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Volumn 105, Issue 6 II, 2000, Pages 1063-1070

IL-4/IL-13 signaling beyond JAK/STAT

Author keywords

BCL 6; Cell signaling; Dok; Fes; IL 13; IL 4; Interleukins; IRS; SOCS; Transcription factor

Indexed keywords

INTERLEUKIN 13; INTERLEUKIN 4;

EID: 0033945403     PISSN: 00916749     EISSN: None     Source Type: Journal    
DOI: 10.1067/mai.2000.107604     Document Type: Article
Times cited : (335)

References (89)
  • 1
    • 0029867119 scopus 로고    scopus 로고
    • IL-4 and IL-13 receptors: Are they one and the same?
    • Callard RE, Matthews DJ, Hibbert L. IL-4 and IL-13 receptors: Are they one and the same? Immunol Today 1996;17:108-10.
    • (1996) Immunol Today , vol.17 , pp. 108-110
    • Callard, R.E.1    Matthews, D.J.2    Hibbert, L.3
  • 3
    • 0029879016 scopus 로고    scopus 로고
    • Molecular and biological characteristics of interleukin-13
    • de Vries JE. Molecular and biological characteristics of interleukin-13. Chem Immunol 1996;63:204-18.
    • (1996) Chem Immunol , vol.63 , pp. 204-218
    • De Vries, J.E.1
  • 4
    • 0033595261 scopus 로고    scopus 로고
    • Interleukin-4-dependent production of PPAR-gamma ligands in macrophages by 12/15-lipoxygenase
    • Huang JT, Welch JS, Ricote M, et al. Interleukin-4-dependent production of PPAR-gamma ligands in macrophages by 12/15-lipoxygenase. Nature 1999;400:378-82.
    • (1999) Nature , vol.400 , pp. 378-382
    • Huang, J.T.1    Welch, J.S.2    Ricote, M.3
  • 6
    • 0025376201 scopus 로고
    • Molecular cloning of a cDNA encoding the human interleukin 4 receptor
    • Galizzi JP, Zuber CE, Harada N, et al. Molecular cloning of a cDNA encoding the human interleukin 4 receptor. Int Immunol 1990;2:669-75.
    • (1990) Int Immunol , vol.2 , pp. 669-675
    • Galizzi, J.P.1    Zuber, C.E.2    Harada, N.3
  • 7
    • 0030068217 scopus 로고    scopus 로고
    • Cloning and characterization of a binding subunit of the interleukin 13 receptor that is also a component of the interleukin 4 receptor
    • Hilton DJ, Zhang JG, Metcalf D, Alexander WS, Nicola NA, Willson TA. Cloning and characterization of a binding subunit of the interleukin 13 receptor that is also a component of the interleukin 4 receptor. Proc Natl Acad Sci U S A 1996;93:497-501.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 497-501
    • Hilton, D.J.1    Zhang, J.G.2    Metcalf, D.3    Alexander, W.S.4    Nicola, N.A.5    Willson, T.A.6
  • 8
    • 10544246077 scopus 로고    scopus 로고
    • CDNA cloning and characterization of the human interleukin 13 receptor alpha chain
    • Aman MJ, Tayebi N, Obiri NI, Puri RK, Modi WS, Leonard WJ. cDNA cloning and characterization of the human interleukin 13 receptor alpha chain. J Biol Chem 1996;271:29265-70.
    • (1996) J Biol Chem , vol.271 , pp. 29265-29270
    • Aman, M.J.1    Tayebi, N.2    Obiri, N.I.3    Puri, R.K.4    Modi, W.S.5    Leonard, W.J.6
  • 9
    • 0032167603 scopus 로고    scopus 로고
    • The murine IL-13 receptor alpha 2: Molecular cloning, characterization, and comparison with murine IL-13 receptor alpha 1
    • Donaldson DD, Whitters MJ, Fitz LJ, et al. The murine IL-13 receptor alpha 2: molecular cloning, characterization, and comparison with murine IL-13 receptor alpha 1. J Immunol 1998;161:2317-24.
    • (1998) J Immunol , vol.161 , pp. 2317-2324
    • Donaldson, D.D.1    Whitters, M.J.2    Fitz, L.J.3
  • 10
    • 0033574713 scopus 로고    scopus 로고
    • Crystal structure of the interleukin4/receptor alpha chain complex reveals a mosaic binding interface
    • Hage T, Sebald W, Reinemer P. Crystal structure of the interleukin4/receptor alpha chain complex reveals a mosaic binding interface. Cell 1999;97:271-81.
    • (1999) Cell , vol.97 , pp. 271-281
    • Hage, T.1    Sebald, W.2    Reinemer, P.3
  • 11
    • 0028126979 scopus 로고
    • Design of human interleukin-4 antagonists inhibiting interleukin-4-dependent and interleukin-13-dependent responses in T-cells and B-cells with high efficiency
    • Tony HP, Shen BJ, Reusch P, Sebald W. Design of human interleukin-4 antagonists inhibiting interleukin-4-dependent and interleukin-13-dependent responses in T-cells and B-cells with high efficiency. Eur J Biochem 1994;225:659-65.
    • (1994) Eur J Biochem , vol.225 , pp. 659-665
    • Tony, H.P.1    Shen, B.J.2    Reusch, P.3    Sebald, W.4
  • 12
    • 0029035685 scopus 로고
    • The primary binding subunit of the human interleukin-4 receptor is also a component of the interleukin-13 receptor
    • Zurawski SM, Chomarat P, Djossou O, et al. The primary binding subunit of the human interleukin-4 receptor is also a component of the interleukin-13 receptor. J Biol Chem 1995;270:13869-78.
