메뉴 건너뛰기




Volumn 23, Issue 19, 2003, Pages 7068-7081

Protein kinase Cα (PKCα) acts upstream of PKCθ to activate IκB kinase and NF-κB in T lymphocytes

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CD28 ANTIGEN; CD3 ANTIGEN; I KAPPA B KINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; ISOENZYME; PROTEIN KINASE C; PROTEIN KINASE C ALPHA; PROTEIN KINASE C BETA1; PROTEIN KINASE C INHIBITOR; PROTEIN KINASE C THETA; RNA; ROTTLERIN; T LYMPHOCYTE RECEPTOR; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; ACETOPHENONE DERIVATIVE; BENZOPYRAN DERIVATIVE; CALCIUM; CHUK PROTEIN, HUMAN; ENZYME INHIBITOR; IKBKB PROTEIN, HUMAN; IKBKE PROTEIN, HUMAN; INTERLEUKIN 2; PRKCA PROTEIN, HUMAN; PRKCQ PROTEIN, HUMAN; PROTEIN SERINE THREONINE KINASE; ZINC FINGER PROTEIN;

EID: 0141669117     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.19.7068-7081.2003     Document Type: Article
Times cited : (114)

References (70)
  • 1
    • 0024759789 scopus 로고
    • A 65-kD subunit of active NF-κB is required for inhibition of NF-κB by IκB
    • Baeuerle, P. A., and D. Baltimore. 1989. A 65-kD subunit of active NF-κB is required for inhibition of NF-κB by IκB. Genes Dev. 3:1689-1698.
    • (1989) Genes Dev. , vol.3 , pp. 1689-1698
    • Baeuerle, P.A.1    Baltimore, D.2
  • 2
    • 0027418818 scopus 로고
    • Molecular cloning and characterization of PKCθ, a novel member of the protein kinase C (PKC) gene family expressed predominantly in hematopoietic cells
    • Baier, G., D. Telford, L. Giampa, K. M. Coggeshall, G. Baier-Bitterlich, N. Isakov, and A. Altman. 1993. Molecular cloning and characterization of PKCθ, a novel member of the protein kinase C (PKC) gene family expressed predominantly in hematopoietic cells. J. Biol. Chem. 268:4997-5004.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4997-5004
    • Baier, G.1    Telford, D.2    Giampa, L.3    Coggeshall, K.M.4    Baier-Bitterlich, G.5    Isakov, N.6    Altman, A.7
  • 4
    • 0026783210 scopus 로고
    • IκB interacts with the nuclear localization sequences of the subunits of NF-κB: A mechanism for cytoplasmic retention
    • Beg, A. A., S. M. Ruben, R. I. Scheinman, S. Haskill, C. A. Rosen, and A. S. Baldwin, Jr. 1992. IκB interacts with the nuclear localization sequences of the subunits of NF-κB: a mechanism for cytoplasmic retention. Genes Dev. 6:1899-1913.
    • (1992) Genes Dev. , vol.6 , pp. 1899-1913
    • Beg, A.A.1    Ruben, S.M.2    Scheinman, R.I.3    Haskill, S.4    Rosen, C.A.5    Baldwin A.S., Jr.6
  • 5
    • 0034780788 scopus 로고    scopus 로고
    • The analysis of costimulatory receptor signaling cascades in normal T lymphocytes using in vitro gene transfer and reporter gene analysis
    • Bell, M. P., C. J. Huntoon, D. Graham, and D. J. McKean. 2001. The analysis of costimulatory receptor signaling cascades in normal T lymphocytes using in vitro gene transfer and reporter gene analysis. Nat. Med. 7:1155-1158.
    • (2001) Nat. Med. , vol.7 , pp. 1155-1158
    • Bell, M.P.1    Huntoon, C.J.2    Graham, D.3    McKean, D.J.4
  • 6
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge, M. J. 1993. Inositol trisphosphate and calcium signalling. Nature 361:315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 9
    • 0028986075 scopus 로고
    • Control of IκB-α proteolysis by site-specific, signal-induced phosphorylation
    • Brown, K., S. Gerstberger, L. Carlson, G. Franzoso, and U. Siebenlist. 1995. Control of IκB-α proteolysis by site-specific, signal-induced phosphorylation. Science 267:1485-1488.
