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Volumn 160, Issue 9, 1998, Pages 4182-4189

Activation of p21-CDC42/Rac-activated kinases by CD28 signaling: p21- activated kinase (PAK) and MEK kinase 1 (MEKK1) may mediate the interplay between CD3 and CD28 signals

Author keywords

[No Author keywords available]

Indexed keywords

CD28 ANTIGEN; CD3 ANTIGEN; CELL SURFACE RECEPTOR; CERAMIDE; GUANINE NUCLEOTIDE BINDING PROTEIN; INTERLEUKIN 2; PROTEIN P21; T LYMPHOCYTE RECEPTOR;

EID: 0032080604     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (72)

References (44)
  • 1
    • 0023720148 scopus 로고
    • T cell antigen receptor genes and T cell recognition
    • Davis, M. M., and P. J. Bjorkman. 1988. T cell antigen receptor genes and T cell recognition. Nature 334:395.
    • (1988) Nature , vol.334 , pp. 395
    • Davis, M.M.1    Bjorkman, P.J.2
  • 2
    • 0029874657 scopus 로고    scopus 로고
    • T cell antigen receptor signal transduction pathways
    • Cantrell, D. 1996. T cell antigen receptor signal transduction pathways. Annu. Rev. Immunol. 14:259.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 259
    • Cantrell, D.1
  • 3
    • 43949164661 scopus 로고
    • Signal transduction events leading to T-cell lymphokine gene expression
    • Fraser, J. D., D. Straus, and A. Weiss. 1993. Signal transduction events leading to T-cell lymphokine gene expression. Immunol. Today 14:357.
    • (1993) Immunol. Today , vol.14 , pp. 357
    • Fraser, J.D.1    Straus, D.2    Weiss, A.3
  • 4
    • 0023514599 scopus 로고
    • Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system
    • Aruffo, A., and B. Seed. 1987. Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system. Proc. Natl. Acad. Sci. USA 84:8573.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8573
    • Aruffo, A.1    Seed, B.2
  • 5
    • 0028342859 scopus 로고
    • CD28 of T lymphocytes associates with phosphatidylinositol 3-kinase
    • August, A., and B. Dupont. 1995. CD28 of T lymphocytes associates with phosphatidylinositol 3-kinase. Int. Immunol 6:769.
    • (1995) Int. Immunol , vol.6 , pp. 769
    • August, A.1    Dupont, B.2
  • 6
    • 0028118512 scopus 로고
    • Stimulation of CD28 triggers an association between CD28 and phosphatidylinositol 3-kinase in Jurkat cells
    • Truitt, K. E., C. M. Hicks, and J. B. Imboden. 1994. Stimulation of CD28 triggers an association between CD28 and phosphatidylinositol 3-kinase in Jurkat cells. J. Exp. Med. 179:1071.
    • (1994) J. Exp. Med. , vol.179 , pp. 1071
    • Truitt, K.E.1    Hicks, C.M.2    Imboden, J.B.3
  • 7
    • 0028221022 scopus 로고
    • T-cell antigen CD28 interacts with the lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr(P)-Met-Xaa-Met motif
    • Prasad, K. V. S., Y.-C. Cai, M. Raab, B. Duckworth, L. Cantley, S. E. Shoelson, and C. E. Rudd. 1994. T-cell antigen CD28 interacts with the lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr(P)-Met-Xaa-Met motif. Proc. Natl. Acad. Sci. USA 91:2834.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2834
    • Prasad, K.V.S.1    Cai, Y.-C.2    Raab, M.3    Duckworth, B.4    Cantley, L.5    Shoelson, S.E.6    Rudd, C.E.7
  • 8
    • 0028972712 scopus 로고
    • CD28-mediated costimulation in the absence of phosphatidylinositol 3-kinase association and activation
    • Crooks, M. E., D. R. Littman, R. H. Carter, D. T. Fearon, A. Weiss, and P. E. Stein. 1995. CD28-mediated costimulation in the absence of phosphatidylinositol 3-kinase association and activation. Mol. Cell. Biol. 15:6820.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6820
    • Crooks, M.E.1    Littman, D.R.2    Carter, R.H.3    Fearon, D.T.4    Weiss, A.5    Stein, P.E.6