    • (1995) J Biol Chem , vol.270 , pp. 13869-13878
    • Zurawski, S.M.1    Chomarat, P.2    Djossou, O.3
  • 13
    • 0032007351 scopus 로고    scopus 로고
    • IL-13, IL-4Ralpha, and Stato are required for the expulsion of the gastrointestinal nematode parasite Nippostrongylus brasiliensis
    • Urban JF Jr, Noben-Trauth N, Donaldson DD, et al. IL-13, IL-4Ralpha, and Stato are required for the expulsion of the gastrointestinal nematode parasite Nippostrongylus brasiliensis. Immunity 1998;8:255-64.
    • (1998) Immunity , vol.8 , pp. 255-264
    • Urban Jr., J.F.1    Noben-Trauth, N.2    Donaldson, D.D.3
  • 14
    • 15144358874 scopus 로고    scopus 로고
    • Interleukin-4 signaling in B lymphocytes from patients with X-linked severe combined immunodeficiency
    • Taylor N, Candotti F, Smith S, et al. Interleukin-4 signaling in B lymphocytes from patients with X-linked severe combined immunodeficiency. J Biol Chem 1997;272:7314-9.
    • (1997) J Biol Chem , vol.272 , pp. 7314-7319
    • Taylor, N.1    Candotti, F.2    Smith, S.3
  • 15
    • 0031570471 scopus 로고    scopus 로고
    • The IL-4 receptor alpha-chain cytoplasmic domain is sufficient for activation of JAK-1 and STAT6 and the induction of IL-4-specific gene expression
    • Reichel M, Nelson BH, Greenberg PD, Rothman PB. The IL-4 receptor alpha-chain cytoplasmic domain is sufficient for activation of JAK-1 and STAT6 and the induction of IL-4-specific gene expression. J Immunol 1997;158:5860-7.
    • (1997) J Immunol , vol.158 , pp. 5860-5867
    • Reichel, M.1    Nelson, B.H.2    Greenberg, P.D.3    Rothman, P.B.4
  • 16
    • 0032525073 scopus 로고    scopus 로고
    • Interleukin-13 receptor alpha' but not alpha chain: A functional component of interleukin-4 receptors
    • Murata T, Taguchi J, Puri RK. Interleukin-13 receptor alpha' but not alpha chain: a functional component of interleukin-4 receptors. Blood 1998;91:3884-91.
    • (1998) Blood , vol.91 , pp. 3884-3891
    • Murata, T.1    Taguchi, J.2    Puri, R.K.3
  • 17
    • 0027993022 scopus 로고
    • Functional activation of Jakl and Jak3 by selective association with IL-2 receptor subunits
    • Miyazaki T, Kawahara A, Fujii H, et al. Functional activation of Jakl and Jak3 by selective association with IL-2 receptor subunits. Science 1994;266:1045-7.
    • (1994) Science , vol.266 , pp. 1045-1047
    • Miyazaki, T.1    Kawahara, A.2    Fujii, H.3
  • 18
    • 0028171065 scopus 로고
    • Interaction of IL-2R beta and gamma c chains with Jakl and Jak3: Implications for XSCID and XCID
    • Russell SM, Johnston JA, Noguchi M, et al. Interaction of IL-2R beta and gamma c chains with Jakl and Jak3: implications for XSCID and XCID. Science 1994;266:1042-5.
    • (1994) Science , vol.266 , pp. 1042-1045
    • Russell, S.M.1    Johnston, J.A.2    Noguchi, M.3
  • 19
    • 0029019017 scopus 로고
    • Interleukin-13 signal transduction in lymphohemopoietic cells. Similarities and differences in signal transduction with interleukin-4 and insulin
    • Welham MJ, Learmonth L, Bone H, Schrader JW. Interleukin-13 signal transduction in lymphohemopoietic cells. Similarities and differences in signal transduction with interleukin-4 and insulin. J Biol Chem 1995;270:12286-96.
    • (1995) J Biol Chem , vol.270 , pp. 12286-12296
    • Welham, M.J.1    Learmonth, L.2    Bone, H.3    Schrader, J.W.4
  • 20
    • 0033610862 scopus 로고    scopus 로고
    • Induction of 15-lipoxygenase expression by IL-13 requires tyrosine phosphorylation of Jak2 and Tyk2 in human monocytes
    • Roy B, Cathcart MK. Induction of 15-lipoxygenase expression by IL-13 requires tyrosine phosphorylation of Jak2 and Tyk2 in human monocytes. J Biol Chem 1998;273:32023-9.
    • (1998) J Biol Chem , vol.273 , pp. 32023-32029
    • Roy, B.1    Cathcart, M.K.2
  • 21
    • 0031561791 scopus 로고    scopus 로고
    • Comparison of IL-13- And IL-4-induced signaling in EBV-immortalized human B cells
    • Murata T, Puri RK. Comparison of IL-13- and IL-4-induced signaling in EBV-immortalized human B cells. Cell Immunol 1997;175:33-40.
    • (1997) Cell Immunol , vol.175 , pp. 33-40
    • Murata, T.1    Puri, R.K.2
  • 22
    • 0025813375 scopus 로고
    • Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein
    • Sun XJ, Rothenberg P, Kahn CR, et al. Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein. Nature 1991;352:73-7.
    • (1991) Nature , vol.352 , pp. 73-77
    • Sun, X.J.1    Rothenberg, P.2    Kahn, C.R.3
  • 23
    • 0031616132 scopus 로고    scopus 로고
    • The IRS-signaling system: A network of docking proteins that mediate insulin and cytokine action
    • White MF. The IRS-signaling system: a network of docking proteins that mediate insulin and cytokine action. Recent Prog Horm Res 1998;53:119-38.