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 10
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • Brummelkamp, T. R., R. Bernards, and R. Agami. 2002. A system for stable expression of short interfering RNAs in mammalian cells. Science 296:550-553.
    • (2002) Science , vol.296 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 11
  • 12
    • 0028108027 scopus 로고
    • Threonine-497 is a critical site for permissive activation of protein kinase C α
    • Cazaubon, S., F. Bornancin, and P. J. Parker. 1994. Threonine-497 is a critical site for permissive activation of protein kinase C α. Biochem. J. 301:443-448.
    • (1994) Biochem. J. , vol.301 , pp. 443-448
    • Cazaubon, S.1    Bornancin, F.2    Parker, P.J.3
  • 13
    • 0027390139 scopus 로고
    • Molecular basis for developmental changes in interleukin-2 gene inducibility
    • Chen, D., and E. V. Rothenberg. 1993. Molecular basis for developmental changes in interleukin-2 gene inducibility. Mol. Cell. Biol. 13:228-237.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 228-237
    • Chen, D.1    Rothenberg, E.V.2
  • 14
    • 0028831997 scopus 로고
    • Calcium signaling
    • Clapham, D. E. 1995. Calcium signaling. Cell. 80:259-268.
    • (1995) Cell , vol.80 , pp. 259-268
    • Clapham, D.E.1
  • 15
    • 0038233011 scopus 로고    scopus 로고
    • Determination of the calcium-binding sites of the C2 domain of protein kinase C α that are critical for its translocation to the plasma membrane
    • Corbalan-Garcia, S., J. A. Rodriguez-Alfaro, and J. C. Gomez-Fernandez. 1999. Determination of the calcium-binding sites of the C2 domain of protein kinase C α that are critical for its translocation to the plasma membrane. Biochem. J. 337:513-521.
    • (1999) Biochem. J. , vol.337 , pp. 513-521
    • Corbalan-Garcia, S.1    Rodriguez-Alfaro, J.A.2    Gomez-Fernandez, J.C.3
  • 16
    • 0034724201 scopus 로고    scopus 로고
    • NF-κB activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-θ
    • Coudronniere, N., M. Villalba, N. Englund, and A. Altman. 2000. NF-κB activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-θ. Proc. Natl. Acad. Sci. USA 97:3394-3399.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3394-3399
    • Coudronniere, N.1    Villalba, M.2    Englund, N.3    Altman, A.4
  • 17
    • 0028342952 scopus 로고
    • Signal transmission between the plasma membrane and nucleus of T lymphocytes
    • Crabtree, G. R., and N. A. Clipstone. 1994. Signal transmission between the plasma membrane and nucleus of T lymphocytes. Annu. Rev. Biochem. 63:1045-1083.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 1045-1083
    • Crabtree, G.R.1    Clipstone, N.A.2
  • 18
    • 0029670083 scopus 로고    scopus 로고
    • Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation
    • DiDonato, J., F. Mercurio, C. Rosette, J. Wu-Li, H. Suyang, S. Ghosh, and M. Karin. 1996. Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation. Mol. Cell. Biol. 16:1295-1304.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1295-1304
    • DiDonato, J.1    Mercurio, F.2    Rosette, C.3    Wu-Li, J.4    Suyang, H.5    Ghosh, S.6    Karin, M.7
  • 19
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
    • DiDonato, J. A., M. Hayakawa, D. M. Rothwarf, E. Zandi, and M. Karin. 1997. A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature 388:548-554.
    • (1997) Nature , vol.388 , pp. 548-554
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 21
    • 0032580202 scopus 로고    scopus 로고
    • Calcium oscillations increase the efficiency and specificity of gene expression
    • Dolmetsch, R. E., K. Xu, and R. S. Lewis. 1998. Calcium oscillations increase the efficiency and specificity of gene expression. Nature 392:933-936.
    • (1998) Nature , vol.392 , pp. 933-936
    • Dolmetsch, R.E.1    Xu, K.2    Lewis, R.S.3
  • 24
    • 0032143922 scopus 로고    scopus 로고
    • The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation
    • Garcia-Paramio, P., Y. Cabrerizo, F. Bornancin, and P. J. Parker. 1998. The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation. Biochem. J. 333:631-636.
