메뉴 건너뛰기




Volumn 55, Issue 6, 2007, Pages 537-544

Protein kinase C theta (PKCθ): A key player in T cell life and death

Author keywords

CD28; PKC ; Signal transduction; T cell; TCR

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN KINASE C THETA; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR NFAT;

EID: 34250692040     PISSN: 10436618     EISSN: 10961186     Source Type: Journal    
DOI: 10.1016/j.phrs.2007.04.009     Document Type: Review
Times cited : (167)

References (85)
  • 1
    • 0027418818 scopus 로고
    • Molecular cloning and characterization of PKCθ, a human novel member of the protein kinase C (PKC) gene family expressed predominantly in hematopoietic cells
    • Baier G., Telford D., Giampa L., et al. Molecular cloning and characterization of PKCθ, a human novel member of the protein kinase C (PKC) gene family expressed predominantly in hematopoietic cells. J Biol Chem 268 (1993) 4997-5004
    • (1993) J Biol Chem , vol.268 , pp. 4997-5004
    • Baier, G.1    Telford, D.2    Giampa, L.3
  • 2
    • 0027153592 scopus 로고
    • Molecular cloning and expression of a cDNA encoding a novel isoenzyme of protein kinase C (nPKC). A new member of the nPKC family expressed in skeletal muscle, megakaryoblastic cells, and platelets
    • Chang J.D., Xu Y., Raychowdhury M.K., et al. Molecular cloning and expression of a cDNA encoding a novel isoenzyme of protein kinase C (nPKC). A new member of the nPKC family expressed in skeletal muscle, megakaryoblastic cells, and platelets. J Biol Chem 268 (1993) 14208-14214
    • (1993) J Biol Chem , vol.268 , pp. 14208-14214
    • Chang, J.D.1    Xu, Y.2    Raychowdhury, M.K.3
  • 3
    • 0026665459 scopus 로고
    • A new member of the protein kinase C family, nPKCθ, predominantly expressed in skeletal muscle
    • Osada S., Mizuno K., Saido T.C., et al. A new member of the protein kinase C family, nPKCθ, predominantly expressed in skeletal muscle. Mol Cell Biol 12 (1992) 3930-3938
    • (1992) Mol Cell Biol , vol.12 , pp. 3930-3938
    • Osada, S.1    Mizuno, K.2    Saido, T.C.3
  • 4
    • 0037902559 scopus 로고    scopus 로고
    • Protein kinase C-θ (PKCθ): it's all about location, location, location
    • Altman A., and Villalba M. Protein kinase C-θ (PKCθ): it's all about location, location, location. Immunol Rev 192 (2003) 53-63
    • (2003) Immunol Rev , vol.192 , pp. 53-63
    • Altman, A.1    Villalba, M.2
  • 5
    • 0036604936 scopus 로고    scopus 로고
    • Protein kinase C-θ: signaling from the center of the T-cell synapse
    • Arendt C.W., Albrecht B., Soos T.J., et al. Protein kinase C-θ: signaling from the center of the T-cell synapse. Curr Opin Immunol 14 (2002) 323-330
    • (2002) Curr Opin Immunol , vol.14 , pp. 323-330
    • Arendt, C.W.1    Albrecht, B.2    Soos, T.J.3
  • 6
    • 85047682875 scopus 로고    scopus 로고
    • Protein kinase C-θ in T cell activation
    • Isakov N., and Altman A. Protein kinase C-θ in T cell activation. Annu Rev Immunol 20 (2002) 761-794
    • (2002) Annu Rev Immunol , vol.20 , pp. 761-794
    • Isakov, N.1    Altman, A.2
  • 7
    • 0034602963 scopus 로고    scopus 로고
    • Regulation of protein kinase Cθ function during T cell activation by Lck-mediated tyrosine phosphorylation
    • Liu Y., Witte S., Liu Y.C., et al. Regulation of protein kinase Cθ function during T cell activation by Lck-mediated tyrosine phosphorylation. J Biol Chem 275 (2000) 3603-3609
    • (2000) J Biol Chem , vol.275 , pp. 3603-3609
    • Liu, Y.1    Witte, S.2    Liu, Y.C.3
  • 8
    • 4444245423 scopus 로고    scopus 로고
    • Protein kinase C and beyond
    • Spitaler M., and Cantrell D.A. Protein kinase C and beyond. Nat Immunol 5 (2004) 785-790
    • (2004) Nat Immunol , vol.5 , pp. 785-790
    • Spitaler, M.1    Cantrell, D.A.2
  • 9
    • 0031012266 scopus 로고    scopus 로고
    • Selective modulation of protein kinase C-θ during T-cell activation