    • (1998) Recent Prog Horm Res , vol.53 , pp. 119-138
    • White, M.F.1
  • 24
    • 0029148591 scopus 로고
    • Role of IRS-2 in insulin and cytokine signalling
    • SunXJ, WangLM,ZhangY, et al. Role of IRS-2 in insulin and cytokine signalling. Nature 1995;377:173-7.
    • (1995) Nature , vol.377 , pp. 173-177
    • Sun, X.J.1    Wang, L.M.2    Zhang, Y.3
  • 25
    • 0027507755 scopus 로고
    • 1RS-1 : Essential for insulin- And IL-4-stimulated mitogenesis in hematopoietic cells
    • Wang LM, Myers MG Jr, Sun XJ, Aaronson SA, White M, Pierce JH. 1RS-1 : essential for insulin- and IL-4-stimulated mitogenesis in hematopoietic cells. Science 1993;261:1591-4.
    • (1993) Science , vol.261 , pp. 1591-1594
    • Wang, L.M.1    Myers Jr., M.G.2    Sun, X.J.3    Aaronson, S.A.4    White, M.5    Pierce, J.H.6
  • 26
    • 0023814924 scopus 로고
    • Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect its tyrosine kinase activity
    • White MF, Livingston JN, Backer JM, et al. Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect its tyrosine kinase activity. Cell 1988;54:641-9.
    • (1988) Cell , vol.54 , pp. 641-649
    • White, M.F.1    Livingston, J.N.2    Backer, J.M.3
  • 27
    • 0028219966 scopus 로고
    • An IL-4 receptor region containing an insulin receptor motif is important for IL4-mediated IRS-1 phosphorylation and cell growth
    • Keegan AD, Nelms K, White M, Wang LM, Pierce JH, Paul WE. An IL-4 receptor region containing an insulin receptor motif is important for IL4-mediated IRS-1 phosphorylation and cell growth. Cell 1994;76:811-20.
    • (1994) Cell , vol.76 , pp. 811-820
    • Keegan, A.D.1    Nelms, K.2    White, M.3    Wang, L.M.4    Pierce, J.H.5    Paul, W.E.6
  • 28
    • 0032053709 scopus 로고    scopus 로고
    • Mechanisms and consequences of activation of protein kinase B/Akt
    • Downward J. Mechanisms and consequences of activation of protein kinase B/Akt. Curr Opin Cell Biol 1998;10:262-7.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 262-267
    • Downward, J.1
  • 29
    • 0032518467 scopus 로고    scopus 로고
    • 3-Phosphoinositide-dependent protein kinase l (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro
    • Alessi DR, Kozlowski MT, Weng QP, Morrice N, Avruch J. 3-Phosphoinositide-dependent protein kinase l (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro. Curr Biol 1998;8:69-81.
    • (1998) Curr Biol , vol.8 , pp. 69-81
    • Alessi, D.R.1    Kozlowski, M.T.2    Weng, Q.P.3    Morrice, N.4    Avruch, J.5
  • 30
    • 0030444051 scopus 로고    scopus 로고
    • IL-4 protects cells from apoptosis via the insulin receptor substrate pathway and a second independent signaling pathway
    • Zamorano J, Wang HY, Wang LM, Pierce JH, Keegan AD. IL-4 protects cells from apoptosis via the insulin receptor substrate pathway and a second independent signaling pathway. J Immunol 1996;157:4926-34.
    • (1996) J Immunol , vol.157 , pp. 4926-4934
    • Zamorano, J.1    Wang, H.Y.2    Wang, L.M.3    Pierce, J.H.4    Keegan, A.D.5
  • 31
    • 0032191896 scopus 로고    scopus 로고
    • Linking extracellular survival signals and the apoptotic machinery
    • Nunez G, del Peso L. Linking extracellular survival signals and the apoptotic machinery. Curr Opin Neurobiol 1998;8:613-8.
    • (1998) Curr Opin Neurobiol , vol.8 , pp. 613-618
    • Nunez, G.1    Del Peso, L.2
  • 32
    • 0032560514 scopus 로고    scopus 로고
    • Dissociation of cytokine-induced phosphorylation of Bad and activation of PKB/akt: Involvement of MEK upstream of Bad phosphorylation
    • Scheid MP, Duronio V. Dissociation of cytokine-induced phosphorylation of Bad and activation of PKB/akt: involvement of MEK upstream of Bad phosphorylation. Proc Natl Acad Sci U S A 1998;95:7439-44.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7439-7444
    • Scheid, M.P.1    Duronio, V.2
  • 33
    • 0032126362 scopus 로고    scopus 로고
    • FRIP, a hematopoietic cell-specific rasGAP-interacting protein phosphorylated in response to cytokine stimulation
    • Nelms K, Snow AL, Hu-Li J, Paul WE. FRIP, a hematopoietic cell-specific rasGAP-interacting protein phosphorylated in response to cytokine stimulation. Immunity 1998;9:13-24.
    • (1998) Immunity , vol.9 , pp. 13-24
    • Nelms, K.1    Snow, A.L.2    Hu-Li, J.3    Paul, W.E.4
  • 34
    • 0032570581 scopus 로고    scopus 로고
    • Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins
    • Di Cristofano A, Carpino N, Dunant N, et al. Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins. J Biol Chem 1998;273:4827-30.
    • (1998) J Biol Chem , vol.273 , pp. 4827-4830
    • Di Cristofano, A.1    Carpino, N.2    Dunant, N.3
  • 35
    • 0031459864 scopus 로고    scopus 로고
    • P62(dok): A con sti tu lively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells
    • Carpino N, Wisniewski D, Strife A, et al. p62(dok): a con sti tu lively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells. Cell 1997;88:197-204.
