메뉴 건너뛰기




Volumn 10, Issue 2, 2000, Pages 83-92

Role of the cytoplasmic domains of the type I interferon receptor subunits in signaling

Author keywords

Domains; Interferon; Receptor; Signaling

Indexed keywords

CELL SURFACE RECEPTOR; CYTOKINE; INTERFERON RECEPTOR; TYROSINE;

EID: 0033925935     PISSN: 1044579X     EISSN: None     Source Type: Journal    
DOI: 10.1006/scbi.2000.0311     Document Type: Article
Times cited : (41)

References (101)
  • 3
    • 0026739463 scopus 로고
    • The interferon system. A bird's eye view of its biochemistry
    • Sen G C, Lengyel P. The interferon system. A bird's eye view of its biochemistry. J Biol Chem. 267:1992;5017-5020.
    • (1992) J Biol Chem , vol.267 , pp. 5017-5020
    • Sen, G.C.1    Lengyel, P.2
  • 4
    • 0032692405 scopus 로고    scopus 로고
    • The type I Interferon receptor: Structure, function and evolution of family business
    • Mogensen E, Lewerenz M, Reboul J, Lutfalla G, Uzé G. The type I Interferon receptor: structure, function and evolution of family business. J Interferon Cyt Res. 19:1999;1069-1098.
    • (1999) J Interferon Cyt Res , vol.19 , pp. 1069-1098
    • Mogensen, E.1    Lewerenz, M.2    Reboul, J.3    Lutfalla, G.4    Uzé, G.5
  • 6
    • 0028117299 scopus 로고
    • Cytokine therapeutics: Lessons from interferon α
    • Gutterman J U. Cytokine therapeutics: lessons from interferon α Proc Natl Acad Sci. 91:1994;1198-1205.
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 1198-1205
    • Gutterman, J.U.1
  • 7
    • 0029069145 scopus 로고
    • Transcriptional responses to polypeptide ligands: The JAK-STAT pathway
    • Schindler S, Darnell J JE. Transcriptional responses to polypeptide ligands: the JAK-STAT pathway. Annu Rev Biochem. 64:1995;621-651.
    • (1995) Annu Rev Biochem , vol.64 , pp. 621-651
    • Schindler, S.1    Darnell, J.J.2
  • 10
    • 85176673130 scopus 로고
    • A null mutation in the gene encoding a type I interferon receptor component eliminates antiproliferative and antiviral responses to interferons alpha and beta and alters macrophage responses
    • [published erratum appears in Apr 30
    • S, Y, Hwang, P, J, Hertzog, K, A, Holland, S, H, Sumarsono, M, J, Tymms, J, A, Hamilton, G, Whitty, I, Bertoncello, I, Kola, 1995, A null mutation in the gene encoding a type I interferon receptor component eliminates antiproliferative and antiviral responses to interferons alpha and beta and alters macrophage responses [published erratum appears in Proc Natl Acad Sci USA 1996 Apr 30;93(9):4519].
    • (1995) Proc Natl Acad Sci USA , vol.93 , Issue.9 , pp. 4519
    • Hwang, S.Y.1    Hertzog, P.J.2    Holland, K.A.3    Sumarsono, S.H.4    Tymms, M.J.5    Hamilton, J.A.6    Whitty, G.7    Bertoncello, I.8    Kola, I.9
  • 13
    • 0032489552 scopus 로고    scopus 로고
    • Identification of a domain in the β subunit of the Type I Interferon (IFN) receptor that exhibits a negative regulatory effect in the growth inhibitory action of Type I IFNs
    • Platanias L C, Domanski P, Nadeau O W, Yi T, Uddin S, Fish E, Neel B G, Colamonici O R. Identification of a domain in the β subunit of the Type I Interferon (IFN) receptor that exhibits a negative regulatory effect in the growth inhibitory action of Type I IFNs. J Biol Chem. 273:1998;5577-5581.
    • (1998) J Biol Chem , vol.273 , pp. 5577-5581
    • Platanias, L.C.1    Domanski, P.2    Nadeau, O.W.3    Yi, T.4    Uddin, S.5    Fish, E.6    Neel, B.G.7    Colamonici, O.R.8
  • 14
    • 0033559537 scopus 로고    scopus 로고
    • Dissociation between interferon- α -induced anti-viral and growth pathways
    • Arora T, Floyd-Smith G, Espy M J, Jelinek D. Dissociation between interferon- α -induced anti-viral and growth pathways. J Immunol. 162:1999;3289-3297.
    • (1999) J Immunol , vol.162 , pp. 3289-3297
    • Arora, T.1    Floyd-Smith, G.2    Espy, M.J.3    Jelinek, D.4
  • 16
    • 0027328343 scopus 로고
    • The alphas, betas, and kinases of cytokine receptor complexes
    • Stahl N, Yancopoulos G D. The alphas, betas, and kinases of cytokine receptor complexes. Cell. 74:1992;587-590.