  • 9
    • 0028956419 scopus 로고
    • Phosphatidylinositol 3-kinase activity is not essential for CD28 costimulatory activity in Jurkat T cells: Studies with a selective inhibitor, wortmannin
    • Lu, Y., C. A. Phillips, and J. M. Trevillyan. 1995. Phosphatidylinositol 3-kinase activity is not essential for CD28 costimulatory activity in Jurkat T cells: studies with a selective inhibitor, wortmannin. Eur. J. Immunol. 25:533.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 533
    • Lu, Y.1    Phillips, C.A.2    Trevillyan, J.M.3
  • 10
    • 0029056902 scopus 로고
    • Phorbol ester treatment inhibits phosphatidylinositol 3-kinase activation by, and association with, CD28, a T-lymphocyte surface receptor
    • Hutchcroft, J. E., D. P. Franklin, B. Tsai, D. Harrison-Findik, L. Varticovski, and B. E. Bierer. 1995. Phorbol ester treatment inhibits phosphatidylinositol 3-kinase activation by, and association with, CD28, a T-lymphocyte surface receptor. Proc. Natl. Acad. Sci. USA 92:8808.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8808
    • Hutchcroft, J.E.1    Franklin, D.P.2    Tsai, B.3    Harrison-Findik, D.4    Varticovski, L.5    Bierer, B.E.6
  • 11
    • 0028169441 scopus 로고
    • The role of p21ras in CD28 signal transduction: Triggering of CD28 with antibodies, but not the ligand B7-1, activates p21ras
    • Nunès, J. A., Y. Collette, A. Truneh, D. Olive, and D. A. Cantrell. 1994. The role of p21ras in CD28 signal transduction: triggering of CD28 with antibodies, but not the ligand B7-1, activates p21ras. J. Exp. Med. 180:1067.
    • (1994) J. Exp. Med. , vol.180 , pp. 1067
    • Nunès, J.A.1    Collette, Y.2    Truneh, A.3    Olive, D.4    Cantrell, D.A.5
  • 13
    • 0029035315 scopus 로고
    • Sphingomyelin-ceramide turnover in CD28 co-stimulatory signalling
    • Chan, G., and A. Ochi. 1995. Sphingomyelin-ceramide turnover in CD28 co-stimulatory signalling. Eur. J. Immunol. 25:1999.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 1999
    • Chan, G.1    Ochi, A.2
  • 15
    • 0027461121 scopus 로고
    • Activation of the sphingomyelin signalling pathway in intact EL4 cells and in a cell-free system by IL-1β
    • Mathias, S., A. Younes, C. Kan, I. Orlow, C. Joseph, and R. N. Kolesnick. 1993. Activation of the sphingomyelin signalling pathway in intact EL4 cells and in a cell-free system by IL-1β. Science 259:519.
    • (1993) Science , vol.259 , pp. 519
    • Mathias, S.1    Younes, A.2    Kan, C.3    Orlow, I.4    Joseph, C.5    Kolesnick, R.N.6
  • 18
    • 0028291525 scopus 로고
    • JNK is involved in signal integration during costimulation of T lymphocytes
    • Su, B., E. Jacinto, M. Hibi, T. Kallunki, M. Karin, and Y. Ben-Neriah. 1994. JNK is involved in signal integration during costimulation of T lymphocytes. Cell 77:727.
    • (1994) Cell , vol.77 , pp. 727
    • Su, B.1    Jacinto, E.2    Hibi, M.3    Kallunki, T.4    Karin, M.5    Ben-Neriah, Y.6
  • 19
    • 0030803278 scopus 로고    scopus 로고
    • Fas- Or ceramide-induced apoptosis is mediated by a Rac1-regulated activation of Jun N-terminal kinase/p38 kinases and GADD153
    • Brenner, B., U. Koppenhoefer, C. Weinstock, O. Linderkamp, F. Lang, and E. Gulbins. 1997. Fas-or ceramide-induced apoptosis is mediated by a Rac1-regulated activation of Jun N-terminal kinase/p38 kinases and GADD153. J. Biol. Chem. 272:22173.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22173
    • Brenner, B.1    Koppenhoefer, U.2    Weinstock, C.3    Linderkamp, O.4    Lang, F.5    Gulbins, E.6
  • 20
    • 0031044561 scopus 로고    scopus 로고