    • (1997) Cell , vol.88 , pp. 197-204
    • Carpino, N.1    Wisniewski, D.2    Strife, A.3
  • 36
    • 0031444245 scopus 로고    scopus 로고
    • Identification of the Abl- And rasGAP-associated 62 kDa protein as a docking protein, Dok
    • Yamanashi Y, Baltimore D. Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok. Cell 1997;88:205-11.
    • (1997) Cell , vol.88 , pp. 205-211
    • Yamanashi, Y.1    Baltimore, D.2
  • 37
    • 0030795790 scopus 로고    scopus 로고
    • Receptor-associated constitutive protein tyrosine phosphatase activity controls the kinase function of JAKL
    • Haque SJ, Wu Q, Kammer W, et al. Receptor-associated constitutive protein tyrosine phosphatase activity controls the kinase function of JAKL Proc Natl Acad Sci U S A 1997;94:8563-8.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8563-8568
    • Haque, S.J.1    Wu, Q.2    Kammer, W.3
  • 38
    • 0030582671 scopus 로고    scopus 로고
    • The emerging field of receptor-mediated inhibitory signaling: SHP or SHIP?
    • Scharenberg AM, Kinet JP The emerging field of receptor-mediated inhibitory signaling: SHP or SHIP? Cell 1996;87:961-4.
    • (1996) Cell , vol.87 , pp. 961-964
    • Scharenberg, A.M.1    Kinet, J.P.2
  • 39
    • 0032545279 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase Shp-1 is a negative regulator of IL-4- And IL-13-dependent signal transduction
    • Haque SJ, Harbor P, Tabrizi M, Yi T, Williams BR. Protein-tyrosine phosphatase Shp-1 is a negative regulator of IL-4- and IL-13-dependent signal transduction. J Biol Chem 1998;273:33893-6.
    • (1998) J Biol Chem , vol.273 , pp. 33893-33896
    • Haque, S.J.1    Harbor, P.2    Tabrizi, M.3    Yi, T.4    Williams, B.R.5
  • 40
    • 0032523416 scopus 로고    scopus 로고
    • Involvement of SHP-2 in multiple aspects of IL-2 signaling: Evidence for a positive regulatory role
    • GadinaM, Stancato LM, Bacon CM, Larner AC, O'SheaJJ. Involvement of SHP-2 in multiple aspects of IL-2 signaling: evidence for a positive regulatory role. J Immunol 1998;160:4657-61.
    • (1998) J Immunol , vol.160 , pp. 4657-4661
    • Gadina, M.1    Stancato, L.M.2    Bacon, C.M.3    Larner, A.C.4    O'Shea, J.J.5
  • 41
    • 0027158159 scopus 로고
    • The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp
    • Kuhne MR, Pawson T, Lienhard GE, Feng GS. The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp. J Biol Chem 1993;268:11479-81.
    • (1993) J Biol Chem , vol.268 , pp. 11479-11481
    • Kuhne, M.R.1    Pawson, T.2    Lienhard, G.E.3    Feng, G.S.4
  • 42
    • 0030962582 scopus 로고    scopus 로고
    • Interleukin-4 (IL-4) induces phosphatidylinositol 3-kinase (p85) dephosphorylation. Implications for the role of SHP-1 in the IL-4-induced signals in human B cells
    • Imani F, Rager KJ, Catipovic B, Marsh DG. Interleukin-4 (IL-4) induces phosphatidylinositol 3-kinase (p85) dephosphorylation. Implications for the role of SHP-1 in the IL-4-induced signals in human B cells. J Biol Chem 1997;272:7927-31.
    • (1997) J Biol Chem , vol.272 , pp. 7927-7931
    • Imani, F.1    Rager, K.J.2    Catipovic, B.3    Marsh, D.G.4
  • 43
    • 0028932411 scopus 로고
    • Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by Fc gamma RUB 1
    • D'Ambrosio D, Hippen KL, Minskoff SA, et al. Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by Fc gamma RUB 1. Science 1995;268:293-7.
    • (1995) Science , vol.268 , pp. 293-297
    • D'Ambrosio, D.1    Hippen, K.L.2    Minskoff, S.A.3
  • 44
    • 0030024788 scopus 로고    scopus 로고
    • Recruitment of tyrosine phosphatase HCP by the killer cell inhibitor receptor
    • Burshtyn DN, Scharenberg AM, Wagtmann N, et al. Recruitment of tyrosine phosphatase HCP by the killer cell inhibitor receptor. Immunity 1996;4:77-85.
    • (1996) Immunity , vol.4 , pp. 77-85
    • Burshtyn, D.N.1    Scharenberg, A.M.2    Wagtmann, N.3
  • 45
    • 0028780730 scopus 로고
    • A 13-amino-acid motif in the cytoplasmic domain of Fc gamma RUB modulates B-cell receptor signalling
    • Muta T, Kurosaki T, Misulovin Z, Sanchez M, Nussenzweig MC, Ravetch JV. A 13-amino-acid motif in the cytoplasmic domain of Fc gamma RUB modulates B-cell receptor signalling. Nature 1994;369:340.
    • (1994) Nature , vol.369 , pp. 340
    • Muta, T.1    Kurosaki, T.2    Misulovin, Z.3    Sanchez, M.4    Nussenzweig, M.C.5    Ravetch, J.V.6
  • 46
    • 0028851582 scopus 로고
    • The same tyrosine-based inhibition motif, in the intracytoplasmic domain of Fc gamma RUB, regulates negatively BCR-, TCR-, and FcR-dependent cell activation
    • Daeron M, Latour S, Malbec O, et al. The same tyrosine-based inhibition motif, in the intracytoplasmic domain of Fc gamma RUB, regulates negatively BCR-, TCR-, and FcR-dependent cell activation. Immunity 1995;3:635-46.