    • Monks C.R.F., Kupfer H., Tamir I., et al. Selective modulation of protein kinase C-θ during T-cell activation. Nature 385 (1997) 83-86
    • (1997) Nature , vol.385 , pp. 83-86
    • Monks, C.R.F.1    Kupfer, H.2    Tamir, I.3
  • 10
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: a molecular machine controlling T cell activation
    • Grakoui A., Bromley S.K., Sumen C., et al. The immunological synapse: a molecular machine controlling T cell activation. Science 285 (1999) 221-227
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1    Bromley, S.K.2    Sumen, C.3
  • 11
    • 0034644505 scopus 로고    scopus 로고
    • Signaling takes shape in the immune system
    • Dustin M.L., and Chan A.C. Signaling takes shape in the immune system. Cell 103 (2000) 283-294
    • (2000) Cell , vol.103 , pp. 283-294
    • Dustin, M.L.1    Chan, A.C.2
  • 12
    • 0034232037 scopus 로고    scopus 로고
    • The immunological synapse and the actin cytoskeleton: molecular hardware for T cell signaling
    • Dustin M.L., and Cooper J.A. The immunological synapse and the actin cytoskeleton: molecular hardware for T cell signaling. Nat Immunol 1 (2000) 23-29
    • (2000) Nat Immunol , vol.1 , pp. 23-29
    • Dustin, M.L.1    Cooper, J.A.2
  • 13
    • 0033534525 scopus 로고    scopus 로고
    • The actin cytoskeleton and lymphocyte activation
    • Penninger J.M., and Crabtree G.R. The actin cytoskeleton and lymphocyte activation. Cell 96 (1999) 9-12
    • (1999) Cell , vol.96 , pp. 9-12
    • Penninger, J.M.1    Crabtree, G.R.2
  • 14
    • 0032545218 scopus 로고    scopus 로고
    • A receptor/cytoskeletal movement triggered by costimulation during T cell activation
    • Wülfing C., and Davis M.M. A receptor/cytoskeletal movement triggered by costimulation during T cell activation. Science 282 (1998) 2266-2269
    • (1998) Science , vol.282 , pp. 2266-2269
    • Wülfing, C.1    Davis, M.M.2
  • 15
    • 0035037684 scopus 로고    scopus 로고
    • Lipid microdomains and the role of PKCθ in T cell activation
    • Bi K., and Altman A. Lipid microdomains and the role of PKCθ in T cell activation. Semin Immunol 13 (2001) 139-146
    • (2001) Semin Immunol , vol.13 , pp. 139-146
    • Bi, K.1    Altman, A.2
  • 16
    • 0035039037 scopus 로고    scopus 로고
    • Co-stimulation and counter-stimulation: lipid raft clustering controls TCR signaling and functional outcomes
    • Miceli M.C., Moran M., Chung C.D., et al. Co-stimulation and counter-stimulation: lipid raft clustering controls TCR signaling and functional outcomes. Semin Immunol 13 (2001) 115-128
    • (2001) Semin Immunol , vol.13 , pp. 115-128
    • Miceli, M.C.1    Moran, M.2    Chung, C.D.3
  • 17
    • 0032986671 scopus 로고    scopus 로고
    • Membrane compartmentation and the response to antigen
    • Xavier R., and Seed B. Membrane compartmentation and the response to antigen. Curr Opin Immunol 11 (1999) 265-269
    • (1999) Curr Opin Immunol , vol.11 , pp. 265-269
    • Xavier, R.1    Seed, B.2
  • 18
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular clusters in T cells
    • Monks C.R., Freiberg B.A., Kupfer H., et al. Three-dimensional segregation of supramolecular clusters in T cells. Nature 395 (1998) 82-86
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3
  • 19
    • 27844473354 scopus 로고    scopus 로고
    • A dynamic view of the immunological synapse
    • Dustin M.L. A dynamic view of the immunological synapse. Semin Immunol 17 (2005) 400-410
    • (2005) Semin Immunol , vol.17 , pp. 400-410
    • Dustin, M.L.1
  • 20
    • 0035374476 scopus 로고    scopus 로고
    • Antigen-induced translocation of PKC-θ to membrane rafts is required for T cell activation
    • Bi K., Tanaka Y., Coudronniere N., et al. Antigen-induced translocation of PKC-θ to membrane rafts is required for T cell activation. Nat Immunol 2 (2001) 556-563
    • (2001) Nat Immunol , vol.2 , pp. 556-563
    • Bi, K.1    Tanaka, Y.2    Coudronniere, N.3
  • 21
    • 0037105477 scopus 로고    scopus 로고
