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Volumn 130, Issue 2, 1997, Pages 126-131

Regulation of signal transduction through the T cell antigen receptor

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EID: 0031213828     PISSN: 00222143     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2143(97)90088-3     Document Type: Conference Paper
Times cited : (3)

References (56)
  • 1
    • 0030250114 scopus 로고    scopus 로고
    • Complex complexes: Signaling at the TCR
    • Wange RL, Samelson LE. Complex complexes: signaling at the TCR. Immunity 1996;5:197-205.
    • (1996) Immunity , vol.5 , pp. 197-205
    • Wange, R.L.1    Samelson, L.E.2
  • 3
    • 0026095639 scopus 로고
    • Functional activation of the T cell antigen receptor induces tyrosine phosphorylation of phospholipase C-γl
    • Weiss A, Koretzky G, Schatzman R, Kadlecek T. Functional activation of the T cell antigen receptor induces tyrosine phosphorylation of phospholipase C-γl. Proc Natl Acad Sci USA 1991;88:5484-8.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5484-5488
    • Weiss, A.1    Koretzky, G.2    Schatzman, R.3    Kadlecek, T.4
  • 4
    • 0027337561 scopus 로고
    • p21 Ras couples the T cell antigen receptor to extracellular signal-regulated kinase 2 in T lymphocytes
    • Izquierdo M, Leevers SJ, Marshall CJ, Cantrell D. p21 Ras couples the T cell antigen receptor to extracellular signal-regulated kinase 2 in T lymphocytes. J Exp Med 1993;178: 1199-208.
    • (1993) J Exp Med , vol.178 , pp. 1199-1208
    • Izquierdo, M.1    Leevers, S.J.2    Marshall, C.J.3    Cantrell, D.4
  • 6
    • 0026078930 scopus 로고
    • Structure of the T cell antigen receptor (TCR): Two CD3 epsilon subunits in a functional TCR/CD3 complex
    • de la Hera A, Muller U, Olsson C, Isaaz S, Tunnacliffe A. Structure of the T cell antigen receptor (TCR): two CD3 epsilon subunits in a functional TCR/CD3 complex. J Exp Med 1991;173:7-17.
    • (1991) J Exp Med , vol.173 , pp. 7-17
    • De La Hera, A.1    Muller, U.2    Olsson, C.3    Isaaz, S.4    Tunnacliffe, A.5
  • 7
    • 0022993986 scopus 로고
    • Antigen activation of murine T cells induces tyrosine phosphorylation of a polypeptide associated with the T cell antigen receptor
    • Samelson LE, Patel MD, Weissman AM, Harford JB, Klausner RD. Antigen activation of murine T cells induces tyrosine phosphorylation of a polypeptide associated with the T cell antigen receptor. Cell 1986;46:1083-90.
    • (1986) Cell , vol.46 , pp. 1083-1090
    • Samelson, L.E.1    Patel, M.D.2    Weissman, A.M.3    Harford, J.B.4    Klausner, R.D.5
  • 8
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth M. Antigen receptor tail clue. Nature 1989;338:383-4.
    • (1989) Nature , vol.338 , pp. 383-384
    • Reth, M.1
  • 9
    • 0027399703 scopus 로고
    • Functional characterization of a signal transducing motif present in the T cell antigen receptor ζ chain
    • Irving BA, Chan AC, Weiss A. Functional characterization of a signal transducing motif present in the T cell antigen receptor ζ chain. J Exp Med 1993;177:1093-103.
    • (1993) J Exp Med , vol.177 , pp. 1093-1103
    • Irving, B.A.1    Chan, A.C.2    Weiss, A.3
  • 10
    • 0026544338 scopus 로고
    • The T cell receptor/CD3 complex is composed of at least two autonomous transduction modules
    • Wegener AM, Letourneur F, Hoeveloer A, Brocker T, Luton F, Malissen B. The T cell receptor/CD3 complex is composed of at least two autonomous transduction modules. Cell 1992; 68:83-95.
    • (1992) Cell , vol.68 , pp. 83-95
    • Wegener, A.M.1    Letourneur, F.2    Hoeveloer, A.3    Brocker, T.4    Luton, F.5    Malissen, B.6
  • 11
    • 0028209548 scopus 로고
    • Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases
    • Iwashima M, Irving BA, van Oers NSC, Chan AC, Weiss A. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science 1994;263:1136-9.