    • (1995) Immunity , vol.3 , pp. 635-646
    • Daeron, M.1    Latour, S.2    Malbec, O.3
  • 47
    • 0001325237 scopus 로고    scopus 로고
    • The association of atopy with a gain-of-function mutation in the alpha subunit of the interleukin-4 receptor
    • Hershey GK, Friedrich MF, Esswein LA, Thomas ML, Chatila TA. The association of atopy with a gain-of-function mutation in the alpha subunit of the interleukin-4 receptor. N Engl J Med 1997;337:1720-5.
    • (1997) N Engl J Med , vol.337 , pp. 1720-1725
    • Hershey, G.K.1    Friedrich, M.F.2    Esswein, L.A.3    Thomas, M.L.4    Chatila, T.A.5
  • 48
    • 0032528425 scopus 로고    scopus 로고
    • Regulation of apoptosis by tyrosine-containing domains of IL-4R alpha: Y497 and Y713, but not the STAT6-docking tyrosines, signal protection from apoptosis
    • Zamorano J, Keegan AD. Regulation of apoptosis by tyrosine-containing domains of IL-4R alpha: Y497 and Y713, but not the STAT6-docking tyrosines, signal protection from apoptosis. J Immunol 1998; 161:859-67.
    • (1998) J Immunol , vol.161 , pp. 859-867
    • Zamorano, J.1    Keegan, A.D.2
  • 49
    • 0034703082 scopus 로고    scopus 로고
    • Positive regulation of IL-4 mediated proliferation by the SH2-containing inositol 5'-phosphatase (SHIP)
    • In press
    • Giallourakis C, Kashiwada M, Pan P, et al. Positive regulation of IL-4 mediated proliferation by the SH2-containing inositol 5'-phosphatase (SHIP). J Biol Chem. In press, 2000.
    • (2000) J Biol Chem.
    • Giallourakis, C.1    Kashiwada, M.2    Pan, P.3
  • 50
    • 0029978202 scopus 로고    scopus 로고
    • The 145-kDa protein induced to associate with She by multiple cytokines is an inositol tetraphosphate and phosphaudylinositol 3,4,5- Triphosphate 5-phosphatase
    • Damen JE, Liu L, Rosten P, et al. The 145-kDa protein induced to associate with She by multiple cytokines is an inositol tetraphosphate and phosphaudylinositol 3,4,5- triphosphate 5-phosphatase. Proc Natl Acad Sci USA 1996;93:1689-93.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1689-1693
    • Damen, J.E.1    Liu, L.2    Rosten, P.3
  • 51
    • 0029902217 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of She is not required for proliferation or viability signaling by granulocytemacrophage colony-stimulating factor in hematopoietic cell lines
    • Durstin M, Inhorn RC, Griffin JD. Tyrosine phosphorylation of She is not required for proliferation or viability signaling by granulocytemacrophage colony-stimulating factor in hematopoietic cell lines. J Immunol 1996;157:534-40.
    • (1996) J Immunol , vol.157 , pp. 534-540
    • Durstin, M.1    Inhorn, R.C.2    Griffin, J.D.3
  • 52
    • 0030975468 scopus 로고    scopus 로고
    • The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with She, and its induction of apoptosis
    • Liu L, Damen JE, Hughes MR, Babic I, Jirik FR, Krystal G. The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with She, and its induction of apoptosis. J Biol Chem 1997;272:8983-8.
    • (1997) J Biol Chem , vol.272 , pp. 8983-8988
    • Liu, L.1    Damen, J.E.2    Hughes, M.R.3    Babic, I.4    Jirik, F.R.5    Krystal, G.6
  • 54
    • 0029859565 scopus 로고    scopus 로고
    • Cloning and characterization of human SHIP, the 145-kD inositol 5phosphatase that associates with SHC after cytokine stimulation
    • Ware MD, Rosten P, Damen JE, Liu L, Humphries RK, Krystal G. Cloning and characterization of human SHIP, the 145-kD inositol 5phosphatase that associates with SHC after cytokine stimulation. Blood 1996;88:2833-40.
    • (1996) Blood , vol.88 , pp. 2833-2840
    • Ware, M.D.1    Rosten, P.2    Damen, J.E.3    Liu, L.4    Humphries, R.K.5    Krystal, G.6
  • 55
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • Franke TF, Kaplan DR, Cantley LC, Toker A. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science 1997;275:665-8.
    • (1997) Science , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 56
    • 0034610982 scopus 로고    scopus 로고
    • A dual role for src homology 2 domain-containing inositol-5-phosphatase (SHIP) in immunity. Aberrant development and enhanced function of b lymphocytes in SHIP(-/)- Mice
    • Helgason CD, Kalberer CP, Damen JE, et al. A dual role for src homology 2 domain-containing inositol-5-phosphatase (SHIP) in immunity. Aberrant development and enhanced function of b lymphocytes in SHIP(-/)- mice. J Exp Med 2000;191:781-94.
    • (2000) J Exp Med , vol.191 , pp. 781-794
    • Helgason, C.D.1    Kalberer, C.P.2    Damen, J.E.3
  • 57
    • 0028040875 scopus 로고
    • The POZ domain: A conserved protein-protein interaction motif
    • Bardwell VJ, Treisman R. The POZ domain: a conserved protein-protein interaction motif. Genes Dev 1994;8:1664-77.
    • (1994) Genes Dev , vol.8 , pp. 1664-1677
    • Bardwell, V.J.1    Treisman, R.2
  • 58
    • 0025853152 scopus 로고
    • The KUP gene, located on human chromosome 14, encodes a protein with two distant zinc fingers
    • Chardin P, Courtois G, Mattei MG, Gisselbrecht S. The KUP gene, located on human chromosome 14, encodes a protein with two distant zinc fingers. Nucleic Acids Res 1991;19:1431-6.