    • (1992) Cell , vol.74 , pp. 587-590
    • Stahl, N.1    Yancopoulos, G.D.2
  • 17
    • 0028845212 scopus 로고
    • Cytokine receptor signaling
    • Ihle J N. Cytokine receptor signaling. Nature. 337:1995;591-594.
    • (1995) Nature , vol.337 , pp. 591-594
    • Ihle, J.N.1
  • 18
    • 0028117163 scopus 로고
    • Cytokine signal transduction
    • Kishimoto T, Taga T, Akira S. Cytokine signal transduction. Cell. 76:1994;253-262.
    • (1994) Cell , vol.76 , pp. 253-262
    • Kishimoto, T.1    Taga, T.2    Akira, S.3
  • 19
    • 0030046753 scopus 로고    scopus 로고
    • STATS:Signal transducers and activators of transcription
    • Ihle J E. STATS:Signal transducers and activators of transcription. Cell. 84:1996;331-334.
    • (1996) Cell , vol.84 , pp. 331-334
    • Ihle, J.E.1
  • 20
    • 0030840464 scopus 로고    scopus 로고
    • Stats and gene regulation
    • Darnell J EJ. Stats and gene regulation. Science. 277:1997;1630-1635.
    • (1997) Science , vol.277 , pp. 1630-1635
    • Darnell, J.E.1
  • 23
    • 0028025053 scopus 로고
    • Isolation and mapping of human chromosome 21 cDNA: Progress in constructing a chromosome 21 expression map
    • Cheng J-F, Boyartchuk V, Zhu Y. Isolation and mapping of human chromosome 21 cDNA: Progress in constructing a chromosome 21 expression map. Genomics. 23:1994;75-84.
    • (1994) Genomics , vol.23 , pp. 75-84
    • Cheng, J.-F.1    Boyartchuk, V.2    Zhu, Y.3
  • 24
    • 0027355586 scopus 로고
    • GART, SON, IFNAR, and CRF2-4 genes cluster on human chromosome 21 and mouse chromosome 16
    • Cheng S, Lutfalla G, Uze G, Chumakov I M, Gardiner K. GART, SON, IFNAR, and CRF2-4 genes cluster on human chromosome 21 and mouse chromosome 16. Mamm Genome. 4:1993;338-342.
    • (1993) Mamm Genome , vol.4 , pp. 338-342
    • Cheng, S.1    Lutfalla, G.2    Uze, G.3    Chumakov, I.M.4    Gardiner, K.5
  • 25
    • 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
  • 26
    • 0027325225 scopus 로고
    • Identification of a novel subunit of the type I interferon receptor localized to human chromosome 21
    • Colamonici O R, Domanski P. Identification of a novel subunit of the type I interferon receptor localized to human chromosome 21. J Biol Chem. 268:1993;10895-10899.
    • (1993) J Biol Chem , vol.268 , pp. 10895-10899
    • Colamonici, O.R.1    Domanski, P.2
  • 27
    • 0026462899 scopus 로고
    • Structural analysis of the human interferon gamma receptor: A small segment of the intracellular domain is specifically required for class I major histocompatibility complex antigen induction and antiviral activity
    • Cook J R, Jung V, Schwartz B, Wang P, Pestka S. Structural analysis of the human interferon gamma receptor: a small segment of the intracellular domain is specifically required for class I major histocompatibility complex antigen induction and antiviral activity. Proc Natl Acad Sci USA. 89:1992;11317-11321.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11317-11321
    • Cook, J.R.1    Jung, V.2    Schwartz, B.3    Wang, P.4    Pestka, S.5
  • 28
    • 0028173630 scopus 로고
    • Sublocalization of the human interferon-gamma receptor accessory factor gene and characterization of accessory factor activity by yeast artificial chromosomal fragmentation
    • Cook J R, Emanuel S L, Donnelly R J, Soh J, Mariano T M, Schwartz B, Rhee S, Pestka S. Sublocalization of the human interferon-gamma receptor accessory factor gene and characterization of accessory factor activity by yeast artificial chromosomal fragmentation. J Biol Chem. 269:1994;7013-7018.
    • (1994) J Biol Chem , vol.269 , pp. 7013-7018
    • Cook, J.R.1    Emanuel, S.L.2    Donnelly, R.J.3    Soh, J.4    Mariano, T.M.5    Schwartz, B.6    Rhee, S.7    Pestka, S.8
  • 30
    • 0027211970 scopus 로고
    • Effect of increased gene dosage expression on the alpha-interferon receptors in Down's syndrome
    • Gerdes A M, Horder M, Petersen P H, Bonnevie-Nielsen V. Effect of increased gene dosage expression on the alpha-interferon receptors in Down's syndrome. Biochim Biophys Acta. 1181:1993;135-140.