    • (1994) Science , vol.263 , pp. 1136-1139
    • Iwashima, M.1    Irving, B.A.2    Van Oers, N.S.C.3    Chan, A.C.4    Weiss, A.5
  • 12
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T. Protein modules and signalling networks. Nature 1995;373:573-80.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 13
    • 0026483786 scopus 로고
    • ZAP-70: A 70 kd protein-tyrosine kinase that associates with the TCR ζ chain
    • Chan AC, Iwashima M, Turck CW, Weiss A. ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR ζ chain. Cell 1992;71:649-62.
    • (1992) Cell , vol.71 , pp. 649-662
    • Chan, A.C.1    Iwashima, M.2    Turck, C.W.3    Weiss, A.4
  • 14
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss A, Littman DR. Signal transduction by lymphocyte antigen receptors. Cell 1994;76:263-74.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 15
    • 0025835006 scopus 로고
    • T cell antigen receptor ligation induces tyrosine phosphorylation of phospholipase C-γ1
    • Secrist JP, Karnitz L, Abraham R. T cell antigen receptor ligation induces tyrosine phosphorylation of phospholipase C-γ1. J Biol Chem 1991;266:12135-9.
    • (1991) J Biol Chem , vol.266 , pp. 12135-12139
    • Secrist, J.P.1    Karnitz, L.2    Abraham, R.3
  • 16
    • 0026018057 scopus 로고
    • CD3 stimulation causes phosphorylation of phospholipase C-γ1 on serine and tyrosine residues in a human T cell line
    • Park DJ, Rho HW, Rhee SG. CD3 stimulation causes phosphorylation of phospholipase C-γ1 on serine and tyrosine residues in a human T cell line. Proc Natl Acad Sci U S A 1991;88:5453-6.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 5453-5456
    • Park, D.J.1    Rho, H.W.2    Rhee, S.G.3
  • 17
    • 0021917674 scopus 로고
    • Transmembrane signalling by the T cell antigen receptor: Perturbation of the T3-antigen receptor complex generates inositol phosphates and releases calcium ions from intracellular stores
    • Imboden JB, Stobo JD. Transmembrane signalling by the T cell antigen receptor: perturbation of the T3-antigen receptor complex generates inositol phosphates and releases calcium ions from intracellular stores. J Exp Med 1985;161:446-56.
    • (1985) J Exp Med , vol.161 , pp. 446-456
    • Imboden, J.B.1    Stobo, J.D.2
  • 18
    • 0021750054 scopus 로고
    • Inositol trisphosphate, a novel second messenger in cellular signal transduction
    • Berridge MJ, Irvine RF. Inositol trisphosphate, a novel second messenger in cellular signal transduction. Nature 1984; 312:315-21.
    • (1984) Nature , vol.312 , pp. 315-321
    • Berridge, M.J.1    Irvine, R.F.2
  • 20
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor
    • Straus DB, Weiss A. Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor. Cell 1992;70:585-93.
    • (1992) Cell , vol.70 , pp. 585-593
    • Straus, D.B.1    Weiss, A.2
  • 21
    • 0029999327 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Grb2-associated proteins correlates with phospholipase Cγ1 activation in T cells
    • Motto D, Musci M, Ross SE, Koretzky GA. Tyrosine phosphorylation of Grb2-associated proteins correlates with phospholipase Cγ1 activation in T cells. Mol Cell Biol 1996;16: 2823-9.
    • (1996) Mol Cell Biol , vol.16 , pp. 2823-2829
    • Motto, D.1    Musci, M.2    Ross, S.E.3    Koretzky, G.A.4
  • 22
    • 0030457304 scopus 로고    scopus 로고
    • Killer cell inhibitory receptor recognition of human leukocyte antigen (HLA) class I blocks formation of a pp36/PLC-γ signaling complex in human natural killer (NK) cells
    • Valiante NM, Phillips JH, Lanier LL, Parham P. Killer cell inhibitory receptor recognition of human leukocyte antigen (HLA) class I blocks formation of a pp36/PLC-γ signaling complex in human natural killer (NK) cells. J Exp Med 1996;184:2243-50.
    • (1996) J Exp Med , vol.184 , pp. 2243-2250
    • Valiante, N.M.1    Phillips, J.H.2    Lanier, L.L.3    Parham, P.4
  • 24
    • 0026643141 scopus 로고
    • Identification of calcineurin as a key signaling enzyme in T-lymphocyte activation
    • Clipstone NA, Crabtree GR. Identification of calcineurin as a key signaling enzyme in T-lymphocyte activation. Nature 1992;357:695-7.