    • (1991) Nucleic Acids Res , vol.19 , pp. 1431-1436
    • Chardin, P.1    Courtois, G.2    Mattei, M.G.3    Gisselbrecht, S.4
  • 59
    • 0027411688 scopus 로고
    • Fusion between a novel Kruppel-like zinc finger gene and the retinoic acid receptor-alpha locus due to a variant t(l 1;17) translocation associated with acute promyelocytic leukaemia
    • Chen Z, Brand NJ, Chen A, et al. Fusion between a novel Kruppel-like zinc finger gene and the retinoic acid receptor-alpha locus due to a variant t(l 1;17) translocation associated with acute promyelocytic leukaemia. EMBO J 1993;12:1161-7.
    • (1993) EMBO J , vol.12 , pp. 1161-1167
    • Chen, Z.1    Brand, N.J.2    Chen, A.3
  • 60
    • 0025955580 scopus 로고
    • The Drosophila Broad-Complex encodes a family of related proteins containing zinc fingers
    • DiBello PR, Withers DA, Bayer CA, Fristrom JW, Guild GM. The Drosophila Broad-Complex encodes a family of related proteins containing zinc fingers. Genetics 1991;129:385-97.
    • (1991) Genetics , vol.129 , pp. 385-397
    • DiBello, P.R.1    Withers, D.A.2    Bayer, C.A.3    Fristrom, J.W.4    Guild, G.M.5
  • 61
    • 0027254765 scopus 로고
    • Transcriptional represser ZF5 identifies a new conserved domain in zinc finger proteins
    • Numoto M, Niwa O, Kaplan J, et al. Transcriptional represser ZF5 identifies a new conserved domain in zinc finger proteins. Nucleic Acids Res 1993;21:3767-75.
    • (1993) Nucleic Acids Res , vol.21 , pp. 3767-3775
    • Numoto, M.1    Niwa, O.2    Kaplan, J.3
  • 62
    • 0028110129 scopus 로고
    • The BTB domain, found primarily in zinc finger proteins, defines an evolutionary conserved family that includes several developmentally regulated genes in Drosophila
    • Zollman S, Godt D, Prive GG, Couderc JL, Laski FA. The BTB domain, found primarily in zinc finger proteins, defines an evolutionary conserved family that includes several developmentally regulated genes in Drosophila. Proc Natl Acad Sci U S A 1994;91:10717-21.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10717-10721
    • Zollman, S.1    Godt, D.2    Prive, G.G.3    Couderc, J.L.4    Laski, F.A.5
  • 63
    • 0029902260 scopus 로고    scopus 로고
    • BCL-6, a POZ/zinc-finger protein, is a sequence-specific transcriptional repressor
    • Chang CC, Ye BH, Chaganti RS, Dalla-Favera R. BCL-6, a POZ/zinc-finger protein, is a sequence-specific transcriptional repressor. Proc Natl Acad Sci USA 1996;93:6947-52.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6947-6952
    • Chang, C.C.1    Ye, B.H.2    Chaganti, R.S.3    Dalla-Favera, R.4
  • 64
    • 0030923519 scopus 로고    scopus 로고
    • Corepressor SMRT binds the BTB/POZ repressing domain of the LAZ3/BCL6 oncoprotein
    • Dhordain P, Albagli O, Lin RJ, et al. Corepressor SMRT binds the BTB/POZ repressing domain of the LAZ3/BCL6 oncoprotein. Proc Natl Acad Sci U S A 1997;94:10762-7.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10762-10767
    • Dhordain, P.1    Albagli, O.2    Lin, R.J.3
  • 65
    • 0029899571 scopus 로고    scopus 로고
    • Transcriptional repression by the proto-oncogene BCL-6
    • Seyfert VL, Allman D, He Y, Staudt LM. Transcriptional repression by the proto-oncogene BCL-6. Oncogene 1996;12:2331-42.
    • (1996) Oncogene , vol.12 , pp. 2331-2342
    • Seyfert, V.L.1    Allman, D.2    He, Y.3    Staudt, L.M.4
  • 66
    • 0027306091 scopus 로고
    • LAZ3, a novel zinc-finger encoding gene, is disrupted by recurring chromosome 3q27 translocations in human lymphomas
    • Kerckaert JP, Deweindt C, Tilly H, Quief S, Lecocq G, Bastard C. LAZ3, a novel zinc-finger encoding gene, is disrupted by recurring chromosome 3q27 translocations in human lymphomas. Nat Genet 1993;5:66-70.
    • (1993) Nat Genet , vol.5 , pp. 66-70
    • Kerckaert, J.P.1    Deweindt, C.2    Tilly, H.3    Quief, S.4    Lecocq, G.5    Bastard, C.6
  • 67
    • 0028031988 scopus 로고
    • Gene involved in the 3q27 translocation associated with B-cell lymphoma, BCL5, encodes a Kruppel-like zinc-finger protein
    • Miki T, Kawamata N, Hirosawa S, Aoki N. Gene involved in the 3q27 translocation associated with B-cell lymphoma, BCL5, encodes a Kruppel-like zinc-finger protein. Blood 1994;83:26-32.
    • (1994) Blood , vol.83 , pp. 26-32
    • Miki, T.1    Kawamata, N.2    Hirosawa, S.3    Aoki, N.4
  • 68
    • 0027299245 scopus 로고
    • Cloning of bcl-6, the locus involved in chromosome translocations affecting band 3q27 in Bcell lymphoma
    • Ye BH, Rao PH, Chaganti RS, Dalla-Favera R. Cloning of bcl-6, the locus involved in chromosome translocations affecting band 3q27 in Bcell lymphoma. Cancer Res 1993;53:2732-5.
