메뉴 건너뛰기




Volumn 24, Issue 22, 2005, Pages 3869-3880

Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCθ in T lymphocytes

Author keywords

Autophosphorylation; Cellular function; IL 2 activation; PKC ; T cells

Indexed keywords

CD3 ANTIGEN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 2; LYMPHOCYTE ANTIGEN RECEPTOR; PHORBOL ESTER; PROTEIN KINASE B; PROTEIN KINASE C THETA; THREONINE; TRANSCRIPTION FACTOR NFAT; VANADIC ACID;

EID: 27844439874     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600856     Document Type: Article
Times cited : (47)

References (28)
  • 1
    • 0038701681 scopus 로고    scopus 로고
    • The PKC gene module: Molecular biosystematics to resolve its T cell functions
    • Baier G (2003) The PKC gene module: molecular biosystematics to resolve its T cell functions. Immunol Rev 192: 64-79
    • (2003) Immunol Rev , vol.192 , pp. 64-79
    • Baier, G.1
  • 3
    • 0036278214 scopus 로고    scopus 로고
    • + T-lymphocytes: New partners in TCR/CD28 signal integration
    • + T-lymphocytes: new partners in TCR/CD28 signal integration. Mol Immunol 38: 1087-1099
    • (2002) Mol Immunol , vol.38 , pp. 1087-1099
    • Bauer, B.1    Baier, G.2
  • 4
    • 0037464468 scopus 로고    scopus 로고
    • AKT1/PKBα is recruited to lipid rafts and activated downstream of PKC isotypes in CD3-induced T cell signaling
    • Bauer B, Jenny M, Fresser F, Uberall F, Baier G (2003) AKT1/PKBα is recruited to lipid rafts and activated downstream of PKC isotypes in CD3-induced T cell signaling. FEBS Lett 541: 155-162
    • (2003) FEBS Lett , vol.541 , pp. 155-162
    • Bauer, B.1    Jenny, M.2    Fresser, F.3    Uberall, F.4    Baier, G.5
  • 8
    • 0020529186 scopus 로고
    • Presence of specific binding sites for phorbol ester tumor promoters in human epidermal and dermal cells in culture but lack of down regulation in epidermal cells
    • Chida K, Kuroki T (1983) Presence of specific binding sites for phorbol ester tumor promoters in human epidermal and dermal cells in culture but lack of down regulation in epidermal cells. Cancer Res 43: 3638-3642
    • (1983) Cancer Res , vol.43 , pp. 3638-3642
    • Chida, K.1    Kuroki, T.2
  • 9
    • 0032585532 scopus 로고    scopus 로고
    • Regulation of conventional PKC isozymes by PDK-1
    • Dutil EM, Toker A, Newton AC (1998) Regulation of conventional PKC isozymes by PDK-1. Curr Biol 8: 1366-1375
    • (1998) Curr Biol , vol.8 , pp. 1366-1375
    • Dutil, E.M.1    Toker, A.2    Newton, A.C.3
  • 10
    • 22144437706 scopus 로고    scopus 로고
    • Stimulus-induced phosphorylation of PKCθ at the Ser-695 hydrophobic-motif in human T lymphocytes
    • Freeley M, Volkov Y, Kelleher D, Long A (2005) Stimulus-induced phosphorylation of PKCθ at the Ser-695 hydrophobic-motif in human T lymphocytes. Biochem Biophys Res Commun 334: 619-630
    • (2005) Biochem Biophys Res Commun , vol.334 , pp. 619-630
    • Freeley, M.1    Volkov, Y.2    Kelleher, D.3    Long, A.4
  • 11
    • 4644357300 scopus 로고    scopus 로고
    • Kinase peptide specificity: Improved determination and relevance to protein phosphorylation
    • Fujii K, Zhu G, Liu Y, Hallam J, Chen L, Herrero J, Shaw S (2004) Kinase peptide specificity: improved determination and relevance to protein phosphorylation. Proc Natl Acad Sci USA 101: 13744-13749
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13744-13749
    • Fujii, K.1    Zhu, G.2    Liu, Y.3    Hallam, J.4    Chen, L.5    Herrero, J.6    Shaw, S.7
  • 13
    • 15944410614 scopus 로고    scopus 로고
    • PDK1 nucleates T cell receptor-induced signaling complex for NF-κB activation
    • Lee KY, D'Acquisto F, Hayden MS, Shim JH, Ghosh S (2005) PDK1 nucleates T cell receptor-induced signaling complex for NF-κB activation. Science 308: 114-118
    • (2005) Science , vol.308 , pp. 114-118