    • (1993) Biochim Biophys Acta , vol.1181 , pp. 135-140
    • Gerdes, A.M.1    Horder, M.2    Petersen, P.H.3    Bonnevie-Nielsen, V.4
  • 31
    • 0028271922 scopus 로고
    • A gene on human chromosome 21 located in the region 21q22.2 to 21q22.3 encodes a factor necessary for signal transduction and antiviral response to type I interferons
    • Hertzog P, Hwang S Y, Holland K A, Tymms M J, Iannello R, Kola I. A gene on human chromosome 21 located in the region 21q22.2 to 21q22.3 encodes a factor necessary for signal transduction and antiviral response to type I interferons. J Biol Chem. 269:1994;14088-14093.
    • (1994) J Biol Chem , vol.269 , pp. 14088-14093
    • Hertzog, P.1    Hwang, S.Y.2    Holland, K.A.3    Tymms, M.J.4    Iannello, R.5    Kola, I.6
  • 32
    • 0030774938 scopus 로고    scopus 로고
    • A type I interferon signaling factor, ISF21, encoded on chromosome 21 is distinct from receptor components and their down-regulation and is necessary for transcriptional activation of interferon-regulated genes
    • Holland K A, Owczarek C M, Hwang S Y, Tymms M J, Constantinescu S N, Pfeffer L W, Kola I, Hertzog P J. A type I interferon signaling factor, ISF21, encoded on chromosome 21 is distinct from receptor components and their down-regulation and is necessary for transcriptional activation of interferon-regulated genes. J Biol Chem. 272:1997;21045-21051.
    • (1997) J Biol Chem , vol.272 , pp. 21045-21051
    • Holland, K.A.1    Owczarek, C.M.2    Hwang, S.Y.3    Tymms, M.J.4    Constantinescu, S.N.5    Pfeffer, L.W.6    Kola, I.7    Hertzog, P.J.8
  • 33
  • 34
    • 0027232965 scopus 로고
    • A new member of the cytokine receptor gene family maps on chromosome 21 at less than 35 kb from IFNAR
    • Lutfalla G, Gardiner K, Uzé G. A new member of the cytokine receptor gene family maps on chromosome 21 at less than 35 kb from IFNAR. Genomics. 16:1993;366-373.
    • (1993) Genomics , vol.16 , pp. 366-373
    • Lutfalla, G.1    Gardiner, K.2    Uzé, G.3
  • 35
    • 0029097828 scopus 로고
    • Three distinc loci on human chromosome 21 contribute to intereferon- α / β responsiveness
    • Raz r, Cheung K, Ling L, Levy D E. Three distinc loci on human chromosome 21 contribute to intereferon- α / β responsiveness. Somatic Cell and Mol Genet. 21:1995;139-145.
    • (1995) Somatic Cell and Mol Genet , vol.21 , pp. 139-145
    • Raz, R.1    Cheung, K.2    Ling, L.3    Levy, D.E.4
  • 36
    • 0017232189 scopus 로고
    • Antibodies to a cell-surface component coded by human chromosome 21 inhibit action of interferon
    • Revel M, Bash D, Ruddle F H. Antibodies to a cell-surface component coded by human chromosome 21 inhibit action of interferon. Nature (London). 260:1976;139-141.
    • (1976) Nature (London) , vol.260 , pp. 139-141
    • Revel, M.1    Bash, D.2    Ruddle, F.H.3
  • 38
    • 0027292430 scopus 로고
    • Identification of a yeast artificial chromosome clone encoding an accessory factor for the human interferon gamma receptor: Evidence for multiple accessory factors
    • Soh J, Donnelly R J, Mariano T M, Cook J R, Schwartz B, Pestka S. Identification of a yeast artificial chromosome clone encoding an accessory factor for the human interferon gamma receptor: evidence for multiple accessory factors. Proc Natl Acad Sci. 90:1993;8737-8741.
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 8737-8741
    • Soh, J.1    Donnelly, R.J.2    Mariano, T.M.3    Cook, J.R.4    Schwartz, B.5    Pestka, S.6
  • 39
    • 0017229444 scopus 로고
    • Chromosome 21 and the cell growth inhibitory effect of human interferon preparations
    • Tan Y H. Chromosome 21 and the cell growth inhibitory effect of human interferon preparations. Nature (London). 260:1976;141-143.
    • (1976) Nature (London) , vol.260 , pp. 141-143
    • Tan, Y.H.1
  • 40
    • 0016210247 scopus 로고
    • Human chromosome 21 dosage: Effect on the expression of the interferon induced antiviral state
    • Tan Y H, Schneider E L, Tischfield J, Epstein C J, Ruddle F H. Human chromosome 21 dosage: effect on the expression of the interferon induced antiviral state. Science. 186:1974;61-63.
    • (1974) Science , vol.186 , pp. 61-63
    • Tan, Y.H.1    Schneider, E.L.2    Tischfield, J.3    Epstein, C.J.4    Ruddle, F.H.5
  • 41
    • 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
  • 42
    • 0029148972 scopus 로고
    • Cloning and expression of a long form of the β subunit of the interferon α receptor that is required for interferon signaling
    • Domanski P, Witte M, Kellum M, Menachen R, Larner A, Pitha-Rowe P, Colamonici O R. Cloning and expression of a long form of the β subunit of the interferon α receptor that is required for interferon 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    Menachen, R.4    Larner, A.5    Pitha-Rowe, P.6    Colamonici, O.R.7
  • 45
    • 0025015138 scopus 로고
    • Genetic transfer of a functional human interferon receptor into mouse cells: Cloning and expression of its cDNA
    • Uzé G, Lutfalla G, Gresser I. Genetic transfer of a functional human interferon receptor into mouse cells: cloning and expression of its cDNA. Cell. 60:1990;225-234.