    • (1993) Cancer Res , vol.53 , pp. 2732-2735
    • Ye, B.H.1    Rao, P.H.2    Chaganti, R.S.3    Dalla-Favera, R.4
  • 69
    • 0027288335 scopus 로고
    • Identification of the gene associated with the recurring chromosomal translocations t(3;14)(q27;q32) and t(3;22)(q27;ql 1) in B-cell lymphomas
    • Baron BW, Nucifora G, McCabe N, Espinosa RD, Le Beau MM, McKeithan TW. Identification of the gene associated with the recurring chromosomal translocations t(3;14)(q27;q32) and t(3;22)(q27;ql 1) in B-cell lymphomas. Proc Natl Acad Sci U S A 1993;90:5262-6.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 5262-5266
    • Baron, B.W.1    Nucifora, G.2    McCabe, N.3    Espinosa, R.D.4    Le Beau, M.M.5    McKeithan, T.W.6
  • 70
    • 0030901289 scopus 로고    scopus 로고
    • Control of inflammation, cytokine expression, and germinal center formation by BCL-6
    • Dent AL, Shaffer AL, Yu X, Allman D, Staudt LM. Control of inflammation, cytokine expression, and germinal center formation by BCL-6. Science 1997;276:589-92.
    • (1997) Science , vol.276 , pp. 589-592
    • Dent, A.L.1    Shaffer, A.L.2    Yu, X.3    Allman, D.4    Staudt, L.M.5
  • 71
    • 0032827421 scopus 로고    scopus 로고
    • Transcriptional repression of Stato-dependent interleukin-4-induced genes by BCL-6: Specific regulation of iepsilon transcription and immunoglobulin E switching
    • Harris MB, Chang CC, Berton MT, et al. Transcriptional repression of Stato-dependent interleukin-4-induced genes by BCL-6: specific regulation of iepsilon transcription and immunoglobulin E switching. Mol Cell Biol 1999;19:7264-75.
    • (1999) Mol Cell Biol , vol.19 , pp. 7264-7275
    • Harris, M.B.1    Chang, C.C.2    Berton, M.T.3
  • 72
    • 0029045421 scopus 로고
    • BCL-6 protein is expressed in germinal-center B cells
    • Cattoretti G, Chang CC, Cechova K, et al. BCL-6 protein is expressed in germinal-center B cells. Blood 1995;86:45-53.
    • (1995) Blood , vol.86 , pp. 45-53
    • Cattoretti, G.1    Chang, C.C.2    Cechova, K.3
  • 73
    • 0029118040 scopus 로고
    • A specific monoclonal antibody (PG-B6) detects expression of the BCL-6 protein in germinal center B cells
    • Flenghi L, Ye BH, Fizzotti M, et al. A specific monoclonal antibody (PG-B6) detects expression of the BCL-6 protein in germinal center B cells. AmJPathol 1995;147:405-11.
    • (1995) AmJPathol , vol.147 , pp. 405-411
    • Flenghi, L.1    Ye, B.H.2    Fizzotti, M.3
  • 74
    • 0029019660 scopus 로고
    • BCL-6 gene product, a 92- To 98-kD nuclear phosphoprotein, is highly expressed in germinal center B cells and their neoplastic counterparts
    • Onizuka T, Moriyama M, Yamochi T, et al. BCL-6 gene product, a 92- to 98-kD nuclear phosphoprotein, is highly expressed in germinal center B cells and their neoplastic counterparts. Blood 1995;86:28-37.
    • (1995) Blood , vol.86 , pp. 28-37
    • Onizuka, T.1    Moriyama, M.2    Yamochi, T.3
  • 75
    • 17144439800 scopus 로고    scopus 로고
    • The BCL-6 proto-oncogene controls germinal-centre formation and Th2-type inflammation
    • Ye BH, Cattoretti G, Shen Q, et al. The BCL-6 proto-oncogene controls germinal-centre formation and Th2-type inflammation. Nat Genet 1997;16:161-70.
    • (1997) Nat Genet , vol.16 , pp. 161-170
    • Ye, B.H.1    Cattoretti, G.2    Shen, Q.3
  • 76
    • 0033566955 scopus 로고    scopus 로고
    • BCL-6-deficient mice reveal an IL-4-independent, STAT6-dependent pathway that con-trols susceptibility to infection by Leishmania major
    • Dent AL, Doherty TM, Paul WE, Sher A, Staudt LM. BCL-6-deficient mice reveal an IL-4-independent, STAT6-dependent pathway that con-trols susceptibility to infection by Leishmania major. J Immunol 1999;163:2098-103.
    • (1999) J Immunol , vol.163 , pp. 2098-2103
    • Dent, A.L.1    Doherty, T.M.2    Paul, W.E.3    Sher, A.4    Staudt, L.M.5
  • 77
    • 0032506130 scopus 로고    scopus 로고
    • T helper type 2 inflammatory disease in the absence of interleukin 4 and transcription factor STAT6
    • Dent AL, Hu-Li J, Paul WE, Staudt LM. T helper type 2 inflammatory disease in the absence of interleukin 4 and transcription factor STAT6. Proc Natl Acad Sci U S A 1998;95:13823-8.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 13823-13828
    • Dent, A.L.1    Hu-Li, J.2    Paul, W.E.3    Staudt, L.M.4
  • 78
    • 0030839112 scopus 로고    scopus 로고
    • A new protein containing an SH2 domain that inhibits JAK kinases
    • Endo TA, Masuhara M, Yokouchi M, et al. A new protein containing an SH2 domain that inhibits JAK kinases. Nature 1997;387:921-4.
