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Volumn 157, Issue 9, 1996, Pages 3775-3782

The Catalytic Domain of pp56lck, but Not Its Regulatory Domain, Is Sufficient for Inducing IL-2 Production

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; DNA BINDING PROTEIN; INTERLEUKIN 2; IONOMYCIN; IONOPHORE; LYMPHOCYTE ANTIGEN RECEPTOR; NUCLEAR PROTEIN; PEPTIDE FRAGMENT; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE LCK; PROTEIN TYROSINE KINASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR NFAT; TUMOR PROTEIN;

EID: 0030293621     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (2)

References (45)
  • 3
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the lck Tyr kinase in signal transduction through the T cell antigen receptor
    • Straus, D. B., and A. Weiss. 1992. Genetic evidence for the involvement of the lck Tyr kinase in signal transduction through the T cell antigen receptor. Cell 70:585.
    • (1992) Cell , vol.70 , pp. 585
    • Straus, D.B.1    Weiss, A.2
  • 6
    • 0026612411 scopus 로고
    • fyn mutant mice display differential signaling in thymocytes and peripheral T cells
    • fyn mutant mice display differential signaling in thymocytes and peripheral T cells. Cell 70:741.
    • (1992) Cell , vol.70 , pp. 741
    • Stein, P.L.1    Lee, H.-M.2    Rich, S.3    Soriano, P.4
  • 11
    • 0003102172 scopus 로고
    • The src-family of protein kinases
    • B. Kemp and P. F. Alewood, eds. CRC Press, Boca Raton
    • Cooper, J. A. 1990. The src-family of protein kinases. In Peptides and Protein Phosphorylation. B. Kemp and P. F. Alewood, eds. CRC Press, Boca Raton, pp. 85.
    • (1990) Peptides and Protein Phosphorylation , pp. 85
    • Cooper, J.A.1
  • 13
    • 0024425159 scopus 로고
    • The lck tyrosine protein kinase interacts with the cytoplasmic tail of CD4 glycoprotein through its unique amino-terminal domain
    • Shaw, A. S., K. E. Amrein, C. Hammond, D. F. Stern, B. M. Sefton, and J. K. Rose. 1989. The lck tyrosine protein kinase interacts with the cytoplasmic tail of CD4 glycoprotein through its unique amino-terminal domain. Cell 59:627.
    • (1989) Cell , vol.59 , pp. 627
    • Shaw, A.S.1    Amrein, K.E.2    Hammond, C.3    Stern, D.F.4    Sefton, B.M.5    Rose, J.K.6
  • 14
    • 0025017463 scopus 로고
    • Structural nature of the interaction between T lymphocyte surface molecule CD4 and the intracellular protein kinase lck
    • Vega, M. A., M. C. Kuo, A. C. Carrera, and J. L. Strominger. 1990. Structural nature of the interaction between T lymphocyte surface molecule CD4 and the intracellular protein kinase lck. Eur. J. Immunol. 20:453.
    • (1990) Eur. J. Immunol. , vol.20 , pp. 453
    • Vega, M.A.1    Kuo, M.C.2    Carrera, A.C.3    Strominger, J.L.4
  • 15
    • 0025765803 scopus 로고
    • SH2 and SH3 elements that control interactions of cytoplasmic signaling molecules
    • Koch, C. A., D. Anderson, M. F. Moran, C. Ellis, and T. Pawson. 1991. SH2 and SH3 elements that control interactions of cytoplasmic signaling molecules. Science 252:668.
    • (1991) Science , vol.252 , pp. 668
    • Koch, C.A.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 17
    • 0027257445 scopus 로고
    • A kinase-independent function of lck in potentiating antigen-specific T cell activation
    • Xu, H., and D. R., Littman. 1993. A kinase-independent function of lck in potentiating antigen-specific T cell activation. Cell 74:633.