    • (1998) Biochem. J. , vol.333 , pp. 631-636
    • Garcia-Paramio, P.1    Cabrerizo, Y.2    Bornancin, F.3    Parker, P.J.4
  • 25
    • 0028911139 scopus 로고
    • Analysis of the role of protein kinase C-α, -ε, and -ζ in T cell activation
    • Genot, E. M., P. J. Parker, and D. A. Cantrell. 1995. Analysis of the role of protein kinase C-α, -ε, and -ζ in T cell activation. J. Biol. Chem. 270:9833-9839.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9833-9839
    • Genot, E.M.1    Parker, P.J.2    Cantrell, D.A.3
  • 26
    • 0032566435 scopus 로고    scopus 로고
    • IκB kinases serve as a target of CD28 signaling
    • Harhaj, E. W., and S. C. Sun. 1998. IκB kinases serve as a target of CD28 signaling. J. Biol. Chem. 273:25185-25190.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25185-25190
    • Harhaj, E.W.1    Sun, S.C.2
  • 27
    • 0024584166 scopus 로고
    • κB-specific DNA binding proteins: Role in the regulation of human interleukin-2 gene expression
    • Hoyos, B., D. W. Ballard, E. Bohnlein, M. Siekevitz, and W. C. Greene. 1989. κB-specific DNA binding proteins: role in the regulation of human interleukin-2 gene expression. Science 244:457-460.
    • (1989) Science , vol.244 , pp. 457-460
    • Hoyos, B.1    Ballard, D.W.2    Bohnlein, E.3    Siekevitz, M.4    Greene, W.C.5
  • 28
    • 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, J. B., and J. D. Stobo. 1985. 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. 161:446-456.
    • (1985) J. Exp. Med. , vol.161 , pp. 446-456
    • Imboden, J.B.1    Stobo, J.D.2
  • 29
    • 0026742603 scopus 로고
    • Accelerated proliferation and interleukin-2 production of thymocytes by stimulation of soluble anti-CD3 monoclonal antibody in transgenic mice carrying a rabbit protein kinase C α
    • Iwamoto, T., M. Hagiwara, H. Hidaka, T. Isomura, D. Kioussis, and I. Nakashima. 1992. Accelerated proliferation and interleukin-2 production of thymocytes by stimulation of soluble anti-CD3 monoclonal antibody in transgenic mice carrying a rabbit protein kinase C α. J. Biol. Chem. 267:18644-18648.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18644-18648
    • Iwamoto, T.1    Hagiwara, M.2    Hidaka, H.3    Isomura, T.4    Kioussis, D.5    Nakashima, I.6
  • 30
    • 0029041568 scopus 로고
    • Transcriptional regulation of the IL-2 gene
    • Jain, J., C. Loh, and A. Rao. 1995. Transcriptional regulation of the IL-2 gene. Curr. Opin. Immunol. 7:333-342.
    • (1995) Curr. Opin. Immunol. , vol.7 , pp. 333-342
    • Jain, J.1    Loh, C.2    Rao, A.3
  • 31
    • 0025915550 scopus 로고
    • Physiologic activation of T cells via the T cell receptor induces NF-κB
    • Jamieson, C., P. G. McCaffrey, A. Rao, and R. Sen. 1991. Physiologic activation of T cells via the T cell receptor induces NF-κB. J. Immunol. 147:416-420.
    • (1991) J. Immunol. , vol.147 , pp. 416-420
    • Jamieson, C.1    McCaffrey, P.G.2    Rao, A.3    Sen, R.4
  • 32
    • 0030589362 scopus 로고    scopus 로고
    • 2+ influx. Functional synergy between Raf and calcineurin
    • 2+ influx. Functional synergy between Raf and calcineurin. J. Immunol. 157:5277-5283.
    • (1996) J. Immunol. , vol.157 , pp. 5277-5283
    • Kanno, T.1    Siebenlist, U.2
  • 33
    • 0030611049 scopus 로고    scopus 로고
    • 2+ differentially regulates conventional protein kinase Cs' membrane interaction and activation
    • 2+ differentially regulates conventional protein kinase Cs' membrane interaction and activation. J. Biol. Chem. 272:25959-25967.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25959-25967
    • Keranen, L.M.1    Newton, A.C.2
  • 36
    • 0029000938 scopus 로고
    • RelA is a potent transcriptional activator of the CD28 response element within the interleukin 2 promoter
    • Lai, J.-H., G. Horvath, J. Subleski, J. Bruder, P. Ghosh, and T.-H. Tan. 1995. RelA is a potent transcriptional activator of the CD28 response element within the interleukin 2 promoter. Mol. Cell. Biol. 15:4260-4271.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4260-4271
    • Lai, J.-H.1    Horvath, G.2    Subleski, J.3    Bruder, J.4    Ghosh, P.5    Tan, T.-H.6
  • 39
    • 0033082990 scopus 로고    scopus 로고
    • The proto-oncogene Cot kinase participates in CD3/CD28 induction of NF-κB acting through the NF-κB-inducing kinase and IκB kinases
    • Lin, X., E. T. Cunningham, Jr., Y. Mu, R. Geleziunas, and W. C. Greene. 1999. The proto-oncogene Cot kinase participates in CD3/CD28 induction of NF-κB acting through the NF-κB-inducing kinase and IκB kinases. Immunity 10:271-280.