    • Cutting edge: quantitative imaging of raft accumulation in the immunological synapse
    • Burack W.R., Lee K.H., Holdorf A.D., et al. Cutting edge: quantitative imaging of raft accumulation in the immunological synapse. J Immunol 15 169 (2002) 2837-2841
    • (2002) J Immunol , vol.15 , Issue.169 , pp. 2837-2841
    • Burack, W.R.1    Lee, K.H.2    Holdorf, A.D.3
  • 22
    • 0037047136 scopus 로고    scopus 로고
    • CD28 plays a critical role in the segregation of PKCθ within the immunologic synapse
    • Huang J., Lo P.F., Zal T., et al. CD28 plays a critical role in the segregation of PKCθ within the immunologic synapse. Proc Natl Acad Sci USA 99 (2002) 9369-9373
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9369-9373
    • Huang, J.1    Lo, P.F.2    Zal, T.3
  • 23
    • 0032931973 scopus 로고    scopus 로고
    • Costimulatory regulation of T cell function
    • Chambers C.A., and Allison J.P. Costimulatory regulation of T cell function. Curr Opin Cell Biol 11 (1999) 203-210
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 203-210
    • Chambers, C.A.1    Allison, J.P.2
  • 24
    • 0030833571 scopus 로고    scopus 로고
    • T cell clonal anergy
    • Schwartz R.H. T cell clonal anergy. Curr Opin Immunol 9 (1997) 351-357
    • (1997) Curr Opin Immunol , vol.9 , pp. 351-357
    • Schwartz, R.H.1
  • 25
    • 18844473151 scopus 로고    scopus 로고
    • PKC-θ is required for TCR-induced NF-κB activation in mature but not immature T lymphocytes
    • Sun Z., Arendt C.W., Ellmeier W., et al. PKC-θ is required for TCR-induced NF-κB activation in mature but not immature T lymphocytes. Nature 404 (2000) 402-407
    • (2000) Nature , vol.404 , pp. 402-407
    • Sun, Z.1    Arendt, C.W.2    Ellmeier, W.3
  • 26
    • 0031204429 scopus 로고    scopus 로고
    • Involvement of Rel, Fos, and Jun proteins in binding activity to the IL-2 promoter CD28 response element/AP-1 sequence in human T cells
    • McGuire K.L., and Iacobelli M. Involvement of Rel, Fos, and Jun proteins in binding activity to the IL-2 promoter CD28 response element/AP-1 sequence in human T cells. J Immunol 159 (1997) 1319-1327
    • (1997) J Immunol , vol.159 , pp. 1319-1327
    • McGuire, K.L.1    Iacobelli, M.2
  • 27
    • 28944445460 scopus 로고    scopus 로고
    • Differential roles of PKC-θ in the regulation of intracellular calcium concentration in primary T cells
    • Manicassamy S., Sadim M., Ye R.D., et al. Differential roles of PKC-θ in the regulation of intracellular calcium concentration in primary T cells. J Mol Biol 355 (2006) 347-359
    • (2006) J Mol Biol , vol.355 , pp. 347-359
    • Manicassamy, S.1    Sadim, M.2    Ye, R.D.3
  • 28
    • 0038620475 scopus 로고    scopus 로고
    • 2+ mobilization and NFAT cell activation in primary mouse T cells
    • 2+ mobilization and NFAT cell activation in primary mouse T cells. J Exp Med 197 (2003) 1525-1535
    • (2003) J Exp Med , vol.197 , pp. 1525-1535
    • Pfeifhofer, C.1    Kofler, K.2    Gruber, T.3
  • 29
    • 8444225946 scopus 로고    scopus 로고
    • The roles of CARMA1, Bcl10, and MALT1 in antigen receptor signaling
    • Lin X., and Wang D. The roles of CARMA1, Bcl10, and MALT1 in antigen receptor signaling. Semin Immunol 16 (2004) 429-435
    • (2004) Semin Immunol , vol.16 , pp. 429-435
    • Lin, X.1    Wang, D.2
  • 30
    • 2342611054 scopus 로고    scopus 로고
    • T-cell-receptor- and B-cell-receptor-mediated activation of NF-κB in lymphocytes
    • Weil R., and Israel A. T-cell-receptor- and B-cell-receptor-mediated activation of NF-κB in lymphocytes. Curr Opin Immunol 16 (2004) 374-381
    • (2004) Curr Opin Immunol , vol.16 , pp. 374-381
    • Weil, R.1    Israel, A.2
  • 31
    • 8644283766 scopus 로고    scopus 로고
    • The molecular adapter Carma1 controls entry of IκB kinase into the central immune synapse
    • Hara H., Bakal C., Wada T., et al. The molecular adapter Carma1 controls entry of IκB kinase into the central immune synapse. J Exp Med 200 (2004) 1167-1177