    • (1992) Nature , vol.357 , pp. 695-697
    • Clipstone, N.A.1    Crabtree, G.R.2
  • 25
    • 0028936711 scopus 로고
    • NFATP, a cyclosporin-sensitive transcription factor implicated in cytokine gene induction
    • Rao A. NFATP, a cyclosporin-sensitive transcription factor implicated in cytokine gene induction. J Leukoc Biol 1995; 57:536-42.
    • (1995) J Leukoc Biol , vol.57 , pp. 536-542
    • Rao, A.1
  • 26
    • 0028582040 scopus 로고
    • Regulation and function of p21ras in T lymphocytes
    • Pastor MI, Woodrow M, Cantrell D. Regulation and function of p21ras in T lymphocytes. Cancer Surv 1995;22:75-83.
    • (1995) Cancer Surv , vol.22 , pp. 75-83
    • Pastor, M.I.1    Woodrow, M.2    Cantrell, D.3
  • 27
    • 0027357710 scopus 로고
    • Role of GTPases and GTPase regulatory proteins in oncogenesis
    • Grunicke HH, Maly K. Role of GTPases and GTPase regulatory proteins in oncogenesis. Crit Rev Oncog 1993;4:389-402.
    • (1993) Crit Rev Oncog , vol.4 , pp. 389-402
    • Grunicke, H.H.1    Maly, K.2
  • 29
    • 0028287296 scopus 로고
    • The role of Raf-1 in the regulation of extracellular signal-regulated kinase 2 by the T cell antigen receptor
    • Izquierdo M, Bowden S, Cantrell D. The role of Raf-1 in the regulation of extracellular signal-regulated kinase 2 by the T cell antigen receptor. J Exp Med 1994;180:401-6.
    • (1994) J Exp Med , vol.180 , pp. 401-406
    • Izquierdo, M.1    Bowden, S.2    Cantrell, D.3
  • 30
    • 0027521109 scopus 로고
    • Tyrosine phosphorylation and association with phospholipase Cγ-1 of the GAP-associated 62-kD protein after CD2 stimulation of Jurkat T cell
    • Hubert P, Debre P, Boumsell L, Bismuth G. Tyrosine phosphorylation and association with phospholipase Cγ-1 of the GAP-associated 62-kD protein after CD2 stimulation of Jurkat T cell. J Exp Med 1993;178:1587-96.
    • (1993) J Exp Med , vol.178 , pp. 1587-1596
    • Hubert, P.1    Debre, P.2    Boumsell, L.3    Bismuth, G.4
  • 31
    • 0027207287 scopus 로고
    • Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation
    • Gulbins E, Coggeshall KM, Baier G, Katzav S, Burn P, Altman A. Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation. Science 1993; 260:822-5.
    • (1993) Science , vol.260 , pp. 822-825
    • Gulbins, E.1    Coggeshall, K.M.2    Baier, G.3    Katzav, S.4    Burn, P.5    Altman, A.6
  • 32
    • 0026591451 scopus 로고
    • The hematopoietically expressed vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the ber gene and a yeast gene (CDC24) involved in cytoskeletal organization
    • Adams JM, Houston H, Allen J, Lints T, Harvey R. The hematopoietically expressed vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the ber gene and a yeast gene (CDC24) involved in cytoskeletal organization. Oncogene 1992;7:611-8.
    • (1992) Oncogene , vol.7 , pp. 611-618
    • Adams, J.M.1    Houston, H.2    Allen, J.3    Lints, T.4    Harvey, R.5
  • 34
    • 0030230376 scopus 로고    scopus 로고
    • The PI/PTB domain: A new protein interaction domain involved in growth factor receptor signaling
    • Margolis B. The PI/PTB domain: a new protein interaction domain involved in growth factor receptor signaling. J Lab Clin Med 1996;128:235-41.
    • (1996) J Lab Clin Med , vol.128 , pp. 235-241
    • Margolis, B.1
  • 35
    • 0027957728 scopus 로고
    • The GRB2/Sem-5 adaptor protein
    • Downward J. The GRB2/Sem-5 adaptor protein. FEBS Lett 1994;338:113-7.
    • (1994) FEBS Lett , vol.338 , pp. 113-117
    • Downward, J.1
  • 37
    • 0028888604 scopus 로고
    • The PTB domain: A new protein module implicated in signal transduction
    • van der Geer P, Pawson T. The PTB domain: a new protein module implicated in signal transduction. Trends Biochem Sci 1995;20:277-80.