    • (1990) Cell , vol.60 , pp. 225-234
    • Uzé, G.1    Lutfalla, G.2    Gresser, I.3
  • 46
    • 0025102756 scopus 로고
    • Haemopoietic receptors and helical cytokines
    • Bazan J F. Haemopoietic receptors and helical cytokines. Immunol Today. 11:1990;350-354.
    • (1990) Immunol Today , vol.11 , pp. 350-354
    • Bazan, J.F.1
  • 47
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • Bazan J F. Structural design and molecular evolution of a cytokine receptor superfamily. Proc Natl Acad Sci USA. 87:1990;6934-6938.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 48
    • 0025356737 scopus 로고
    • Shared architecture of hormone binding domains in type I and II interferon receptors
    • Bazan J F. Shared architecture of hormone binding domains in type I and II interferon receptors. Cell. 61:1990;753-754.
    • (1990) Cell , vol.61 , pp. 753-754
    • Bazan, J.F.1
  • 49
    • 0024469936 scopus 로고
    • A novel family of growth factors receptors: A common binding domain in the growth hormone, prolactin, erythropoietin and IL-6 receptors, and p75 IL-2 receptor β -chain
    • Bazan J F. A novel family of growth factors receptors: A common binding domain in the growth hormone, prolactin, erythropoietin and IL-6 receptors, and p75 IL-2 receptor β -chain. Biochem Biophys Res Commun. 164:1989;788-795.
    • (1989) Biochem Biophys Res Commun , vol.164 , pp. 788-795
    • Bazan, J.F.1
  • 50
    • 0029863420 scopus 로고    scopus 로고
    • Molecular characterization of an interferon- α receptor 1 subunit (IFNaR1) domain required for TYK2 binding and signal transduction
    • Yan H, Krishnan K, Lim J TE, Contillo L G, Krolewski J J. Molecular characterization of an interferon- α receptor 1 subunit (IFNaR1) domain required for TYK2 binding and signal transduction. Mol Cel Biol. 16:1996;2074-2082.
    • (1996) Mol Cel Biol , vol.16 , pp. 2074-2082
    • Yan, H.1    Krishnan, K.2    Lim, J.T.3    Contillo, L.G.4    Krolewski, J.J.5
  • 53
    • 0029961502 scopus 로고    scopus 로고
    • A negative regulatory region in the intracellular domain of the human interferon-alpha receptor
    • Gibbs V C, Takahashi M, Aguet M, Chuntharapai A. A negative regulatory region in the intracellular domain of the human interferon-alpha receptor. J Biol Chem. 271:1996;28710-22876.
    • (1996) J Biol Chem , vol.271 , pp. 28710-22876
    • Gibbs, V.C.1    Takahashi, M.2    Aguet, M.3    Chuntharapai, A.4
  • 54
    • 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 alpha/beta 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, Pfeffer L M. The antiviral action of interferon is potentiated by removal of the conserved IRTAM domain of the IFNAR1 chain of the interferon alpha/beta receptor: effects on JAK-STAT activation and receptor down-regulation. Virology. 242:1998;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
  • 55
    • 0028972719 scopus 로고
    • Differential regulation of the alpha/beta interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1
    • David M, Chen H E, Goelz S, Larner A C, Neel B G. Differential regulation of the alpha/beta interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol Cell Biol. 15:1995;7050-7058.
    • (1995) Mol Cell Biol , vol.15 , pp. 7050-7058
    • David, M.1    Chen, H.E.2    Goelz, S.3    Larner, A.C.4    Neel, B.G.5
  • 56
    • 0030038677 scopus 로고    scopus 로고
    • The SH2 domain-containing tyrosine phosphatase PTP1D is required for interferon alpha/beta-induced gene expression
    • David M, Zhou G, Pine R, Dixon J E, Larner A C. The SH2 domain-containing tyrosine phosphatase PTP1D is required for interferon alpha/beta-induced gene expression. J Biol Chem. 271:1996;15862-15865.
    • (1996) J Biol Chem , vol.271 , pp. 15862-15865
    • David, M.1    Zhou, G.2    Pine, R.3    Dixon, J.E.4    Larner, A.C.5
  • 57
    • 0032980574 scopus 로고    scopus 로고
    • Shp-2 tyrosine phosphatase functionsas anegative regulator of the interferon-stimulated Jak-Stat pathway
    • You M, Yu D, Feng G. Shp-2 tyrosine phosphatase functionsas anegative regulator of the interferon-stimulated Jak-Stat pathway. Mol Cell Biol. 19:1999;2416-2424.
