메뉴 건너뛰기




Volumn 159, Issue 4, 1997, Pages 1639-1647

Three Domains of SLP-76 Are Required for Its Optimal Function in a T Cell Line

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; DNA BINDING PROTEIN; LYMPHOCYTE ANTIGEN RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; NERVE PROTEIN; NUCLEAR PROTEIN; PHOSPHOPROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SLP 76 SIGNAL TRANSDUCING ADAPTOR PROTEINS; SLP-76 SIGNAL TRANSDUCING ADAPTOR PROTEINS; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR NFAT;

EID: 0031571263     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (72)

References (44)
  • 1
    • 0025325392 scopus 로고
    • Association of the Fyn protein tyrosine kinase with the T cell antigen receptor
    • Samelson, L., A. Phillips, E. Luong, and R. Klausner. 1990. Association of the Fyn protein tyrosine kinase with the T cell antigen receptor. Proc. Natl. Acad. Sci. USA 87:4358.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4358
    • Samelson, L.1    Phillips, A.2    Luong, E.3    Klausner, R.4
  • 2
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the Lck tyrosine kinase in signal transduction through the T cell antigen receptor
    • Straus, D., and A. Weiss. 1992. Genetic evidence for the involvement of the Lck tyrosine kinase in signal transduction through the T cell antigen receptor. Cell 70:585.
    • (1992) Cell , vol.70 , pp. 585
    • Straus, D.1    Weiss, A.2
  • 3
    • 0026483786 scopus 로고
    • ZAP-70: A 70kD protein tyrosine kinase that associates with the TCR zeta chain
    • Chan, A. C., M. Iwashima, C. W. Turck, and A. Weiss. 1992. ZAP-70: a 70kD protein tyrosine kinase that associates with the TCR zeta chain. Cell 71:649.
    • (1992) Cell , vol.71 , pp. 649
    • Chan, A.C.1    Iwashima, M.2    Turck, C.W.3    Weiss, A.4
  • 4
    • 0028209548 scopus 로고
    • Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases
    • Iwashima, M., B. A. Irving, N. S. van Oers, A. C. Chan, and A. Weiss. 1994. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science 263:1136.
    • (1994) Science , vol.263 , pp. 1136
    • Iwashima, M.1    Irving, B.A.2    Van Oers, N.S.3    Chan, A.C.4    Weiss, A.5
  • 5
    • 0029031806 scopus 로고
    • Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins
    • Neumeister, E. N., Y. Zhu, S. Richard, C. Terhorst, A. C. Chan, and A. S. Shaw. 1995. Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins. Mol. Cell. Biol. 15:3171.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3171
    • Neumeister, E.N.1    Zhu, Y.2    Richard, S.3    Terhorst, C.4    Chan, A.C.5    Shaw, A.S.6
  • 6
    • 0028887998 scopus 로고
    • Multiple kinases mediate T-cell-receptor signaling
    • Howe, L. R., and A. Weiss. 1995. Multiple kinases mediate T-cell-receptor signaling. Trends Biochem. Sci. 20:51.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 51
    • Howe, L.R.1    Weiss, A.2
  • 7
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A., and D. R. Littman. 1994. Signal transduction by lymphocyte antigen receptors. Cell 76:263.
    • (1994) Cell , vol.76 , pp. 263
    • Weiss, A.1    Littman, D.R.2
  • 8
    • 0027957728 scopus 로고
    • The GRB2/Sem-5 adaptor protein
    • Downward, J. 1994. The GRB2/Sem-5 adaptor protein. FEBS Lett. 338:113.