    • MEKKs, GCKs, MLKs, PAKs, TAKs, and Tp1s: Upstream regulators of the c-Jun amino-terminal kinases?
    • Fanger, G. R., P. Gerwins, C. Widmann, M. B. Jarpe, and G. L. Johnson. 1997. MEKKs, GCKs, MLKs, PAKs, TAKs, and Tp1s: upstream regulators of the c-Jun amino-terminal kinases? Curr. Opin. Genet. Dev. 7:67.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 67
    • Fanger, G.R.1    Gerwins, P.2    Widmann, C.3    Jarpe, M.B.4    Johnson, G.L.5
  • 21
    • 0029861909 scopus 로고    scopus 로고
    • Regulation of interleukin-2 transcription by inducible stable expression of dominant negative and dominant active mitogen-activated protein kinase kinase kinase in Jurkat T cells: Evidence for the importance of Ras in a pathway that is controlled by dual receptor stimulation
    • Faris, M., N. Kokot, L. Lee, and A. E. Nel. 1996. Regulation of interleukin-2 transcription by inducible stable expression of dominant negative and dominant active mitogen-activated protein kinase kinase kinase in Jurkat T cells: evidence for the importance of Ras in a pathway that is controlled by dual receptor stimulation. J. Biol. Chem. 271:27366.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27366
    • Faris, M.1    Kokot, N.2    Lee, L.3    Nel, A.E.4
  • 23
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and A. Hall. 1992. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389.
    • (1992) Cell , vol.70 , pp. 389
    • Ridley, A.J.1    Hall, A.2
  • 24
    • 0031929654 scopus 로고    scopus 로고
    • Stimulation of CD28 with B7-2 promotes focal adhesion-like cell contacts where Rho family small G proteins accumulates in T cells
    • Kaga, S., S. Ragg, K. A. Rogers, and A. Ochi. 1998. Stimulation of CD28 with B7-2 promotes focal adhesion-like cell contacts where Rho family small G proteins accumulates in T cells. J. Immunol. 160:24.
    • (1998) J. Immunol. , vol.160 , pp. 24
    • Kaga, S.1    Ragg, S.2    Rogers, K.A.3    Ochi, A.4
  • 25
    • 0028985079 scopus 로고
    • MAP kinase pathways in yeast: For mating and more
    • Herskowitz, I. 1995. MAP kinase pathways in yeast: for mating and more. Cell 80:187.
    • (1995) Cell , vol.80 , pp. 187
    • Herskowitz, I.1
  • 26
    • 0029942952 scopus 로고    scopus 로고
    • Cloning of rat MEK kinase 1 cDNA reveals an endogenous membrane-associated 195-kDa protein with a large regulatory domain
    • Xu, S., D. J. Robbins, L. B. Christerson, J. M. English, C. A Vanderbilt, and M. H. Cobb. 1996. Cloning of rat MEK kinase 1 cDNA reveals an endogenous membrane-associated 195-kDa protein with a large regulatory domain. Proc. Natl. Acad. Sci. USA 93:5291.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5291
    • Xu, S.1    Robbins, D.J.2    Christerson, L.B.3    English, J.M.4    Vanderbilt, C.A.5    Cobb, M.H.6
  • 27
    • 0027994349 scopus 로고
    • The sphingomyelin cycle and the second messenger function of ceramide
    • Hannun, Y. A. 1994. The sphingomyelin cycle and the second messenger function of ceramide. J. Biol. Chem. 269:3125.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3125
    • Hannun, Y.A.1
  • 28
    • 0028897113 scopus 로고
    • Transcriptional regulation by extracellular signals: Mechanisms and specificity
    • Hill, C. S., and R. Treisman. 1995. Transcriptional regulation by extracellular signals: mechanisms and specificity. Cell 80:199.
    • (1995) Cell , vol.80 , pp. 199
    • Hill, C.S.1    Treisman, R.2
  • 29
    • 0028915743 scopus 로고
    • GTPase cascades choreographing cellular behavior: Movement, morphogenesis, and more
    • Chant, J., and L. Stower. 1995. GTPase cascades choreographing cellular behavior: movement, morphogenesis, and more. Cell 81:1.