    • (1999) Mol Cell Biol , vol.19 , pp. 2416-2424
    • You, M.1    Yu, D.2    Feng, G.3
  • 58
    • 0029133702 scopus 로고
    • Requirement for MAP kinase (ERK2) activity in interferon alpha- And interferon beta-stimulated gene expression through STAT proteins
    • David M, Petricoin E, 3rd, Benjamin C, Pine R, Weber M J, Larner A C. Requirement for MAP kinase (ERK2) activity in interferon alpha- and interferon beta-stimulated gene expression through STAT proteins. Science. 269:1995;1721-1723.
    • (1995) Science , vol.269 , pp. 1721-1723
    • David, M.1    Petricoin E. III2    Benjamin, C.3    Pine, R.4    Weber, M.J.5    Larner, A.C.6
  • 59
    • 0029965272 scopus 로고    scopus 로고
    • Activation of protein kinase A inhibits interferon induction of the Jak/Stat pathway in U266 cells
    • David M, Petricoin E, 3rd, Larner A C. Activation of protein kinase A inhibits interferon induction of the Jak/Stat pathway in U266 cells. J Biol Chem. 271:1996;4585-4588.
    • (1996) J Biol Chem , vol.271 , pp. 4585-4588
    • David, M.1    Petricoin E. III2    Larner, A.C.3
  • 60
    • 0033527566 scopus 로고    scopus 로고
    • Catalytically Active Tyk2 Is Essential for Interferon- β mediated phosphorylation of Stat3 in interferonα receptor 1 (IFNAR1) but not for activation of phospho inositol 3-kinase
    • Rani M RS, Leaman D W, Han Y, Leung S, Croze E, Fish E N, Wolfman A, Ransohoff R M. Catalytically Active Tyk2 Is Essential for Interferon- β mediated phosphorylation of Stat3 in interferonα receptor 1 (IFNAR1) but not for activation of phospho inositol 3-kinase. J Biol Chem. 274:1999;32507-32511.
    • (1999) J Biol Chem , vol.274 , pp. 32507-32511
    • Rani, M.R.1    Leaman, D.W.2    Han, Y.3    Leung, S.4    Croze, E.5    Fish, E.N.6    Wolfman, A.7    Ransohoff, R.M.8
  • 61
    • 0033609161 scopus 로고    scopus 로고
    • The intracellular domain of interferon-alpha receptor 2c (IFN-alphaR2c) chain is responsible for Stat activation
    • Kotenko S V, Izotova L S, Mirochnitchenko O V, Lee C, Pestka S. The intracellular domain of interferon-alpha receptor 2c (IFN-alphaR2c) chain is responsible for Stat activation. Proc Natl Acad Sci. 96:1999;5007-5012.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 5007-5012
    • Kotenko, S.V.1    Izotova, L.S.2    Mirochnitchenko, O.V.3    Lee, C.4    Pestka, S.5
  • 62
    • 0027055589 scopus 로고
    • Interferon α induces rapid tyrosine phosphorylation of the α subunit of its receptor
    • Platanias L C, Colamonici O R. Interferon α induces rapid tyrosine phosphorylation of the α subunit of its receptor. J Biol Chem. 267:1992;24053-24057.
    • (1992) J Biol Chem , vol.267 , pp. 24053-24057
    • Platanias, L.C.1    Colamonici, O.R.2
  • 63
    • 0028107016 scopus 로고
    • Role of interferon alpha/beta receptor chain 1 in the structure and transmembrane signaling of the interferon alpha/beta receptor complex
    • Constantinescu S N, Croze E, Wang C, Murti A, Basu L, Mullersman J E, Pfeffer L M. Role of interferon alpha/beta receptor chain 1 in the structure and transmembrane signaling of the interferon alpha/beta 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
  • 64
    • 0029670220 scopus 로고    scopus 로고
    • Phosphorylated interferon- α 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, Gupta S, Lim J TE, Schreiber R, Schindler C, Krolewski J J. Phosphorylated interferon- α receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa Stat2 protein. EMBO J. 15:1996;1064-1074.
    • (1996) EMBO J , vol.15 , pp. 1064-1074
    • Yan, H.1    Krishnan, K.2    Greenlund, A.3    Gupta, S.4    Lim, J.T.5    Schreiber, R.6    Schindler, C.7    Krolewski, J.J.8
  • 65
    • 0030945179 scopus 로고    scopus 로고
    • Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor for signaling
    • Li X, Leung S, Kerr I M, Stark G S. Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor for signaling. Mol Cell Biol. 17:1997;2048-2056.