    • Lee, K.Y.1    D'Acquisto, F.2    Hayden, M.S.3    Shim, J.H.4    Ghosh, S.5
  • 14
    • 0037081849 scopus 로고    scopus 로고
    • Phosphorylation of the PKCθ activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo NF-κ induction
    • Liu Y, Graham C, Li A, Fisher RJ, Shaw S (2002) Phosphorylation of the PKCθ activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo NF-κ induction. Biochem J 361: 255-265
    • (2002) Biochem J , vol.361 , pp. 255-265
    • Liu, Y.1    Graham, C.2    Li, A.3    Fisher, R.J.4    Shaw, S.5
  • 15
    • 3242790172 scopus 로고    scopus 로고
    • PKCθ is critical for the development of in vivo T helper (Th)2 cell but not Th1 cell responses
    • Marsland BJ, Soos TJ, Spath G, Littman DR, Kopf M (2004) PKCθ is critical for the development of in vivo T helper (Th)2 cell but not Th1 cell responses. J Exp Med 200: 181-189
    • (2004) J Exp Med , vol.200 , pp. 181-189
    • Marsland, B.J.1    Soos, T.J.2    Spath, G.3    Littman, D.R.4    Kopf, M.5
  • 16
    • 0037388467 scopus 로고    scopus 로고
    • Stoichiometry of site-specific protein phosphorylation estimated with phosphopeptide-specific antibodies
    • Miinea CP, Lienhard GE (2003) Stoichiometry of site-specific protein phosphorylation estimated with phosphopeptide-specific antibodies. Biotechniques 34: 828-831
    • (2003) Biotechniques , vol.34 , pp. 828-831
    • Miinea, C.P.1    Lienhard, G.E.2
  • 17
    • 0027168907 scopus 로고
    • Identification of the major phosphorylation sites of the Raf-1 kinase
    • Morrison DK, Heidecker G, Rapp UR, Copeland TD (1993) Identification of the major phosphorylation sites of the Raf-1 kinase. J Biol Chem 268: 17309-17316
    • (1993) J Biol Chem , vol.268 , pp. 17309-17316
    • Morrison, D.K.1    Heidecker, G.2    Rapp, U.R.3    Copeland, T.D.4
  • 18
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: PKC as a paradigm
    • Newton AC (2003) Regulation of the ABC kinases by phosphorylation: PKC as a paradigm. Biochem J 370: 361-371
    • (2003) Biochem J , vol.370 , pp. 361-371
    • Newton, A.C.1
  • 21
    • 0032477809 scopus 로고    scopus 로고
    • 2+-independent PKC AplII inhibits phorbol ester binding to the C1 domain in a phosphatidic acid-sensitive manner
    • 2+- independent PKC AplII inhibits phorbol ester binding to the C1 domain in a phosphatidic acid-sensitive manner. Biochemistry 37: 1256-1263
    • (1998) Biochemistry , vol.37 , pp. 1256-1263
    • Pepio, A.M.1    Sossin, W.S.2
  • 23
  • 24
    • 0030042104 scopus 로고    scopus 로고
    • Identification and location of an actin-binding motif that is unique to PKCε and participates in the regulation of synaptic function
    • Prekeris R, Mayhew MW, Cooper JB, Terrian DM (1996) Identification and location of an actin-binding motif that is unique to PKCε and participates in the regulation of synaptic function. J Cell Biol 132: 77-90
    • (1996) J Cell Biol , vol.132 , pp. 77-90
    • Prekeris, R.1    Mayhew, M.W.2    Cooper, J.B.3    Terrian, D.M.4
  • 26
    • 0347986633 scopus 로고    scopus 로고
    • Emerging and diverse roles of PKC in immune cell signalling
    • Tan SL, Parker PJ (2003) Emerging and diverse roles of PKC in immune cell signalling. Biochem J 376: 545-552
    • (2003) Biochem J , vol.376 , pp. 545-552
    • Tan, S.L.1    Parker, P.J.2
  • 28
    • 15444372337 scopus 로고    scopus 로고
    • Protein kinase specificity. A strategic collaboration between kinase peptide specificity and substrate recruitment
    • Zhu G, Liu Y, Shaw S (2005) Protein kinase specificity. A strategic collaboration between kinase peptide specificity and substrate recruitment. Cell Cycle 4: 52-56
    • (2005) Cell Cycle , vol.4 , pp. 52-56
    • Zhu, G.1    Liu, Y.2    Shaw, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.