    • (1995) Cell , vol.81 , pp. 1
    • Chant, J.1    Stower, L.2
  • 30
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., and A. Hall. 1995. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81:53.
    • (1995) Cell , vol.81 , pp. 53
    • Nobes, C.D.1    Hall, A.2
  • 31
    • 0026654125 scopus 로고
    • The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., H. F. Paterson, C. L. Johnston, D. Diekman, and A. Hall. 1992. The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling. Cell 70:401.
    • (1992) Cell , vol.70 , pp. 401
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekman, D.4    Hall, A.5
  • 36
    • 0030910706 scopus 로고    scopus 로고
    • Identification of two essential phosphorylated threonine residues in the catalytic domain of Mekk1: Indirect activation by Pak3 and protein kinase C
    • Siow, Y. L., G. B. Kalmar, J. S. Sanghera, G. Tai, S. S. Oh, and S. L. Pelech. 1997. Identification of two essential phosphorylated threonine residues in the catalytic domain of Mekk1: indirect activation by Pak3 and protein kinase C. J. Biol. Chem. 272:7586.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7586
    • Siow, Y.L.1    Kalmar, G.B.2    Sanghera, J.S.3    Tai, G.4    Oh, S.S.5    Pelech, S.L.6
  • 37
    • 0030875602 scopus 로고    scopus 로고
    • MEK kinases are regulated by EGF and selectively interact with Rac/Cdc42
    • Fanger, G. R., N. L. Johnson, and G. L. Johnson. 1997. MEK kinases are regulated by EGF and selectively interact with Rac/Cdc42. EMBO J. 16:4961.
    • (1997) EMBO J. , vol.16 , pp. 4961
    • Fanger, G.R.1    Johnson, N.L.2    Johnson, G.L.3
  • 38
    • 0030755579 scopus 로고    scopus 로고
    • The regulation of anoikis: MEKK-1 activation requires cleavage by caspases
    • Cardone, M. H., G. S. Salvesen, C. Widmann, G. Johnson, and S. M. Frisch. 1997. The regulation of anoikis: MEKK-1 activation requires cleavage by caspases. Cell 90:315.
    • (1997) Cell , vol.90 , pp. 315
    • Cardone, M.H.1    Salvesen, G.S.2    Widmann, C.3    Johnson, G.4    Frisch, S.M.5
  • 39
    • 0028855405 scopus 로고
    • Ceramide: An intracellular signal for apoptosis
    • Hannun, Y. A., and L. M. Obeid. 1995. Ceramide: an intracellular signal for apoptosis. Trends Biochem. Sci. 20:73.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 73
    • Hannun, Y.A.1    Obeid, L.M.2
  • 40
    • 0029000942 scopus 로고
    • Ceramide: A signal for apoptosis or mitogenesis?
    • Kolesnick, R., and Z. Fuks. 1995. Ceramide: a signal for apoptosis or mitogenesis? J. Exp. Med. 181:1949.
    • (1995) J. Exp. Med. , vol.181 , pp. 1949
    • Kolesnick, R.1    Fuks, Z.2
  • 41
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia, Z., M. Dickens, J. Raingeaud, R. J. Davis, and M. E. Greenberg. 1995. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 270: 1326.
    • (1995) Science , vol.270 , pp. 1326
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 42
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signalling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall, C. J. 1995. Specificity of receptor tyrosine kinase signalling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179.
    • (1995) Cell , vol.80 , pp. 179
    • Marshall, C.J.1
  • 44
    • 0027442667 scopus 로고
    • Biologically active lipids are regulators of Rac · GDI complexation
    • Chuang, T.-H., B. P. Bohl, and G. M. Bokoch. 1993. Biologically active lipids are regulators of Rac · GDI complexation. J. Biol. Chem. 268:26206.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26206
    • Chuang, T.-H.1    Bohl, B.P.2    Bokoch, G.M.3


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