    • (1997) Mol Cell Biol , vol.17 , pp. 2048-2056
    • Li, X.1    Leung, S.2    Kerr, I.M.3    Stark, G.S.4
  • 67
    • 0030999696 scopus 로고    scopus 로고
    • Stat3 as an adapter to couple phosphatidylinositol 3-kinase to the IFNAR1 chain of the type I interferon receptor
    • Pfeffer L M, Mullersman J E, Pfeffer S R, Murti A, Shi W, Yang C H. Stat3 as an adapter to couple phosphatidylinositol 3-kinase to the IFNAR1 chain of the type I interferon receptor. Science. 276:1997;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
  • 68
    • 0033548075 scopus 로고    scopus 로고
    • The proximal tyrosines of the cytoplasmic domain of the β chain of the type I interferon receptor are essential for signal transducer and activator of transcription (Stat) 2 activation
    • Nadeau O W, Usacheva A, Uddin S, Platanias L P, Pitha P, Raz R, Levy D, Majchrzak B, Fish E, Colamonici O R. The proximal tyrosines of the cytoplasmic domain of the β chain of the type I interferon receptor are essential for signal transducer and activator of transcription (Stat) 2 activation. J Biol Chem. 274:1999;4045-4052.
    • (1999) J Biol Chem , vol.274 , pp. 4045-4052
    • Nadeau, O.W.1    Usacheva, A.2    Uddin, S.3    Platanias, L.P.4    Pitha, P.5    Raz, R.6    Levy, D.7    Majchrzak, B.8    Fish, E.9    Colamonici, O.R.10
  • 69
    • 0030671276 scopus 로고    scopus 로고
    • A region of the β subunit of the interferon a receptor different from the box 1 interacts with Jak1 and is sufficient to activate the Jak-Stat pathway and induce an antiviral state
    • Domanski P, Nadeau O W, Fish E, Kellum M, Platanias L C, Pitha P, Colamonici O R. A region of the β subunit of the interferon a receptor different from the box 1 interacts with Jak1 and is sufficient to activate the Jak-Stat pathway and induce an antiviral state. J Biol Chem. 272:1997;26388-26393.
    • (1997) J Biol Chem , vol.272 , pp. 26388-26393
    • Domanski, P.1    Nadeau, O.W.2    Fish, E.3    Kellum, M.4    Platanias, L.C.5    Pitha, P.6    Colamonici, O.R.7
  • 70
    • 0032488662 scopus 로고    scopus 로고
    • Differential Use of Distinct Domains of the Type I Interferon (IFN) Receptor β Chain Establishes Signaling Specificity for IFN α 2 and IFN β
    • Domanski P, Platanias L C, Fish E, Kellum M, Pitha P, Colamonici O R. Differential Use of Distinct Domains of the Type I Interferon (IFN) Receptor β Chain Establishes Signaling Specificity for IFN α 2 and IFN β J Biol Chem. 273:1998;3144-3147.
    • (1998) J Biol Chem , vol.273 , pp. 3144-3147
    • Domanski, P.1    Platanias, L.C.2    Fish, E.3    Kellum, M.4    Pitha, P.5    Colamonici, O.R.6
  • 71
    • 0028360574 scopus 로고
    • Tyrosine phosphorylation of the α and β subunits of the Type I interferon receptor. Interferon β selectively induces tyrosine phosphorylation of an α -subunit associated protein
    • Platanias L C, Uddin S, Colamonici O R. Tyrosine phosphorylation of the α and β subunits of the Type I interferon receptor. Interferon β selectively induces tyrosine phosphorylation of an α -subunit associated protein. J Biol Chem. 269:1994;17761-17764.
    • (1994) J Biol Chem , vol.269 , pp. 17761-17764
    • Platanias, L.C.1    Uddin, S.2    Colamonici, O.R.3
  • 72
    • 0029846515 scopus 로고    scopus 로고
    • Differences in interferon α and β signaling. Interferon β selectively induces the interaction of the α and β L subunits of the Type I interferon receptor
    • Platanias L C, Uddin S, Domanski P, Colamonici O R. Differences in interferon α and β signaling. Interferon β selectively induces the interaction of the α and β L subunits of the Type I interferon receptor. J Biol Chem. 271:1996;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
  • 73
    • 0030468346 scopus 로고    scopus 로고
    • The human type I interferon receptor. Identification of the interferon beta-specific receptor-associated phosphoprotein
    • Croze E, Russell-Harde D, Wagner T C, Pu H, Pfeffer L M, Perez H D. The human type I interferon receptor. Identification of the interferon beta-specific receptor-associated phosphoprotein. J Biol Chem. 271:1996;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    Pfeffer, L.M.5    Perez, H.D.6
  • 75
    • 0028175454 scopus 로고
    • Ligand-induced IFN γ receptor tyrosine phosphorylation couples the receptor to its signal transduction pathway system (p91)
    • Greenlund A C, Farrar M A, Viviano B L, Schreiber R D. Ligand-induced IFN γ receptor tyrosine phosphorylation couples the receptor to its signal transduction pathway system (p91). Embo J. 13:1994;1591-1600.
    • (1994) Embo J , vol.13 , pp. 1591-1600
    • Greenlund, A.C.1    Farrar, M.A.2    Viviano, B.L.3    Schreiber, R.D.4
  • 76
    • 0028979707 scopus 로고
    • Stat recruitment by tyrosine-phosphorylated cytokine receptors: An ordered reversible affinity-driven process
    • Greenlund A C, Morales M O, Viviano B L, Yan H, Krolewski J, Schreiber R D. Stat recruitment by tyrosine-phosphorylated cytokine receptors: an ordered reversible affinity-driven process. Immunity. 2:1995;677-687.