    • (1993) Cell , vol.74 , pp. 633
    • Xu, H.1    Littman, D.R.2
  • 19
    • 0026639958 scopus 로고
    • Activated lck tyrosine protein kinase stimulates antigen independent inlerleukin-2 production in T cells
    • Luo, K., and B. Sefton. 1992. Activated lck tyrosine protein kinase stimulates antigen independent inlerleukin-2 production in T cells. Mol. Cell. Biol. 12:4724.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4724
    • Luo, K.1    Sefton, B.2
  • 20
    • 0027732861 scopus 로고
    • Closing in on SH2 specificity
    • Birge, R. B., and H. Hanafusa. 1993. Closing in on SH2 specificity. Science 262:1522.
    • (1993) Science , vol.262 , pp. 1522
    • Birge, R.B.1    Hanafusa, H.2
  • 21
    • 0027439438 scopus 로고
    • The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP
    • Carrera, A. C., K. Alexandrov, and T. M. Roberts. 1993. The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP. Proc. Natl. Acad. Sci. USA 90: 4442.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4442
    • Carrera, A.C.1    Alexandrov, K.2    Roberts, T.M.3
  • 22
    • 0025127909 scopus 로고
    • Cell type specificity and activation requirements for NF-AT-1 (nuclear factor of activated T cells) transcriptional activity determined by a new method using transgenic mice to assay transcriptional activity of an activated nuclear factor
    • Verweij, C. L., C. Guidos, and G. R. Crabtree. 1990. Cell type specificity and activation requirements for NF-AT-1 (nuclear factor of activated T cells) transcriptional activity determined by a new method using transgenic mice to assay transcriptional activity of an activated nuclear factor. J. Biol. Chem. 265:15788.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15788
    • Verweij, C.L.1    Guidos, C.2    Crabtree, G.R.3
  • 25
    • 0021922374 scopus 로고
    • Antigen-specific cytotoxic T cell and antigen-specific proliferating T cell clones can be induced to cytolytic activity by monoclonal Abs against T3
    • Spits, H., H. Yssel, J. Leeuwenberg, and J. E. De Vries. 1985. Antigen-specific cytotoxic T cell and antigen-specific proliferating T cell clones can be induced to cytolytic activity by monoclonal Abs against T3. Eur. J. Immunol. 15:88.
    • (1985) Eur. J. Immunol. , vol.15 , pp. 88
    • Spits, H.1    Yssel, H.2    Leeuwenberg, J.3    De Vries, J.E.4
  • 26
    • 0028206512 scopus 로고
    • Induction, characterization, and functional coupling of the high affinity chemokine receptor for RANTES and macrophage Inflammatory protein-1α upon differentiation of an eosinophilic HL-60 cell line
    • Riper, G. V., D. W. Nicholson, M. P. Scheid, P. A. Fisher, M. S. Springer, and H. Rosen. 1994. Induction, characterization, and functional coupling of the high affinity chemokine receptor for RANTES and macrophage Inflammatory protein-1α upon differentiation of an eosinophilic HL-60 cell line. J. Immunol. 152: 4055.
    • (1994) J. Immunol. , vol.152 , pp. 4055
    • Riper, G.V.1    Nicholson, D.W.2    Scheid, M.P.3    Fisher, P.A.4    Springer, M.S.5    Rosen, H.6
  • 27
    • 0023806075 scopus 로고
    • Single step purification of polypeptides expressed in Escherichia coli as fusions with gluthathione 5-transferase
    • Smith, D. B., and K. S. Johnson. 1988. Single step purification of polypeptides expressed in Escherichia coli as fusions with gluthathione 5-transferase. Gene 61:31.
    • (1988) Gene , vol.61 , pp. 31
    • Smith, D.B.1    Johnson, K.S.2
  • 29
    • 0025194606 scopus 로고
    • lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation
    • lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation. Mol. Cell. Biol. 10:5197.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5197
    • Abraham, N.1    Veillette, A.2
  • 31
    • 0024548313 scopus 로고
    • Contingent genetic regulatory events in T lymphocyte activation
    • Crabtree, O. R. 1989. Contingent genetic regulatory events in T lymphocyte activation. Science 243:355.
    • (1989) Science , vol.243 , pp. 355
    • Crabtree, O.R.1
  • 32
    • 0027336340 scopus 로고
    • ras function is important for T cell antigen receptor and protein kinase C regulation of nuclear factor of activated T cells
    • ras function is important for T cell antigen receptor and protein kinase C regulation of nuclear factor of activated T cells. J. Immunol. 150:3853.