    • (1995) Trends Biochem Sci , vol.20 , pp. 277-280
    • Van Der Geer, P.1    Pawson, T.2
  • 38
    • 0030002817 scopus 로고    scopus 로고
    • Characterization of the roles of SH2 domain-containing proteins in T-lymphocyte activation by using dominant negative SH2 domains
    • Northrop JP, Pustelnik MJ, Lu AT, Grove JR. Characterization of the roles of SH2 domain-containing proteins in T-lymphocyte activation by using dominant negative SH2 domains. Mol Cell Biol 1996;16:2255-63.
    • (1996) Mol Cell Biol , vol.16 , pp. 2255-2263
    • Northrop, J.P.1    Pustelnik, M.J.2    Lu, A.T.3    Grove, J.R.4
  • 39
    • 0028928422 scopus 로고
    • Molecular cloning of SLP-76, a 76 kDa tyrosine phosphoprotein associated with Grb2 in T cells
    • Jackman JK, Motto DG, Sun Q, Tanemoto M, Turck CW, Peltz GA, et al. Molecular cloning of SLP-76, a 76 kDa tyrosine phosphoprotein associated with Grb2 in T cells. J Biol Chem 1995;270:7029-32.
    • (1995) J Biol Chem , vol.270 , pp. 7029-7032
    • Jackman, J.K.1    Motto, D.G.2    Sun, Q.3    Tanemoto, M.4    Turck, C.W.5    Peltz, G.A.6
  • 40
    • 0030002904 scopus 로고    scopus 로고
    • Implication of the Grb2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production
    • Motto DG, Ross SE, Wu J, Hendricks-Taylor LR, Koretzky GA. Implication of the Grb2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production. J Exp Med 1996;183:1937-43.
    • (1996) J Exp Med , vol.183 , pp. 1937-1943
    • Motto, D.G.1    Ross, S.E.2    Wu, J.3    Hendricks-Taylor, L.R.4    Koretzky, G.A.5
  • 41
    • 0000082758 scopus 로고    scopus 로고
    • Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T cell receptor function
    • Wardenburg JB, Fu C, Jackman KJ, Flotow H, Wilkinson SE, Williams DH, et al. Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T cell receptor function. J Biol Chem 1996;271:19641-4.
    • (1996) J Biol Chem , vol.271 , pp. 19641-19644
    • Wardenburg, J.B.1    Fu, C.2    Jackman, K.J.3    Flotow, H.4    Wilkinson, S.E.5    Williams, D.H.6
  • 42
    • 85030292971 scopus 로고    scopus 로고
    • Three domains of SLP-76 are required for its optimal function in a T cell line
    • in press
    • Musci MA, Motto DG, Ross SE, Fang N, Koretzky GA. Three domains of SLP-76 are required for its optimal function in a T cell line. J Immunol (in press).
    • J Immunol
    • Musci, M.A.1    Motto, D.G.2    Ross, S.E.3    Fang, N.4    Koretzky, G.A.5
  • 43
    • 0001584956 scopus 로고    scopus 로고
    • Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation
    • Wu J, Motto DG, Koretzky GA, Weiss A. Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation. Immunity 1996;4:593-602.
    • (1996) Immunity , vol.4 , pp. 593-602
    • Wu, J.1    Motto, D.G.2    Koretzky, G.A.3    Weiss, A.4
  • 44
    • 0030959305 scopus 로고    scopus 로고
    • Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases
    • Musci MA, Hendricks-Taylor LR, Motto DG, Paskind M, Kamens J, Turck CW, et al. Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases. J Biol Chem 1997;272: 11674-7.
    • (1997) J Biol Chem , vol.272 , pp. 11674-11677
    • Musci, M.A.1    Hendricks-Taylor, L.R.2    Motto, D.G.3    Paskind, M.4    Kamens, J.5    Turck, C.W.6
  • 45
    • 0023120729 scopus 로고
    • Cell growth cycle block of T cell hybridomas upon activation with antigen
    • Ashwell JD, Cunningham RE, Noguchi PD, Hernandez D. Cell growth cycle block of T cell hybridomas upon activation with antigen. J Exp Med 1987;165:173-94.
    • (1987) J Exp Med , vol.165 , pp. 173-194
    • Ashwell, J.D.1    Cunningham, R.E.2    Noguchi, P.D.3    Hernandez, D.4
  • 46
    • 0030176384 scopus 로고    scopus 로고
    • Upstream-downstream: CD28 cosignaling pathways and T cell function
    • Rudd CE. Upstream-downstream: CD28 cosignaling pathways and T cell function. Immunity 1996;4:527-34.