    • (2004) J Exp Med , vol.200 , pp. 1167-1177
    • Hara, H.1    Bakal, C.2    Wada, T.3
  • 32
    • 0037827638 scopus 로고    scopus 로고
    • Identifying the MAGUK protein Carma-1 as a central regulator of humoral immune responses and atopy by genome-wide mouse mutagenesis
    • Jun J.E., Wilson L.E., Vinuesa C.G., et al. Identifying the MAGUK protein Carma-1 as a central regulator of humoral immune responses and atopy by genome-wide mouse mutagenesis. Immunity 18 (2003) 751-762
    • (2003) Immunity , vol.18 , pp. 751-762
    • Jun, J.E.1    Wilson, L.E.2    Vinuesa, C.G.3
  • 33
    • 0036707520 scopus 로고    scopus 로고
    • A requirement for CARMA1 in TCR-induced NF-κB activation
    • Wang D., You Y., Case S.M., et al. A requirement for CARMA1 in TCR-induced NF-κB activation. Nat Immunol 3 (2002) 830-835
    • (2002) Nat Immunol , vol.3 , pp. 830-835
    • Wang, D.1    You, Y.2    Case, S.M.3
  • 34
    • 28844500398 scopus 로고    scopus 로고
    • Phosphorylation of the CARMA1 linker controls NF-κB activation
    • Sommer K., Guo B., Pomerantz J.L., et al. Phosphorylation of the CARMA1 linker controls NF-κB activation. Immunity 23 (2005) 561-574
    • (2005) Immunity , vol.23 , pp. 561-574
    • Sommer, K.1    Guo, B.2    Pomerantz, J.L.3
  • 35
    • 28844499919 scopus 로고    scopus 로고
    • Phosphorylation of CARMA1 plays a critical role in T cell receptor-mediated NF-κB activation
    • Matsumoto R., Wang D., Blonska M., et al. Phosphorylation of CARMA1 plays a critical role in T cell receptor-mediated NF-κB activation. Immunity 23 (2005) 575-585
    • (2005) Immunity , vol.23 , pp. 575-585
    • Matsumoto, R.1    Wang, D.2    Blonska, M.3
  • 36
    • 2342629277 scopus 로고    scopus 로고
    • The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes
    • Sun L., Deng L., Ea C.K., et al. The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. Mol Cell 14 (2004) 289-301
    • (2004) Mol Cell , vol.14 , pp. 289-301
    • Sun, L.1    Deng, L.2    Ea, C.K.3
  • 37
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-κB puzzle
    • Ghosh S., and Karin M. Missing pieces in the NF-κB puzzle. Cell 109 Suppl (2002) S81-S96
    • (2002) Cell , vol.109 , Issue.SUPPL
    • Ghosh, S.1    Karin, M.2
  • 38
    • 12544250145 scopus 로고    scopus 로고
    • Role for protein kinase C-θ (PKCθ) in TCR/CD28-mediated signaling through the canonical but not the non-canonical pathway for NF-κB activation
    • Li Y., Sedwick C.E., Hu J., et al. Role for protein kinase C-θ (PKCθ) in TCR/CD28-mediated signaling through the canonical but not the non-canonical pathway for NF-κB activation. J Biol Chem 280 (2005) 1217-1223
    • (2005) J Biol Chem , vol.280 , pp. 1217-1223
    • Li, Y.1    Sedwick, C.E.2    Hu, J.3
  • 39
    • 0029670089 scopus 로고    scopus 로고
    • PKCθ isoenzyme selective stimulation of the transcription factor complex AP-1 in T lymphocytes
    • Baier-Bitterlich G., Überall F., Bauer B., et al. PKCθ isoenzyme selective stimulation of the transcription factor complex AP-1 in T lymphocytes. Mol Cell Biol 16 (1996) 1842-1850
    • (1996) Mol Cell Biol , vol.16 , pp. 1842-1850
    • Baier-Bitterlich, G.1    Überall, F.2    Bauer, B.3
  • 40
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • Shaulian E., and Karin M. AP-1 as a regulator of cell life and death. Nat Cell Biol 4 (2002) E131-E136
    • (2002) Nat Cell Biol , vol.4
    • Shaulian, E.1    Karin, M.2
  • 42
    • 1842524184 scopus 로고    scopus 로고
    • SPAK kinase is a substrate and target of PKCθ in T-cell receptor-induced AP-1 activation pathway
    • Li Y., Hu J., Vita R., et al. SPAK kinase is a substrate and target of PKCθ in T-cell receptor-induced AP-1 activation pathway. EMBO J 23 (2004) 1112-1122
    • (2004) EMBO J , vol.23 , pp. 1112-1122
    • Li, Y.1    Hu, J.2    Vita, R.3
  • 43
    • 3042645122 scopus 로고    scopus 로고
    • 2+ signaling by PKCθ in restimulated T cells via a Tec kinase-dependent pathway