    • (1997) Nature , vol.387 , pp. 921-924
    • Endo, T.A.1    Masuhara, M.2    Yokouchi, M.3
  • 79
    • 0030755934 scopus 로고    scopus 로고
    • Structure and function of a new STAT-induced STAT inhibitor
    • Naka T, Narazaki M, Hirata M, et al. Structure and function of a new STAT-induced STAT inhibitor. Nature 1997;387:924-9.
    • (1997) Nature , vol.387 , pp. 924-929
    • Naka, T.1    Narazaki, M.2    Hirata, M.3
  • 80
    • 0030792590 scopus 로고    scopus 로고
    • A family of cytokine-inducible inhibitors of signalling
    • Starr R, Willson TA, Viney EM, et al. A family of cytokine-inducible inhibitors of signalling. Nature 1997;387:917-21.
    • (1997) Nature , vol.387 , pp. 917-921
    • Starr, R.1    Willson, T.A.2    Viney, E.M.3
  • 81
    • 13144258732 scopus 로고    scopus 로고
    • Twenty proteins containing a C-terminal SOCS box form five structural classes
    • Hilton DJ, Richardson RT, Alexander WS, et al. Twenty proteins containing a C-terminal SOCS box form five structural classes. Proc Natl Acad Sci US A 1998;95:114-9.
    • (1998) Proc Natl Acad Sci US A , vol.95 , pp. 114-119
    • Hilton, D.J.1    Richardson, R.T.2    Alexander, W.S.3
  • 82
    • 0032573161 scopus 로고    scopus 로고
    • Three distinct domains of SSI-1/SOCS-l/JAB protein are required forits suppression of interleukin 6 signaling
    • Narazaki M, Fujimoto M, Matsumoto T, et al. Three distinct domains of SSI-1/SOCS-l/JAB protein are required forits suppression of interleukin 6 signaling. Proc Natl Acad Sci U S A 1998;95:13130-4.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 13130-13134
    • Narazaki, M.1    Fujimoto, M.2    Matsumoto, T.3
  • 83
    • 0033555258 scopus 로고    scopus 로고
    • Mutational analyses of the SOCS proteins suggest a dual domain requirement but distinct mechanisms for inhibition of LIE and IL-6 signal transduction
    • Nicholson SE, Willson TA, Farley A, et al. Mutational analyses of the SOCS proteins suggest a dual domain requirement but distinct mechanisms for inhibition of LIE and IL-6 signal transduction. EMBO J 1999;18:375-85.
    • (1999) EMBO J , vol.18 , pp. 375-385
    • Nicholson, S.E.1    Willson, T.A.2    Farley, A.3
  • 84
    • 20244389693 scopus 로고    scopus 로고
    • The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop
    • Yasukawa H, Misawa H, Sakamoto H, et al. The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop. EMBO J 1999;18:1309-20.
    • (1999) EMBO J , vol.18 , pp. 1309-1320
    • Yasukawa, H.1    Misawa, H.2    Sakamoto, H.3
  • 85
    • 0033120880 scopus 로고    scopus 로고
    • Cutting edge: SOCS-1 is a potent inhibitor of IL-4 signal transduction
    • Losman JA, Chen XP, Hilton D, Rothman P. Cutting edge: SOCS-1 is a potent inhibitor of IL-4 signal transduction. J Immunol 1999;162: 3770-4.
    • (1999) J Immunol , vol.162 , pp. 3770-3774
    • Losman, J.A.1    Chen, X.P.2    Hilton, D.3    Rothman, P.4
  • 86
    • 0032850616 scopus 로고    scopus 로고
    • Interferons inhibit activation of STAT6 by interleukin 4 in human monocytes by inducing SOCS-1 gene expression
    • Dickensheets HL, Venkataraman C, Schindler U, Donnelly RP. Interferons inhibit activation of STAT6 by interleukin 4 in human monocytes by inducing SOCS-1 gene expression. Proc Natl Acad Sci U S A 1999;96:10800-5.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 10800-10805
    • Dickensheets, H.L.1    Venkataraman, C.2    Schindler, U.3    Donnelly, R.P.4
  • 87
    • 0033120515 scopus 로고    scopus 로고
    • Repression of IL-4-induced gene expression by IFN-gamma requires Statl activation
    • Venkataraman C, Leung S, Salvekar A, Mano H, Schindler U. Repression of IL-4-induced gene expression by IFN-gamma requires Statl activation. J Immunol 1999;162:4053-61.
    • (1999) J Immunol , vol.162 , pp. 4053-4061
    • Venkataraman, C.1    Leung, S.2    Salvekar, A.3    Mano, H.4    Schindler, U.5
  • 88
    • 13044276245 scopus 로고    scopus 로고
    • Accelerated apoptosis of lymphocytes by augmented induction of Bax in SSI-1 (STAT-induced STAT inhibitor-1) deficient mice
    • Naka T, Matsumoto T, Narazaki M, et al. Accelerated apoptosis of lymphocytes by augmented induction of Bax in SSI-1 (STAT-induced STAT inhibitor-1) deficient mice. Proc Natl Acad Sci U S A 1998;95:15577-82.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15577-15582
    • Naka, T.1    Matsumoto, T.2    Narazaki, M.3
  • 89
    • 0032564463 scopus 로고    scopus 로고
    • Liver degeneration and lymphoid deficiencies in mice lacking suppressor of cytokine signaling-1
    • Starr R, Metcalf D, Elefanty AG, et al. Liver degeneration and lymphoid deficiencies in mice lacking suppressor of cytokine signaling-1. Proc Natl Acad Sci U S A 1998;95:14395-9.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14395-14399
    • Starr, R.1    Metcalf, D.2    Elefanty, A.G.3


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