    • (1995) Immunity , vol.2 , pp. 677-687
    • Greenlund, A.C.1    Morales, M.O.2    Viviano, B.L.3    Yan, H.4    Krolewski, J.5    Schreiber, R.D.6
  • 77
    • 0028931604 scopus 로고
    • Choice of Stats and other substrates specified by modular tyrosine-based motifs in cytokine receptors
    • Stahl N, Farruggella T J, Boulton T J, Zhong Z, Darnell J JE, Yancopoulos G D. Choice of Stats and other substrates specified by modular tyrosine-based motifs in cytokine receptors. Science. 267:1995;1349-1353.
    • (1995) Science , vol.267 , pp. 1349-1353
    • Stahl, N.1    Farruggella, T.J.2    Boulton, T.J.3    Zhong, Z.4    Darnell, J.J.5    Yancopoulos, G.D.6
  • 78
    • 0028148055 scopus 로고
    • Acute phase response factor and additional members of the interferon-stimulated gene factor 3 family integrate diverse signals from cytokines, interferons, and growth factors
    • Raz R, Durbin J E, Levy D E. Acute phase response factor and additional members of the interferon-stimulated gene factor 3 family integrate diverse signals from cytokines, interferons, and growth factors. J Biol Chem. 269:1994;24391-24395.
    • (1994) J Biol Chem , vol.269 , pp. 24391-24395
    • Raz, R.1    Durbin, J.E.2    Levy, D.E.3
  • 79
    • 0032526097 scopus 로고    scopus 로고
    • Interferon-alpha activates signal transducers and activators of transcription 5 and 6 in Daudi cells
    • Fasler-Kan E, Pansky A, Wiederkehr M, Battegay M, Heim M H. Interferon-alpha activates signal transducers and activators of transcription 5 and 6 in Daudi cells. Eur J Biochem. 254:1998;514-519.
    • (1998) Eur J Biochem , vol.254 , pp. 514-519
    • Fasler-Kan, E.1    Pansky, A.2    Wiederkehr, M.3    Battegay, M.4    Heim, M.H.5
  • 80
    • 0033560095 scopus 로고    scopus 로고
    • Interferon-alpha activates multiple STAT proteins and upregulates proliferation-associated IL-2Ralpha, c-myc, and pim-1 genes in human T cells
    • Matikainen S, Sareneva T, Ronni T, Lehtonen A, Koskinen P J, Julkunen I. Interferon-alpha activates multiple STAT proteins and upregulates proliferation-associated IL-2Ralpha, c-myc, and pim-1 genes in human T cells. Blood. 93:1999;1980-1991.
    • (1999) Blood , vol.93 , pp. 1980-1991
    • Matikainen, S.1    Sareneva, T.2    Ronni, T.3    Lehtonen, A.4    Koskinen, P.J.5    Julkunen, I.6
  • 85
    • 0029937270 scopus 로고    scopus 로고
    • Impaired IL-12 responses and enhancement of Th2 cells in Stat4-deficient mice
    • Kaplan M H, Sun Y-L, Hoey T, Grusby M J. Impaired IL-12 responses and enhancement of Th2 cells in Stat4-deficient mice. Nature. 382:1996;174-177.
    • (1996) Nature , vol.382 , pp. 174-177
    • Kaplan, M.H.1    Sun, Y.-L.2    Hoey, T.3    Grusby, M.J.4
  • 88
    • 0028982917 scopus 로고
    • Interferon- α engages the insulin receptor substrate-1 to associate with the phosphatidylinositol 3'-kinase
    • Uddin S, Yenush L, Sun X-J, Sweet M E, White M F, Platanias L C. Interferon- α engages the insulin receptor substrate-1 to associate with the phosphatidylinositol 3'-kinase. J Biol Chem. 270:1995;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
  • 89
    • 0031093545 scopus 로고    scopus 로고
    • Activation of the phosphatidyl inositol 3 kinase serine kinase by interferon α
    • Uddin S, Fish E N, Sher D A, Gardciola C, White M F, Platanias L C. Activation of the phosphatidyl inositol 3 kinase serine kinase by interferon α J Immunol. 158:1997;2390-2397.
    • (1997) J Immunol , vol.158 , pp. 2390-2397
    • Uddin, S.1    Fish, E.N.2    Sher, D.A.3    Gardciola, C.4    White, M.F.5    Platanias, L.C.6
  • 90
    • 0033604577 scopus 로고    scopus 로고
    • Signaling by distinct classes of phosphoinositide 3-kinases
    • Vanhaesebroeck B, Waterfield M D. Signaling by distinct classes of phosphoinositide 3-kinases. Exp Cell Res. 253:1999;239-254.