    • (1996) Immunity , vol.4 , pp. 527-534
    • Rudd, C.E.1
  • 47
    • 0030025598 scopus 로고    scopus 로고
    • Comparison of CD28-B7.1 and B7.2 functional interaction in resting human T cells: Phosphatidylinositol 3-kinase association to CD28 and cytokine production
    • Ghiotto-Ragueneau M, Battifora M, Truneh A, Waterfield MD, Olive D. Comparison of CD28-B7.1 and B7.2 functional interaction in resting human T cells: phosphatidylinositol 3-kinase association to CD28 and cytokine production. Eur J Immunol 1996;26:34-41.
    • (1996) Eur J Immunol , vol.26 , pp. 34-41
    • Ghiotto-Ragueneau, M.1    Battifora, M.2    Truneh, A.3    Waterfield, M.D.4    Olive, D.5
  • 48
    • 0028802706 scopus 로고
    • Selective CD28pYMNM mutations implicate phosphatidylinositol 3-kinase in CD86-CD28-mediated costimulation
    • Cai YC, Cefai D, Schneider H, Raab M, Nabavi N, Rudd CE. Selective CD28pYMNM mutations implicate phosphatidylinositol 3-kinase in CD86-CD28-mediated costimulation. Immunity 1995;3:417-26.
    • (1995) Immunity , vol.3 , pp. 417-426
    • Cai, Y.C.1    Cefai, D.2    Schneider, H.3    Raab, M.4    Nabavi, N.5    Rudd, C.E.6
  • 49
    • 0027925818 scopus 로고
    • Structure and function of phosphatidylinositol 3-kinase: A potential second messenger system involved in growth control
    • Fry MJ, Waterfield MD. Structure and function of phosphatidylinositol 3-kinase: a potential second messenger system involved in growth control. Trans R Soc Lond 1993;340:337-44.
    • (1993) Trans R Soc Lond , vol.340 , pp. 337-344
    • Fry, M.J.1    Waterfield, M.D.2
  • 50
    • 0029161647 scopus 로고
    • CD28/CTLA-4 receptor structure, binding stoichiometry and aggregation during T cell activation
    • Linsley PS, Ledbetter J, Peach R, Bajorath J. CD28/CTLA-4 receptor structure, binding stoichiometry and aggregation during T cell activation. Res Immunol 1995;146:130-40.
    • (1995) Res Immunol , vol.146 , pp. 130-140
    • Linsley, P.S.1    Ledbetter, J.2    Peach, R.3    Bajorath, J.4
  • 51
    • 0030001318 scopus 로고    scopus 로고
    • Regulation of T cell receptor signaling by tyrosine phosphatase SYP association with CTLA-4
    • Marengere LE, Waterhouse P, Duncan GS, Mittrucker HW, Feng GS. Regulation of T cell receptor signaling by tyrosine phosphatase SYP association with CTLA-4. Science 1996; 272:1170-3.
    • (1996) Science , vol.272 , pp. 1170-1173
    • Marengere, L.E.1    Waterhouse, P.2    Duncan, G.S.3    Mittrucker, H.W.4    Feng, G.S.5
  • 52
    • 0028867420 scopus 로고
    • Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue destruction, revealing a critical negative regulatory role of CTLA-4
    • Tivol EA, Borriello F, Schweitzer AN, Lynch WP, Bluestone JA, Sharpe AH. Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue destruction, revealing a critical negative regulatory role of CTLA-4. Immunity 1995;3:541-7.
    • (1995) Immunity , vol.3 , pp. 541-547
    • Tivol, E.A.1    Borriello, F.2    Schweitzer, A.N.3    Lynch, W.P.4    Bluestone, J.A.5    Sharpe, A.H.6
  • 53
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S. Apoptosis by death factor. Cell 1997;88:355-65.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 54
    • 0029939945 scopus 로고    scopus 로고
    • The roles of costimulation and fas in T cell apoptosis and peripheral tolerance
    • Van Parjs L, Ibraghimov A, Abbas AK. The roles of costimulation and fas in T cell apoptosis and peripheral tolerance. Immunity 1996;4:321-8.
    • (1996) Immunity , vol.4 , pp. 321-328
    • Van Parjs, L.1    Ibraghimov, A.2    Abbas, A.K.3
  • 56
    • 0029899181 scopus 로고    scopus 로고
    • Molecular thanatopsis: A discourse on the Bcl2 family and cell death
    • Yang E, Korsmeyer SJ. Molecular thanatopsis: a discourse on the Bcl2 family and cell death. Blood 1996;88:386-401.
    • (1996) Blood , vol.88 , pp. 386-401
    • Yang, E.1    Korsmeyer, S.J.2


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