    • (1999) Immunity , vol.10 , pp. 271-280
    • Lin, X.1    Cunningham E.T., Jr.2    Mu, Y.3    Geleziunas, R.4    Greene, W.C.5
  • 40
    • 0034031401 scopus 로고    scopus 로고
    • Protein kinase C-θ participates in NF-κB activation induced by CD3-CD28 costimulation through selective activation of IκB kinase β
    • Lin, X., A. O'Mahony, Y. Mu, R. Geleziunas, and W. C. Greene. 2000. Protein kinase C-θ participates in NF-κB activation induced by CD3-CD28 costimulation through selective activation of IκB kinase β. Mol. Cell. Biol. 20:2933-2940.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2933-2940
    • Lin, X.1    O'Mahony, A.2    Mu, Y.3    Geleziunas, R.4    Greene, W.C.5
  • 41
    • 0034602963 scopus 로고    scopus 로고
    • Regulation of protein kinase Cθ function during T cell activation by Lck-mediated tyrosine phosphorylation
    • Liu, Y., S. Witte, Y. C. Liu, M. Doyle, C. Elly, and A. Altman. 2000. Regulation of protein kinase Cθ function during T cell activation by Lck-mediated tyrosine phosphorylation. J. Biol. Chem. 275:3603-3609.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3603-3609
    • Liu, Y.1    Witte, S.2    Liu, Y.C.3    Doyle, M.4    Elly, C.5    Altman, A.6
  • 42
    • 0344923789 scopus 로고    scopus 로고
    • Inhibition of protein kinase C α expression by antisense RNA in transfected Jurkat cells
    • Lopez-Lago, M. A., J. Freire-Moar, and P. Barja. 1999. Inhibition of protein kinase C α expression by antisense RNA in transfected Jurkat cells. Eur. J. Immunol. 29:466-476.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 466-476
    • Lopez-Lago, M.A.1    Freire-Moar, J.2    Barja, P.3
  • 44
    • 0032504259 scopus 로고    scopus 로고
    • 2+ ligands and membrane binding residues
    • 2+ ligands and membrane binding residues. J. Biol. Chem. 273:17544-17552.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17544-17552
    • Medkova, M.1    Cho, W.2
  • 45
    • 0027243576 scopus 로고
    • p105 and p98 precursor proteins play an active role in NF-κB-mediated signal transduction
    • Mercurio, F., J. A. DiDonato, C. Rosette, and M. Karin. 1993. p105 and p98 precursor proteins play an active role in NF-κB-mediated signal transduction. Genes Dev. 7:705-718.
    • (1993) Genes Dev. , vol.7 , pp. 705-718
    • Mercurio, F.1    DiDonato, J.A.2    Rosette, C.3    Karin, M.4
  • 47
    • 0028356989 scopus 로고
    • Characterization of the calcium-binding site that regulates association of protein kinase C with phospholipid bilayers
    • Mosior, M., and R. M. Epand. 1994. Characterization of the calcium-binding site that regulates association of protein kinase C with phospholipid bilayers. J. Biol. Chem. 269:13798-13805.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13798-13805
    • Mosior, M.1    Epand, R.M.2
  • 48
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton, A. C. 1995. Protein kinase C: structure, function, and regulation. J. Biol. Chem. 270:28495-28498.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 49
    • 0032555778 scopus 로고    scopus 로고
    • Protein kinase C: A paradigm for regulation of protein function by two membrane-targeting modules
    • Newton, A. C., and J. E. Johnson. 1998. Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules. Biochim. Biophys. Acta 1376:155-172.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 155-172
    • Newton, A.C.1    Johnson, J.E.2
  • 50
    • 0025975795 scopus 로고
    • DNA binding and IκB inhibition of the cloned p65 subunit of NF-κB, a rel-related polypeptide
    • Nolan, G. P., S. Ghosh, H. C. Liou, P. Tempst, and D. Baltimore. 1991. DNA binding and IκB inhibition of the cloned p65 subunit of NF-κB, a rel-related polypeptide. Cell 64:961-969.