    • 2+ signaling by PKCθ in restimulated T cells via a Tec kinase-dependent pathway. Eur J Immunol 34 (2004) 2001-2011
    • (2004) Eur J Immunol , vol.34 , pp. 2001-2011
    • Altman, A.1    Kaminski, S.2    Busuttil, V.3
  • 44
    • 33646560593 scopus 로고    scopus 로고
    • Diacylglycerol and protein kinase D localization during T lymphocyte activation
    • Spitaler M., Emslie E., Wood C.D., et al. Diacylglycerol and protein kinase D localization during T lymphocyte activation. Immunity 24 (2006) 535-546
    • (2006) Immunity , vol.24 , pp. 535-546
    • Spitaler, M.1    Emslie, E.2    Wood, C.D.3
  • 45
    • 0035474310 scopus 로고    scopus 로고
    • Adaptor proteins in protein kinase C-mediated signal transduction
    • Schechtman D., and Mochly-Rosen D. Adaptor proteins in protein kinase C-mediated signal transduction. Oncogene 20 (2001) 6339-6347
    • (2001) Oncogene , vol.20 , pp. 6339-6347
    • Schechtman, D.1    Mochly-Rosen, D.2
  • 46
    • 17444403210 scopus 로고    scopus 로고
    • The C2 domain of PKCδ is a phosphotyrosine binding domain
    • Benes C.H., Wu N., Elia A.E., et al. The C2 domain of PKCδ is a phosphotyrosine binding domain. Cell 121 (2005) 271-280
    • (2005) Cell , vol.121 , pp. 271-280
    • Benes, C.H.1    Wu, N.2    Elia, A.E.3
  • 47
    • 0034288906 scopus 로고    scopus 로고
    • A novel functional interaction between Vav and PKCθ is required for TCR-induced T cell activation
    • Villalba M., Coudronniere N., Deckert M., et al. A novel functional interaction between Vav and PKCθ is required for TCR-induced T cell activation. Immunity 12 (2000) 151-160
    • (2000) Immunity , vol.12 , pp. 151-160
    • Villalba, M.1    Coudronniere, N.2    Deckert, M.3
  • 48
    • 0037092038 scopus 로고    scopus 로고
    • Translocation of PKCθ in T cells is mediated by a nonconventional, PI3-K- and Vav-dependent pathway, but does not absolutely require phospholipase C
    • Villalba M., Bi K., Hu J., et al. Translocation of PKCθ in T cells is mediated by a nonconventional, PI3-K- and Vav-dependent pathway, but does not absolutely require phospholipase C. J Cell Biol 157 (2002) 253-263
    • (2002) J Cell Biol , vol.157 , pp. 253-263
    • Villalba, M.1    Bi, K.2    Hu, J.3
  • 49
    • 0034644523 scopus 로고    scopus 로고
    • Cellular signaling: pivoting around PDK-1
    • Toker A., and Newton A.C. Cellular signaling: pivoting around PDK-1. Cell 103 (2000) 185-188
    • (2000) Cell , vol.103 , pp. 185-188
    • Toker, A.1    Newton, A.C.2
  • 50
    • 15944410614 scopus 로고    scopus 로고
    • PDK1 nucleates T cell receptor-induced signaling complex for NF-κB activation
    • Lee K.Y., D'Acquisto F., Hayden M.S., et al. PDK1 nucleates T cell receptor-induced signaling complex for NF-κB activation. Science 308 (2005) 114-118
    • (2005) Science , vol.308 , pp. 114-118
    • Lee, K.Y.1    D'Acquisto, F.2    Hayden, M.S.3
  • 51
    • 33645733203 scopus 로고    scopus 로고
    • Comment on "PDK1 nucleates T cell receptor-induced signaling complex for NF-κB activation"
    • [author reply 55]
    • Gruber T., Freeley M., Thuille N., et al. Comment on "PDK1 nucleates T cell receptor-induced signaling complex for NF-κB activation". Science 312 (2006) 55 [author reply 55]
    • (2006) Science , vol.312 , pp. 55
    • Gruber, T.1    Freeley, M.2    Thuille, N.3
  • 52
    • 0031012892 scopus 로고    scopus 로고
    • Determination of the specific substrate sequence motifs of protein kinase C isozymes
    • Nishikawa K., Toker A., Johannes F.-J., et al. Determination of the specific substrate sequence motifs of protein kinase C isozymes. J Biol Chem 272 (1997) 952-960
    • (1997) J Biol Chem , vol.272 , pp. 952-960
    • Nishikawa, K.1    Toker, A.2    Johannes, F.-J.3
  • 53
    • 0032571406 scopus 로고    scopus 로고
    • Protein kinase C-θ phosphorylation of moesin in the actin-binding sequence