    • (1994) FEBS Lett. , vol.338 , pp. 113
    • Downward, J.1
  • 9
    • 0028227284 scopus 로고
    • SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: The guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases
    • Reif, K., L. Buday, J. Downward, and D. A. Cantrell. 1994. SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: the guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases. J. Biol. Chem. 269:14081.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14081
    • Reif, K.1    Buday, L.2    Downward, J.3    Cantrell, D.A.4
  • 10
    • 0028245832 scopus 로고
    • A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells
    • Buday, L., S. E. Egan, P. Rodriguez Viciana, D. A. Cantrell, and J. Downward. 1994. A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells. J. Biol. Chem. 269:9019.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9019
    • Buday, L.1    Egan, S.E.2    Rodriguez Viciana, P.3    Cantrell, D.A.4    Downward, J.5
  • 11
    • 0028101039 scopus 로고
    • In vivo association of Grb2 with pp116, a substrate of the T cell antigen receptor-activated protein tyrosine kinase
    • Motto, D. G., S. E. Ross, J. K. Jackman, Q. Sun, A. L. Olson, P. R. Findell, and G. A. Koretzky. 1994. In vivo association of Grb2 with pp116, a substrate of the T cell antigen receptor-activated protein tyrosine kinase. J. Biol. Chem. 269: 21608.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21608
    • Motto, D.G.1    Ross, S.E.2    Jackman, J.K.3    Sun, Q.4    Olson, A.L.5    Findell, P.R.6    Koretzky, G.A.7
  • 12
    • 0028180585 scopus 로고
    • GRB2 and phospholipase C-gamma 1 associate with a 36- To 38-kilodalton phosphotyrosine protein after T-cell receptor stimulation
    • Sieh, M., A. Batzer, J. Schlessinger, and A. Weiss. 1994. GRB2 and phospholipase C-gamma 1 associate with a 36-to 38-kilodalton phosphotyrosine protein after T-cell receptor stimulation. Mol. Cell. Biol. 14:4435.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4435
    • Sieh, M.1    Batzer, A.2    Schlessinger, J.3    Weiss, A.4
  • 13
    • 0029999327 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Grb2-associatcd proteins correlates with phospholipase C-gamma-1 in T cells
    • Motto, D. G., M. A. Musci, S. E. Ross, and G. A. Koretzky. 1996. Tyrosine phosphorylation of Grb2-associatcd proteins correlates with phospholipase C-gamma-1 in T cells. Mol. Cell. biol. 16:2823.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2823
    • Motto, D.G.1    Musci, M.A.2    Ross, S.E.3    Koretzky, G.A.4
  • 14
    • 0025819499 scopus 로고
    • The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large truncation encompassing a proline-rich domain and a leucine zipper-like motif
    • Blake, T., M. Shapiro, H. Morse, and W. Langdon. 1991. The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large truncation encompassing a proline-rich domain and a leucine zipper-like motif. Oncogene 6:653.
    • (1991) Oncogene , vol.6 , pp. 653
    • Blake, T.1    Shapiro, M.2    Morse, H.3    Langdon, W.4
  • 15
    • 0027215275 scopus 로고
    • The truncation that generated the v-cbl oncogene reveals an ability for nuclear transport, DNA binding, and acute transformation
    • Blake, T., K. Heath, and W. Langdon. 1993. The truncation that generated the v-cbl oncogene reveals an ability for nuclear transport, DNA binding, and acute transformation. EMBO J. 12:2017.
    • (1993) EMBO J. , vol.12 , pp. 2017
    • Blake, T.1    Heath, K.2    Langdon, W.3
  • 16
    • 0028027169 scopus 로고
    • The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor
    • Donovan, J. A., R. L. Wange, W. Y. Langdon, and L. E. Samelson. 1994. The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor. J. Biol. Chem. 269:22921.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22921
    • Donovan, J.A.1    Wange, R.L.2    Langdon, W.Y.3    Samelson, L.E.4
  • 17
    • 0029034440 scopus 로고
    • Interactions of Cbl with Grb2 and phosphatidylinositol 3′-kinase in activated Jurkat cells
    • Meisner, H., B. R. Conway, D. Hartley, and M. P. Czech. 1995. Interactions of Cbl with Grb2 and phosphatidylinositol 3′-kinase in activated Jurkat cells. Mol. Cell. Biol. 15:3571.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3571
    • Meisner, H.1    Conway, B.R.2    Hartley, D.3    Czech, M.P.4
  • 19
    • 0030293529 scopus 로고    scopus 로고
    • Tyrosines 113, 128, and 145 of SLP-76 are required for optimal augmentation of NF-AT promoter activity
    • Fang, N., D. G. Motto, S. E. Ross, and G. A. Koretzky. 1996. Tyrosines 113, 128, and 145 of SLP-76 are required for optimal augmentation of NF-AT promoter activity. J. Immunol. 157:3769.
    • (1996) J. Immunol. , vol.157 , pp. 3769
    • Fang, N.1    Motto, D.G.2    Ross, S.E.3    Koretzky, G.A.4
  • 20
    • 0001584956 scopus 로고    scopus 로고
    • Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation
    • Wu, J., D. G. Motto, G. A. Koretzky, and A. Weiss. 1996. Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation. Immunity 4:593.
    • (1996) Immunity , vol.4 , pp. 593
    • Wu, J.1    Motto, D.G.2    Koretzky, G.A.3    Weiss, A.4
  • 21
    • 0029658306 scopus 로고    scopus 로고
    • p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells
    • Tuosto, L., F. Michel, and O. Acuto. 1996. p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells. J. Exp. Med. 184:1161.