    • (1991) Cell , vol.64 , pp. 961-969
    • Nolan, G.P.1    Ghosh, S.2    Liou, H.C.3    Tempst, P.4    Baltimore, D.5
  • 51
    • 0033553484 scopus 로고    scopus 로고
    • Phorbol ester-induced disruption of the CD4-Lck complex occurs within a detergent-resistant microdomain of the plasma membrane. Involvement of the translocation of activated protein kinase C isoforms
    • Parolini, I., S. Topa, M. Sorice, A. Pace, P. Ceddia, E. Montesoro, A. Pavan, M. P. Lisanti, C. Peschle, and M. Sargiacomo. 1999. Phorbol ester-induced disruption of the CD4-Lck complex occurs within a detergent-resistant microdomain of the plasma membrane. Involvement of the translocation of activated protein kinase C isoforms. J. Biol. Chem. 274:14176-14187.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14176-14187
    • Parolini, I.1    Topa, S.2    Sorice, M.3    Pace, A.4    Ceddia, P.5    Montesoro, E.6    Pavan, A.7    Lisanti, M.P.8    Peschle, C.9    Sargiacomo, M.10
  • 52
  • 53
    • 0037124307 scopus 로고    scopus 로고
    • Protein kinase C β controls nuclear factor κB activation in B cells through selective regulation of the IκB kinase α
    • Saijo, K., I. Mecklenbrauker, A. Santana, M. Leitger, C. Schmedt, and A. Tarakhovsky. 2002. Protein kinase C β controls nuclear factor κB activation in B cells through selective regulation of the IκB kinase α. J. Exp. Med. 195:1647-1652.
    • (2002) J. Exp. Med. , vol.195 , pp. 1647-1652
    • Saijo, K.1    Mecklenbrauker, I.2    Santana, A.3    Leitger, M.4    Schmedt, C.5    Tarakhovsky, A.6
  • 56
    • 0035851112 scopus 로고    scopus 로고
    • Rottlerin is a mitochondrial uncoupler that decreases cellular ATP levels and indirectly blocks protein kinase Cdelta tyrosine phosphorylation
    • Soltoff, S. P. 2001. Rottlerin is a mitochondrial uncoupler that decreases cellular ATP levels and indirectly blocks protein kinase Cdelta tyrosine phosphorylation. J. Biol. Chem. 276:37986-37992.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37986-37992
    • Soltoff, S.P.1
  • 59
    • 0032032140 scopus 로고    scopus 로고
    • Different protein kinase C isoenzymes regulate IL-2 receptor expression or IL-2 synthesis in human lymphocytes stimulated via the TCR
    • Szamel, M., A. Appel, R. Schwinzer, and K. Resch. 1998. Different protein kinase C isoenzymes regulate IL-2 receptor expression or IL-2 synthesis in human lymphocytes stimulated via the TCR. J. Immunol. 160:2207-2214.
    • (1998) J. Immunol. , vol.160 , pp. 2207-2214
    • Szamel, M.1    Appel, A.2    Schwinzer, R.3    Resch, K.4
  • 60
    • 0028986194 scopus 로고
    • IκBα regulates the persistent response in a biphasic activation of NF-κB
    • Thompson, J. E., R. J. Phillips, H. Erdjument-Bromage, P. Tempst, and S. Ghosh. 1995. IκBα regulates the persistent response in a biphasic activation of NF-κB. Cell 80:573-582.
    • (1995) Cell , vol.80 , pp. 573-582
    • Thompson, J.E.1    Phillips, R.J.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 62
    • 0028978032 scopus 로고
    • Phosphorylation of human IκBα on serines 32 and 36 controls IκB-α proteolysis and NF-κB activation in response to diverse stimuli
    • Traenckner, E. B., H. L. Pahl, T. Henkel, K. N. Schmidt, S. Wilk, and P. A. Baeuerle. 1995. Phosphorylation of human IκBα on serines 32 and 36 controls IκB-α proteolysis and NF-κB activation in response to diverse stimuli. EMBO J. 14:2876-2883.