    • Pietromonaco S.F., Simons P.C., Altman A., et al. Protein kinase C-θ phosphorylation of moesin in the actin-binding sequence. J Biol Chem 273 (1998) 7594-7603
    • (1998) J Biol Chem , vol.273 , pp. 7594-7603
    • Pietromonaco, S.F.1    Simons, P.C.2    Altman, A.3
  • 54
    • 18244364886 scopus 로고    scopus 로고
    • ERM-dependent movement of CD43 defines a novel protein complex distal to the immunological synapse
    • Allenspach E.J., Cullinan P., Tong J., et al. ERM-dependent movement of CD43 defines a novel protein complex distal to the immunological synapse. Immunity 15 (2001) 739-750
    • (2001) Immunity , vol.15 , pp. 739-750
    • Allenspach, E.J.1    Cullinan, P.2    Tong, J.3
  • 55
    • 0035652354 scopus 로고    scopus 로고
    • Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin
    • Delon J., Kaibuchi K., and Germain R.N. Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin. Immunity 15 (2001) 691-701
    • (2001) Immunity , vol.15 , pp. 691-701
    • Delon, J.1    Kaibuchi, K.2    Germain, R.N.3
  • 56
    • 0027509048 scopus 로고
    • Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons
    • Yonemura S., Nagafuchi A., Sato N., et al. Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons. J Cell Biol 120 (1993) 437-449
    • (1993) J Cell Biol , vol.120 , pp. 437-449
    • Yonemura, S.1    Nagafuchi, A.2    Sato, N.3
  • 57
    • 0036928182 scopus 로고    scopus 로고
    • Mechanism of recruitment of WASP to the immunological synapse and of its activation following TCR ligation
    • Sasahara Y., Rachid R., Byrne M.J., et al. Mechanism of recruitment of WASP to the immunological synapse and of its activation following TCR ligation. Mol Cell 10 (2002) 1269-1281
    • (2002) Mol Cell , vol.10 , pp. 1269-1281
    • Sasahara, Y.1    Rachid, R.2    Byrne, M.J.3
  • 58
    • 0032118427 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein-deficient mice reveal a role for WASP in T but not B cell activation
    • Snapper S.B., Rosen F.S., Mizoguchi E., et al. Wiskott-Aldrich syndrome protein-deficient mice reveal a role for WASP in T but not B cell activation. Immunity 9 (1998) 81-91
    • (1998) Immunity , vol.9 , pp. 81-91
    • Snapper, S.B.1    Rosen, F.S.2    Mizoguchi, E.3
  • 59
    • 8544233570 scopus 로고    scopus 로고
    • Protein kinase C θ inhibits insulin signaling by phosphorylating IRS1 at Ser-1101
    • Li Y., Soos T.J., Li X., et al. Protein kinase C θ inhibits insulin signaling by phosphorylating IRS1 at Ser-1101. J Biol Chem 279 (2004) 45304-45307
    • (2004) J Biol Chem , vol.279 , pp. 45304-45307
    • Li, Y.1    Soos, T.J.2    Li, X.3
  • 60
    • 8544244084 scopus 로고    scopus 로고
    • PKC-θ knockout mice are protected from fat-induced insulin resistance
    • Kim J.K., Fillmore J.J., Sunshine M.J., et al. PKC-θ knockout mice are protected from fat-induced insulin resistance. J Clin Invest 114 (2004) 823-827
    • (2004) J Clin Invest , vol.114 , pp. 823-827
    • Kim, J.K.1    Fillmore, J.J.2    Sunshine, M.J.3
  • 61
    • 0037081849 scopus 로고    scopus 로고
    • Phosphorylation of the protein kinase C-θ activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-κB induction
    • Liu Y., Graham C., Li A., et al. Phosphorylation of the protein kinase C-θ activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-κB induction. Biochem J 361 Pt 2 (2002) 255-265
    • (2002) Biochem J , vol.361 , Issue.PART 2 , pp. 255-265
    • Liu, Y.1    Graham, C.2    Li, A.3
  • 62
    • 27844439874 scopus 로고    scopus 로고
    • Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCθ in T lymphocytes
    • Thuille N., Heit I., Fresser F., et al. Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCθ in T lymphocytes. EMBO J 24 (2005) 3869-3880
    • (2005) EMBO J , vol.24 , pp. 3869-3880
    • Thuille, N.1    Heit, I.2    Fresser, F.3
  • 63
    • 1642299050 scopus 로고    scopus 로고
    • PKCθ signals activation versus tolerance in vivo