    • (1993) J. Immunol. , vol.150 , pp. 3853
    • Wooddrow, M.A.1    Rayter, S.2    Downward, J.3    Cantrell, D.A.4
  • 34
    • 0022202907 scopus 로고
    • Tumor promoters in conjunction with calcium ionophores mimic antigen stimulation by reactivation of alloantigen primed T lymphocytes
    • Isakov, N., and A. Altman. 1985. Tumor promoters in conjunction with calcium ionophores mimic antigen stimulation by reactivation of alloantigen primed T lymphocytes. J. Immunol. 135:3674.
    • (1985) J. Immunol. , vol.135 , pp. 3674
    • Isakov, N.1    Altman, A.2
  • 35
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Nishizuka, Y. 1986. Studies and perspectives of protein kinase C. Science 233: 305.
    • (1986) Science , vol.233 , pp. 305
    • Nishizuka, Y.1
  • 36
    • 0026607074 scopus 로고
    • CD28 and T cell antigen receptor coordinately regulate IL-2 gene expression in response to superantigen stimulation
    • Fraser, J. D., M. E. Newton, and A. Weiss. 1992. CD28 and T cell antigen receptor coordinately regulate IL-2 gene expression in response to superantigen stimulation. J. Exp. Med. 175:1131.
    • (1992) J. Exp. Med. , vol.175 , pp. 1131
    • Fraser, J.D.1    Newton, M.E.2    Weiss, A.3
  • 37
    • 0028304143 scopus 로고
    • Activation of the src family kinase lck following CD28 crosslinking in the Jurkat leukemic cell line
    • August, A., and B. Dupont. 1994. Activation of the src family kinase lck following CD28 crosslinking in the Jurkat leukemic cell line. Biochem. Biophys. Res. Commun. 199:1466.
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 1466
    • August, A.1    Dupont, B.2
  • 38
    • 0023908650 scopus 로고
    • Early signal transduction by the antigen receptor without commitment to T cell activation
    • Goldsmith, M. A., and A. Weiss. 1988. Early signal transduction by the antigen receptor without commitment to T cell activation. Science 240:1029.
    • (1988) Science , vol.240 , pp. 1029
    • Goldsmith, M.A.1    Weiss, A.2
  • 39
    • 0026730381 scopus 로고
    • Functional analysis of the SH2 and SH3 domains of the lck tyrosine protein kinase
    • Reynolds, P. J., T. R. Hurley, and B. M. Sefton. 1992. Functional analysis of the SH2 and SH3 domains of the lck tyrosine protein kinase. Oncogene 7:1949.
    • (1992) Oncogene , vol.7 , pp. 1949
    • Reynolds, P.J.1    Hurley, T.R.2    Sefton, B.M.3
  • 40
    • 0028467163 scopus 로고
    • An activated lck transgene promotes thymocyte development in rag-1 mutant mice
    • Mombaerts, P., S. J. Anderson, R. M. Perlmutter, T. W. Mak, and S. Tonegawa. 1994. An activated lck transgene promotes thymocyte development in rag-1 mutant mice. Immunity 1:261.
    • (1994) Immunity , vol.1 , pp. 261
    • Mombaerts, P.1    Anderson, S.J.2    Perlmutter, R.M.3    Mak, T.W.4    Tonegawa, S.5
  • 44
    • 0027408247 scopus 로고
    • Identification of a ten-aminoacid proline-rich SH3 binding site
    • Ren, R., B. J. Mayer, P. Cicchetti, and D. Baltimore. 1993. Identification of a ten-aminoacid proline-rich SH3 binding site. Science 259:1157.
    • (1993) Science , vol.259 , pp. 1157
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 45
    • 0027170920 scopus 로고
    • SH3 domains direct cellular localization of signaling molecules
    • Bar-Sagi, D., D. Rotin, A. Batzer, V. Mandiyan, and J. Schlessinger. 1993. SH3 domains direct cellular localization of signaling molecules. Cell 74:83.
    • (1993) Cell , vol.74 , pp. 83
    • Bar-Sagi, D.1    Rotin, D.2    Batzer, A.3    Mandiyan, V.4    Schlessinger, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.