    • (1996) J. Exp. Med. , vol.184 , pp. 1161
    • Tuosto, L.1    Michel, F.2    Acuto, O.3
  • 22
    • 0029832707 scopus 로고    scopus 로고
    • Differential regulation of activation-induced tyrosine phosphorylation and recruitment of SLP-76 to Vav by distinct isoforms of the CD45 protein-tyrosine phosphatase
    • Onodera, H., D. G. Motto, G. A. Koretzky, and D. M. Rothstein. 1996. Differential regulation of activation-induced tyrosine phosphorylation and recruitment of SLP-76 to Vav by distinct isoforms of the CD45 protein-tyrosine phosphatase. J. Biol. Chem. 271:22225.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22225
    • Onodera, H.1    Motto, D.G.2    Koretzky, G.A.3    Rothstein, D.M.4
  • 23
    • 0028595695 scopus 로고
    • The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav
    • Katzav, S., M. Sutherland, G. Packham, T. Yi, and A. Weiss. 1994. The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav. J. Biol. Chem. 269:32579.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32579
    • Katzav, S.1    Sutherland, M.2    Packham, G.3    Yi, T.4    Weiss, A.5
  • 24
    • 0026535589 scopus 로고
    • Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs
    • Margolis, B., P. Hu, S. Katzav, W. Li, J. M. Oliver, A. Ullrich, A. Weiss, and J. Schlessinger. 1992. Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs. Nature 356:71.
    • (1992) Nature , vol.356 , pp. 71
    • Margolis, B.1    Hu, P.2    Katzav, S.3    Li, W.4    Oliver, J.M.5    Ullrich, A.6    Weiss, A.7    Schlessinger, J.8
  • 25
    • 0030002904 scopus 로고    scopus 로고
    • Implication of the Grb2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production
    • Motto, D. G., S. E. Ross, J. Wu, L. R. Hendricks-Taylor, and G. A. Koretzky. 1996. Implication of the Grb2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production. J. Exp. Med. 183:1937.
    • (1996) J. Exp. Med. , vol.183 , pp. 1937
    • Motto, D.G.1    Ross, S.E.2    Wu, J.3    Hendricks-Taylor, L.R.4    Koretzky, G.A.5
  • 27
    • 0024341976 scopus 로고
    • Function of a heterologous muscarinic receptor in T cell antigen receptor signal transduction mutants
    • Goldsmith, M. A., D. M. Desai, T. Schultz, and A. Weiss. 1989. Function of a heterologous muscarinic receptor in T cell antigen receptor signal transduction mutants. J. Biol. Chem. 264:17190.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17190
    • Goldsmith, M.A.1    Desai, D.M.2    Schultz, T.3    Weiss, A.4
  • 28
    • 0024991898 scopus 로고
    • pEF-BOS, a powerful mammalian expression vector
    • Mizushima, S., and S. Nagata. 1990 pEF-BOS, a powerful mammalian expression vector. Nucleic Acids Res. 18:5322.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5322
    • Mizushima, S.1    Nagata, S.2
  • 29
    • 0030038488 scopus 로고    scopus 로고
    • Fas ligation induces apoptosis and Jun kinase activation independently of CD45 and Lck in human T cells
    • Latinis, K. M., and G. A. Koretzky. 1996. Fas ligation induces apoptosis and Jun kinase activation independently of CD45 and Lck in human T cells. Blood 87: 871.
    • (1996) Blood , vol.87 , pp. 871
    • Latinis, K.M.1    Koretzky, G.A.2
  • 30
    • 0021678703 scopus 로고
    • Requirement for the coexpression of T3 and the T cell antigen receptor on a malignant human T cell line
    • Weiss, A., and J. D. Stobo. 1984. Requirement for the coexpression of T3 and the T cell antigen receptor on a malignant human T cell line. J. Exp. Med. 160:1284.
    • (1984) J. Exp. Med. , vol.160 , pp. 1284
    • Weiss, A.1    Stobo, J.D.2
  • 31
    • 0026725397 scopus 로고
    • Electroporation in 'intracellular' buffer increases cell survival
    • van den Hoff, M. J., A. F. Moorman, and W. H. Lamers. 1992. Electroporation in 'intracellular' buffer increases cell survival. Nucleic Acids Res. 20:2902.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 2902
    • Van Den Hoff, M.J.1    Moorman, A.F.2    Lamers, W.H.3
  • 32
    • 0024999862 scopus 로고
    • Stimulation of the phosphatidylinositol pathway can induce T-cell activation
    • Desai, D. M., M. K. Newton, T. Kadlecek, and A. Weiss. 1990. Stimulation of the phosphatidylinositol pathway can induce T-cell activation. Nature 348:66.