    • (1999) Exp Cell Res , vol.253 , pp. 239-254
    • Vanhaesebroeck, B.1    Waterfield, M.D.2
  • 91
    • 0032727032 scopus 로고    scopus 로고
    • Signaling pathways activated by interferons
    • Platanias L C, Fish E N. Signaling pathways activated by interferons. Exp Hematol. 27:1999;1583-1592.
    • (1999) Exp Hematol , vol.27 , pp. 1583-1592
    • Platanias, L.C.1    Fish, E.N.2
  • 92
    • 0033551070 scopus 로고    scopus 로고
    • New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway
    • Cantley L C, Neel B G. New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc Natl Acad Sci. 96:1999;4240-4205.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 4240-4205
    • Cantley, L.C.1    Neel, B.G.2
  • 93
    • 0033537926 scopus 로고    scopus 로고
    • Phosphatidylinositol phosphate kinases, a multifaceted family of signaling enzymes
    • Anderson R A, Boronenkov I V, Doughman S D, Kunz J, Loijens J C. Phosphatidylinositol phosphate kinases, a multifaceted family of signaling enzymes. J Biol Chem. 274:1999;9907-9910.
    • (1999) J Biol Chem , vol.274 , pp. 9907-9910
    • Anderson, R.A.1    Boronenkov, I.V.2    Doughman, S.D.3    Kunz, J.4    Loijens, J.C.5
  • 94
    • 0033515592 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases and their FYVE domain-containing effectors as regulators of vacuolar/lysosomal membrane trafficking pathways
    • Wurmser A E, Gary J D, Emr S D. Phosphoinositide 3-kinases and their FYVE domain-containing effectors as regulators of vacuolar/lysosomal membrane trafficking pathways. J Biol Chem. 274:1999;9129-9132.
    • (1999) J Biol Chem , vol.274 , pp. 9129-9132
    • Wurmser, A.E.1    Gary, J.D.2    Emr, S.D.3
  • 95
    • 0033605718 scopus 로고    scopus 로고
    • The role of phosphoinositide 3-kinase lipid products in cell function
    • Rameh L E, Cantley L C. The role of phosphoinositide 3-kinase lipid products in cell function. J Biol Chem. 274:1999;8347-8350.
    • (1999) J Biol Chem , vol.274 , pp. 8347-8350
    • Rameh, L.E.1    Cantley, L.C.2
  • 96
    • 0032497832 scopus 로고    scopus 로고
    • Structure and function of phosphoinositide 3-kinases
    • Wymann M P, Pirola L. Structure and function of phosphoinositide 3-kinases. Biochim Biophys Acta. 1436:1998;127-150.
    • (1998) Biochim Biophys Acta , vol.1436 , pp. 127-150
    • Wymann, M.P.1    Pirola, L.2
  • 98
    • 0030865679 scopus 로고    scopus 로고
    • 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-alpha receptors
    • Uddin S, Fish E N, Sher D, Gardziola C, Colamonici O R, Kellum M, Pitha P M, White M F, Platanias L C. 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-alpha receptors. Blood. 90:1997;2574-2582.
    • (1997) Blood , vol.90 , pp. 2574-2582
    • Uddin, S.1    Fish, E.N.2    Sher, D.3    Gardziola, C.4    Colamonici, O.R.5    Kellum, M.6    Pitha, P.M.7    White, M.F.8    Platanias, L.C.9
  • 99
    • 0030827881 scopus 로고    scopus 로고
    • Janus kinase-dependent activation of insulin receptor substrate 1 in response to interleukin-4, oncostatin M, and the interferons
    • Burfoot M S, Rogers N C, Watling D, Smith J M, Pons S, Paonessaw G, Pellegrini S, White M F, Kerr I M. Janus kinase-dependent activation of insulin receptor substrate 1 in response to interleukin-4, oncostatin M, and the interferons. J Biol Chem. 272:1997;24183-24190.
    • (1997) J Biol Chem , vol.272 , pp. 24183-24190
    • Burfoot, M.S.1    Rogers, N.C.2    Watling, D.3    Smith, J.M.4    Pons, S.5    Paonessaw, G.6    Pellegrini, S.7    White, M.F.8    Kerr, I.M.9
  • 100
    • 0030043596 scopus 로고    scopus 로고
    • The type I interferon receptor mediates tyrosine phosphorylation of insulin receptor substrate 2
    • Platanias L C, Uddin S, Yetter A, Sun X-J, White M F. The type I interferon receptor mediates tyrosine phosphorylation of insulin receptor substrate 2. J Biol Chem. 271:1996;278-282.
    • (1996) J Biol Chem , vol.271 , pp. 278-282
    • Platanias, L.C.1    Uddin, S.2    Yetter, A.3    Sun, X.-J.4    White, M.F.5
  • 101
    • 0029117304 scopus 로고
    • Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation
    • Wen Z, Zhong Z, Darnell J JE. Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation. Cell. 82:1995;241-250.
    • (1995) Cell , vol.82 , pp. 241-250
    • Wen, Z.1    Zhong, Z.2    Darnell, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.