    • (1995) EMBO J. , vol.14 , pp. 2876-2883
    • Traenckner, E.B.1    Pahl, H.L.2    Henkel, T.3    Schmidt, K.N.4    Wilk, S.5    Baeuerle, P.A.6
  • 63
    • 0033551804 scopus 로고    scopus 로고
    • Protein kinase C and calcineurin synergize to activate IκaB kinase and NF-κB in T lymphocytes
    • Trushin, S. A., K. N. Pennington, A. Algeciras-Schimnich, and C. V. Paya. 1999. Protein kinase C and calcineurin synergize to activate IκaB kinase and NF-κB in T lymphocytes. J. Biol. Chem. 274:22923-22931.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22923-22931
    • Trushin, S.A.1    Pennington, K.N.2    Algeciras-Schimnich, A.3    Paya, C.V.4
  • 64
    • 0023792779 scopus 로고
    • Protein kinase C is required for responses to T cell receptor ligands but not to interleukin-2 in T cells
    • Valge, V. E., J. G. Wong, B. M. Datlof, A. J. Sinskey, and A. Rao. 1988. Protein kinase C is required for responses to T cell receptor ligands but not to interleukin-2 in T cells. Cell 55:101-112.
    • (1988) Cell , vol.55 , pp. 101-112
    • Valge, V.E.1    Wong, J.G.2    Datlof, B.M.3    Sinskey, A.J.4    Rao, A.5
  • 66
    • 0033248120 scopus 로고    scopus 로고
    • Protein kinase CO cooperates with calcineurin to induce Fas ligand expression during activation-induced T cell death
    • Villalba, M., S. Kasibhatla, L. Genestier, A. Mahboubi, D. R. Green, and A. Altman. 1999. Protein kinase CO cooperates with calcineurin to induce Fas ligand expression during activation-induced T cell death, J. Immunol. 163:5813-5819.
    • (1999) J. Immunol. , vol.163 , pp. 5813-5819
    • Villalba, M.1    Kasibhatla, S.2    Genestier, L.3    Mahboubi, A.4    Green, D.R.5    Altman, A.6
  • 67
    • 0032101707 scopus 로고    scopus 로고
    • Calcineurin preferentially synergizes with PKC-θ to activate JNK and IL-2 promoter in T lymphocytes
    • Werlen, G., E. Jacinto, Y. Xia, and M. Karin. 1998. Calcineurin preferentially synergizes with PKC-θ to activate JNK and IL-2 promoter in T lymphocytes. EMBO J. 17:3101-3111.
    • (1998) EMBO J. , vol.17 , pp. 3101-3111
    • Werlen, G.1    Jacinto, E.2    Xia, Y.3    Karin, M.4
  • 68
    • 0029122799 scopus 로고
    • N- and C-terminal sequences control degradation of MAD3/IκBα in response to inducers of NF-κB activity
    • Whiteside, S. T., M. K. Ernst, O. LeBail, C. Laurent-Winter, N. Rice, and A. Israël. 1995. N- and C-terminal sequences control degradation of MAD3/IκBα in response to inducers of NF-κB activity. Mol. Cell. Biol. 15:5339-5345.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5339-5345
    • Whiteside, S.T.1    Ernst, M.K.2    LeBail, O.3    Laurent-Winter, C.4    Rice, N.5    Israël, A.6
  • 69
    • 0030611595 scopus 로고    scopus 로고
    • IκB kinase-β: NF-κB activation and complex formation with IκB kinase-α and NIK
    • Woronicz, J. D., X. Gao, Z. Cao, M. Rothe, and D. V. Goeddel. 1997. IκB kinase-β: NF-κB activation and complex formation with IκB kinase-α and NIK. Science 278:866-869.
    • (1997) Science , vol.278 , pp. 866-869
    • Woronicz, J.D.1    Gao, X.2    Cao, Z.3    Rothe, M.4    Goeddel, D.V.5
  • 70
    • 0030613551 scopus 로고    scopus 로고
    • The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκB phosphorylation and NF-κB activation
    • Zandi, E., D. M. Rothwarf, M. Delhase, M. Hayakawa, and M. Karin. 1997. The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκB phosphorylation and NF-κB activation. Cell 91:243-252.
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.