    • (1990) Nature , vol.348 , pp. 66
    • Desai, D.M.1    Newton, M.K.2    Kadlecek, T.3    Weiss, A.4
  • 33
    • 0025871394 scopus 로고
    • Nuclear association of a T cell-transcription factor blocked by FK-506 and cyclosporin A
    • Flanagan, W. F., B. Corthesy, R. J. Bram, and G. R. Crabtree. 1990. Nuclear association of a T cell-transcription factor blocked by FK-506 and cyclosporin A. Nature 352:803.
    • (1990) Nature , vol.352 , pp. 803
    • Flanagan, W.F.1    Corthesy, B.2    Bram, R.J.3    Crabtree, G.R.4
  • 34
    • 0026596383 scopus 로고
    • Nuclear factor of activated T cells contains Fos and Jun
    • Jain, J., P. G. McCaffrey, V. E. Valge-Archer, and A. Rao. 1992. Nuclear factor of activated T cells contains Fos and Jun. Nature 356:801.
    • (1992) Nature , vol.356 , pp. 801
    • Jain, J.1    McCaffrey, P.G.2    Valge-Archer, V.E.3    Rao, A.4
  • 35
  • 36
    • 0026625939 scopus 로고
    • Immunophilin-sensitive protein phosphatase action in cell signaling pathways
    • Schreiber, S. L. 1992. Immunophilin-sensitive protein phosphatase action in cell signaling pathways. Cell 70:365.
    • (1992) Cell , vol.70 , pp. 365
    • Schreiber, S.L.1
  • 37
    • 0025720735 scopus 로고
    • The role of Jun, Fos, and the AP-1 complex in cell-proliferation and transformation
    • Angel, P., and M. Karin. 1991. The role of Jun, Fos, and the AP-1 complex in cell-proliferation and transformation. Biochim. Biophys. Acta 1072:129.
    • (1991) Biochim. Biophys. Acta , vol.1072 , pp. 129
    • Angel, P.1    Karin, M.2
  • 38
    • 0026695645 scopus 로고
    • Phosphorylation of p62TCF by MAP kinase stimulates ternary complex formation at c-FOS promoter
    • Gille, H., A. Sharrocks, and P. Shaw. 1992. Phosphorylation of p62TCF by MAP kinase stimulates ternary complex formation at c-FOS promoter. Nature 358:414.
    • (1992) Nature , vol.358 , pp. 414
    • Gille, H.1    Sharrocks, A.2    Shaw, P.3
  • 39
    • 0025806587 scopus 로고
    • Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domain
    • Binetruy, B., T. Smeal, and M. Karin. 1991. Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domain. Nature 351:122.
    • (1991) Nature , vol.351 , pp. 122
    • Binetruy, B.1    Smeal, T.2    Karin, M.3
  • 41
    • 0028302767 scopus 로고
    • The T-cell antigen receptor utilizes Lck, Raf-1, and MEK-1 for activating mitogen-activated protein kinase: Evidence for the existence of a second protein kinase C-dependenl pathway in an Lck-negative Jurkat cell mutant
    • Gupta, S., A. Weiss, G. Kumar, S. Wang, and A. Nel. 1994. The T-cell antigen receptor utilizes Lck, Raf-1, and MEK-1 for activating mitogen-activated protein kinase: evidence for the existence of a second protein kinase C-dependenl pathway in an Lck-negative Jurkat cell mutant. J. Biol. Chem. 269:17349.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17349
    • Gupta, S.1    Weiss, A.2    Kumar, G.3    Wang, S.4    Nel, A.5
  • 42
    • 0027337561 scopus 로고
    • ras couples the T cell antigen receptor to extracellular signal-regulated kinase 2 in T lymphocytes
    • ras couples the T cell antigen receptor to extracellular signal-regulated kinase 2 in T lymphocytes. J. Exp. Med. 178:1199.
    • (1993) J. Exp. Med. , vol.178 , pp. 1199
    • Izquierdo, M.1    Leevers, S.J.2    Marshall, C.J.3    Cantrell, D.4
  • 43
    • 0028872649 scopus 로고    scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall, C. J. 1996. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179.
    • (1996) Cell , vol.80 , pp. 179
    • Marshall, C.J.1
  • 44
    • 0030959305 scopus 로고    scopus 로고
    • Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell receptor-stimulated protein tyrosine kinases
    • Musci, M. A., L. R. Hendricks-Taylor, D. G. Motto, M. Paskin, J. Kamens, C. W. Turck, and G. A. Koretzky. 1997. Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell receptor-stimulated protein tyrosine kinases. J. Biol. Chem. 270:11674.
    • (1997) J. Biol. Chem. , vol.270 , pp. 11674
    • Musci, M.A.1    Hendricks-Taylor, L.R.2    Motto, D.G.3    Paskin, M.4    Kamens, J.5    Turck, C.W.6    Koretzky, G.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.