L.M.1    Basu, L.2    Pfeffer, S.R.3    Yang, C.H.4    Murti, A.5    Russell-Harde, D.6    Croze, E.7
  • 18
    • 0030999696 scopus 로고    scopus 로고
    • The role of STAT3 as an adapter to couple phosphatidylinositol-3 kinase to the IFNAR-1 chain of the type I IFN receptor
    • Pfeffer L. M., Mullersman J. E., Pfeffer S. R., Murti A., Shi W., Yang C. H. The role of STAT3 as an adapter to couple phosphatidylinositol-3 kinase to the IFNAR-1 chain of the type I IFN receptor. Science. 276:1997b;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
  • 19
    • 0026741769 scopus 로고
    • Constitutive expression of an ISGF2/IRF1 transgene leads to interferon-independent activation of interferon-inducible genes and resistance to virus infection
    • Pine R. Constitutive expression of an ISGF2/IRF1 transgene leads to interferon-independent activation of interferon-inducible genes and resistance to virus infection. J. Virol. 66:1992;4470-4478.
    • (1992) J. Virol. , vol.66 , pp. 4470-4478
    • Pine, R.1
  • 20
    • 0028097932 scopus 로고
    • Tyrosine phosphorylated p91 binds to a single element in the ISGF2/IRF-1 promoter to mediate induction by IFNα and IFNγ, and is likely to autoregulate the p91 gene
    • Pine R., Canova A., Schindler C. Tyrosine phosphorylated p91 binds to a single element in the ISGF2/IRF-1 promoter to mediate induction by IFNα and IFNγ, and is likely to autoregulate the p91 gene. EMBO J. 13:1994;158-167.
    • (1994) EMBO J. , vol.13 , pp. 158-167
    • Pine, R.1    Canova, A.2    Schindler, C.3
  • 21
    • 0026770248 scopus 로고
    • Interferon-dependent tyrosine phosphorylation of a latent cytoplasmic transcription factor
    • Schindler C., Shuai K., Prezioso V. R., Darnell J. E. Interferon-dependent tyrosine phosphorylation of a latent cytoplasmic transcription factor. Science. 257:1992;809-813.
    • (1992) Science , vol.257 , pp. 809-813
    • Schindler, C.1    Shuai, K.2    Prezioso, V.R.3    Darnell, J.E.4
  • 22
    • 0025015138 scopus 로고
    • Genetic transfer of a functional human interferon α receptor into mouse cells: Cloning and expression of its cDNA
    • Uze G., Lutfalla G., Gresser I. Genetic transfer of a functional human interferon α receptor into mouse cells: Cloning and expression of its cDNA. Cell. 60:1990;225-234.
    • (1990) Cell , vol.60 , pp. 225-234
    • Uze, G.1    Lutfalla, G.2    Gresser, I.3
  • 23
    • 0026521423 scopus 로고
    • Behavior of a cloned murine α/β receptor expressed in homospecific or heterospecific background
    • Uze G., Lutfalla G., Bandu M.-T., Proudhon D., Mogensen K. Behavior of a cloned murine α/β receptor expressed in homospecific or heterospecific background. Proc. Natl. Acad. Sci. USA. 89:1992;4774-4778.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4774-4778
    • Uze, G.1    Lutfalla, G.2    Bandu, M.-T.3    Proudhon, D.4    Mogensen, K.5
  • 24
    • 0025639009 scopus 로고
    • The SIF binding element confers sis/PDGF inducibility onto the c-fos promoter
    • Wagner B. J., Hayes T. E., Hoban C. J., Cochran B. H. The SIF binding element confers sis/PDGF inducibility onto the c-fos promoter. EMBO J. 9:1990;4477-4484.
    • (1990) EMBO J. , vol.9 , pp. 4477-4484
    • Wagner, B.J.1    Hayes, T.E.2    Hoban, C.J.3    Cochran, B.H.4
  • 25
    • 0029670220 scopus 로고    scopus 로고
    • Phosphorylated interferonα receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein
    • Yan H., Krishnan K., Greenlund A. C., Gupta S., Lim J. T. E., Schreiber R. D., Schindler C. W., Krolewski J. J. Phosphorylated interferonα receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein. EMBO J. 15:1996a;1064-1074.
    • (1996) EMBO J. , vol.15 , pp. 1064-1074
    • Yan, H.1    Krishnan, K.2    Greenlund, A.C.3    Gupta, S.4    Lim, J.T.E.5    Schreiber, R.D.6    Schindler, C.W.7    Krolewski, J.J.8
  • 26
    • 0029863420 scopus 로고    scopus 로고
    • Molecular characterization of an alpha interferon receptor 1 subunit (IFNaR1) domain required for tyk2 binding and signal transduction
    • Yan H., Krishnan K., Lim J. T. E., Contillo L. G., Krolewski J. J. Molecular characterization of an alpha interferon receptor 1 subunit (IFNaR1) domain required for tyk2 binding and signal transduction. Mol. Cell. Biol. 16:1996b;2074-2082.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2074-2082
    • Yan, H.1    Krishnan, K.2    Lim, J.T.E.3    Contillo, L.G.4    Krolewski, J.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.