    • Berg-Brown N.N., Gronski M.A., Jones R.G., et al. PKCθ signals activation versus tolerance in vivo. J Exp Med 199 (2004) 743-752
    • (2004) J Exp Med , vol.199 , pp. 743-752
    • Berg-Brown, N.N.1    Gronski, M.A.2    Jones, R.G.3
  • 65
    • 18744364178 scopus 로고    scopus 로고
    • Protein kinase C θ is not essential for T-cell-mediated clearance of murine gammaherpesvirus 68
    • Giannoni F., Lyon A.B., Wareing M.D., et al. Protein kinase C θ is not essential for T-cell-mediated clearance of murine gammaherpesvirus 68. J Virol 79 (2005) 6808-6813
    • (2005) J Virol , vol.79 , pp. 6808-6813
    • Giannoni, F.1    Lyon, A.B.2    Wareing, M.D.3
  • 66
    • 3242790172 scopus 로고    scopus 로고
    • Protein kinase C θ Is critical for the development of in vivo T helper Th2 cell but not Th1 cell responses
    • Marsland B.J., Soos T.J., Spath G., et al. Protein kinase C θ Is critical for the development of in vivo T helper Th2 cell but not Th1 cell responses. J Exp Med 200 (2004) 181-189
    • (2004) J Exp Med , vol.200 , pp. 181-189
    • Marsland, B.J.1    Soos, T.J.2    Spath, G.3
  • 67
    • 8444243253 scopus 로고    scopus 로고
    • Differential regulation of Th2 and Th1 lung inflammatory responses by PKCθ
    • Salek-Ardakani S., So T., Halteman B.S., et al. Differential regulation of Th2 and Th1 lung inflammatory responses by PKCθ. J Immunol 173 (2004) 6440-6447
    • (2004) J Immunol , vol.173 , pp. 6440-6447
    • Salek-Ardakani, S.1    So, T.2    Halteman, B.S.3
  • 68
    • 9644262463 scopus 로고    scopus 로고
    • Signaling pathways in Th2 development
    • Mowen K.A., and Glimcher L.H. Signaling pathways in Th2 development. Immunol Rev 202 (2004) 203-222
    • (2004) Immunol Rev , vol.202 , pp. 203-222
    • Mowen, K.A.1    Glimcher, L.H.2
  • 69
    • 33845589222 scopus 로고    scopus 로고
    • Involvement of GATA3 in protein kinase C θ-induced Th2 cytokine expression
    • Stevens L., Htut T.M., White D., et al. Involvement of GATA3 in protein kinase C θ-induced Th2 cytokine expression. Eur J Immunol 36 (2006) 3305-3314
    • (2006) Eur J Immunol , vol.36 , pp. 3305-3314
    • Stevens, L.1    Htut, T.M.2    White, D.3
  • 70
    • 28244464872 scopus 로고    scopus 로고
    • Protein kinase Cθ controls Th1 cells in experimental autoimmune encephalomyelitis
    • Salek-Ardakani S., So T., Halteman B.S., et al. Protein kinase Cθ controls Th1 cells in experimental autoimmune encephalomyelitis. J Immunol 175 (2005) 7635-7641
    • (2005) J Immunol , vol.175 , pp. 7635-7641
    • Salek-Ardakani, S.1    So, T.2    Halteman, B.S.3
  • 71
    • 33644512418 scopus 로고    scopus 로고
    • Resistance to experimental autoimmune encephalomyelitis and impaired IL-17 production in protein kinase C θ-deficient mice
    • Tan S.L., Zhao J., Bi C., et al. Resistance to experimental autoimmune encephalomyelitis and impaired IL-17 production in protein kinase C θ-deficient mice. J Immunol 176 (2006) 2872-2879
    • (2006) J Immunol , vol.176 , pp. 2872-2879
    • Tan, S.L.1    Zhao, J.2    Bi, C.3
  • 72
    • 33750036982 scopus 로고    scopus 로고
    • Mice deficient in PKC θ demonstrate impaired in vivo T cell activation and protection from T cell-mediated inflammatory diseases
    • Anderson K., Fitzgerald M., Dupont M., et al. Mice deficient in PKC θ demonstrate impaired in vivo T cell activation and protection from T cell-mediated inflammatory diseases. Autoimmunity 39 (2006) 469-478
    • (2006) Autoimmunity , vol.39 , pp. 469-478
    • Anderson, K.1    Fitzgerald, M.2    Dupont, M.3
  • 73
    • 33746210212 scopus 로고    scopus 로고
    • PKC-θ-deficient mice are protected from Th1-dependent antigen-induced arthritis
    • Healy A.M., Izmailova E., Fitzgerald M., et al. PKC-θ-deficient mice are protected from Th1-dependent antigen-induced arthritis. J Immunol 177 (2006) 1886-1893
    • (2006) J Immunol , vol.177 , pp. 1886-1893
    • Healy, A.M.1    Izmailova, E.2    Fitzgerald, M.3
  • 74
    • 33646164439 scopus 로고    scopus 로고
    • Expanding the effector CD4 T-cell repertoire: the Th17 lineage
    • Harrington L.E., Mangan P.R., and Weaver C.T. Expanding the effector CD4 T-cell repertoire: the Th17 lineage. Curr Opin Immunol 18 (2006) 349-356
    • (2006) Curr Opin Immunol , vol.18 , pp. 349-356
    • Harrington, L.E.1    Mangan, P.R.2    Weaver, C.T.3
  • 75
    • 33744984785 scopus 로고    scopus 로고
    • Th17: an effector CD4 T cell lineage with regulatory T cell ties
    • Weaver C.T., Harrington L.E., Mangan P.R., et al. Th17: an effector CD4 T cell lineage with regulatory T cell ties. Immunity 24 (2006) 677-688
    • (2006) Immunity , vol.24 , pp. 677-688
    • Weaver, C.T.1    Harrington, L.E.2    Mangan, P.R.3
  • 76
    • 33646577466 scopus 로고    scopus 로고
    • Reciprocal developmental pathways for the generation of pathogenic effector TH17 and regulatory T cells
    • Bettelli E., Carrier Y., Gao W., et al. Reciprocal developmental pathways for the generation of pathogenic effector TH17 and regulatory T cells. Nature 441 (2006) 235-238
    • (2006) Nature , vol.441 , pp. 235-238
    • Bettelli, E.1    Carrier, Y.2    Gao, W.3
  • 77
    • 9644295708 scopus 로고    scopus 로고
    • Issues in T-helper 1 development-resolved and unresolved
    • Berenson L.S., Ota N., and Murphy K.M. Issues in T-helper 1 development-resolved and unresolved. Immunol Rev 202 (2004) 157-174
    • (2004) Immunol Rev , vol.202 , pp. 157-174
    • Berenson, L.S.1    Ota, N.2    Murphy, K.M.3
  • 78
    • 1842480966 scopus 로고    scopus 로고
    • + regulatory and natural killer-like T cells on signals leading to NF-κB activation
    • + regulatory and natural killer-like T cells on signals leading to NF-κB activation. Proc Natl Acad Sci USA 101 (2004) 4566-4571
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4566-4571
    • Schmidt-Supprian, M.1    Tian, J.2    Grant, E.P.3
  • 80
    • 0034711239 scopus 로고    scopus 로고
    • PKC-θ and ε promote T cell survival by a Rsk-dependent phosphorylation and inactivation of BAD
    • Bertolotto C., Maulon L., Filippa N., et al. PKC-θ and ε promote T cell survival by a Rsk-dependent phosphorylation and inactivation of BAD. J Biol Chem 275 (2000) 37246-37250
    • (2000) J Biol Chem , vol.275 , pp. 37246-37250
    • Bertolotto, C.1    Maulon, L.2    Filippa, N.3
  • 81
    • 0035873711 scopus 로고    scopus 로고
    • PKCθ mediates a selective T cell survival signal via phosphorylation of BAD
    • Villalba M., Bushway P., and Altman A. PKCθ mediates a selective T cell survival signal via phosphorylation of BAD. J Immunol 166 (2001) 5955-5963
    • (2001) J Immunol , vol.166 , pp. 5955-5963
    • Villalba, M.1    Bushway, P.2    Altman, A.3
  • 82
    • 33846346546 scopus 로고    scopus 로고
    • Raf-1 and B-Raf promote protein kinase C theta interaction with BAD
    • Hindley A., and Kolch W. Raf-1 and B-Raf promote protein kinase C theta interaction with BAD. Cell Signal 19 (2006) 547-555
    • (2006) Cell Signal , vol.19 , pp. 547-555
    • Hindley, A.1    Kolch, W.2
  • 84
    • 0033010882 scopus 로고    scopus 로고
    • Bisindolylmaleimide VIII facilitates Fas-mediated apoptosis and inhibits T cell-mediated autoimmune diseases
    • Zhou T., Song L., Yang P., et al. Bisindolylmaleimide VIII facilitates Fas-mediated apoptosis and inhibits T cell-mediated autoimmune diseases. Nat Med 5 (1999) 42-48
    • (1999) Nat Med , vol.5 , pp. 42-48
    • Zhou, T.1    Song, L.2    Yang, P.3
  • 85
    • 0036285316 scopus 로고    scopus 로고
    • Protein kinase C-theta (PKC-theta), an example of a drug target for therapeutic intervention with human T cell leukemias
    • Villalba M., and Altman A. Protein kinase C-theta (PKC-theta), an example of a drug target for therapeutic intervention with human T cell leukemias. Curr Cancer Drug Targets 2 (2002) 125-134
    • (2002) Curr Cancer Drug Targets , vol.2 , pp. 125-134
    • Villalba, M.1    Altman, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.