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Volumn 287, Issue 36, 2012, Pages 30518-30528

Protein kinase Cθ C2 domain is a phosphotyrosine binding module that plays a key role in its activation

Author keywords

[No Author keywords available]

Indexed keywords

AUTOINHIBITORY DOMAIN; BINDING DOMAIN; ENZYME ACTIVATION; HIGH AFFINITY; INTACT PROTEINS; N-TERMINALS; PHOSPHOTYROSINE BINDINGS; PROTEIN KINASE C; REPORTER GENE; T CELL RECEPTOR; T CELLS; T LYMPHOCYTES;

EID: 84865764384     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.391557     Document Type: Article
Times cited : (26)

References (60)
  • 1
    • 0035413601 scopus 로고    scopus 로고
    • Protein kinase C. Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions
    • Newton, A. C. (2001) Protein kinase C. Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions. Chem. Rev. 101, 2353-2364
    • (2001) Chem. Rev. , vol.101 , pp. 2353-2364
    • Newton, A.C.1
  • 2
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh, D. B., Ziegler, W., and Parker, P. J. (2000) Multiple pathways control protein kinase C phosphorylation. EMBO J. 19, 496-503
    • (2000) EMBO J. , vol.19 , pp. 496-503
    • Parekh, D.B.1    Ziegler, W.2    Parker, P.J.3
  • 3
    • 0036855827 scopus 로고    scopus 로고
    • Activation mechanisms of protein kinase C. Maturation, catalytic activation, and targeting
    • Shirai, Y., and Saito, N. (2002) Activation mechanisms of protein kinase C. Maturation, catalytic activation, and targeting. J. Biochem. 132, 663-668
    • (2002) J. Biochem. , vol.132 , pp. 663-668
    • Shirai, Y.1    Saito, N.2
  • 4
    • 0036905264 scopus 로고    scopus 로고
    • Move over protein kinase C, you've got company. Alternative cellular effectors of diacylglycerol and phorbol esters
    • Brose, N., and Rosenmund, C. (2002) Move over protein kinase C, you've got company. Alternative cellular effectors of diacylglycerol and phorbol esters. J. Cell Sci. 115, 4399-4411
    • (2002) J. Cell Sci. , vol.115 , pp. 4399-4411
    • Brose, N.1    Rosenmund, C.2
  • 5
    • 0242321186 scopus 로고    scopus 로고
    • Divergence and complexities in DAG signaling. Looking beyond PKC
    • Yang, C., and Kazanietz, M. G. (2003) Divergence and complexities in DAG signaling. Looking beyond PKC. Trends Pharmacol. Sci. 24, 602-608
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 602-608
    • Yang, C.1    Kazanietz, M.G.2
  • 6
    • 0344443708 scopus 로고    scopus 로고
    • Activation mechanisms of conventional protein kinase C isoforms are determined by the ligand affinity and conformational flexibility of their C1 domains
    • Ananthanarayanan, B., Stahelin, R. V., Digman, M. A., and Cho, W. (2003) Activation mechanisms of conventional protein kinase C isoforms are determined by the ligand affinity and conformational flexibility of their C1 domains. J. Biol. Chem. 278, 46886-46894
    • (2003) J. Biol. Chem. , vol.278 , pp. 46886-46894
    • Ananthanarayanan, B.1    Stahelin, R.V.2    Digman, M.A.3    Cho, W.4
  • 7
    • 0029670030 scopus 로고    scopus 로고
    • Protein kinase Cα contains two activator binding sites that bind phorbol esters and diacylglycerols with opposite affinities
    • Slater, S. J., Ho, C., Kelly, M. B., Larkin, J. D., Taddeo, F. J., Yeager, M. D., and Stubbs, C. D. (1996) Protein kinase Cα contains two activator binding sites that bind phorbol esters and diacylglycerols with opposite affinities. J. Biol. Chem. 271, 4627-4631
    • (1996) J. Biol. Chem. , vol.271 , pp. 4627-4631
    • Slater, S.J.1    Ho, C.2    Kelly, M.B.3    Larkin, J.D.4    Taddeo, F.J.5    Yeager, M.D.6    Stubbs, C.D.7
  • 8
    • 21244504606 scopus 로고    scopus 로고
    • Diacylglycerol-induced membrane targeting and activation of protein kinase Cε. Mechanistic differences between protein kinases Cδ and Cε
    • Stahelin, R. V., Digman, M. A., Medkova, M., Ananthanarayanan, B., Melowic, H. R., Rafter, J. D., and Cho, W. (2005) Diacylglycerol-induced membrane targeting and activation of protein kinase Cε. Mechanistic differences between protein kinases Cδ and Cε. J. Biol. Chem. 280, 19784-19793
    • (2005) J. Biol. Chem. , vol.280 , pp. 19784-19793
    • Stahelin, R.V.1    Digman, M.A.2    Medkova, M.3    Ananthanarayanan, B.4    Melowic, H.R.5    Rafter, J.D.6    Cho, W.7
  • 10
    • 4444368781 scopus 로고    scopus 로고
    • Identification of a general anesthetic binding site in the diacylglycerol-binding domain of protein kinase Cδ
    • Das, J., Addona, G. H., Sandberg, W. S., Husain, S. S., Stehle, T., and Miller, K. W. (2004) Identification of a general anesthetic binding site in the diacylglycerol-binding domain of protein kinase Cδ. J. Biol. Chem. 279, 37964-37972
    • (2004) J. Biol. Chem. , vol.279 , pp. 37964-37972
    • Das, J.1    Addona, G.H.2    Sandberg, W.S.3    Husain, S.S.4    Stehle, T.5    Miller, K.W.6
  • 12
    • 0142135568 scopus 로고    scopus 로고
    • Effects of ethanol on protein kinase C α activity induced by association with Rho GTPases
    • Slater, S. J., Cook, A. C., Seiz, J. L., Malinowski, S. A., Stagliano, B. A., and Stubbs, C. D. (2003) Effects of ethanol on protein kinase C α activity induced by association with Rho GTPases. Biochemistry 42, 12105-12114
    • (2003) Biochemistry , vol.42 , pp. 12105-12114
    • Slater, S.J.1    Cook, A.C.2    Seiz, J.L.3    Malinowski, S.A.4    Stagliano, B.A.5    Stubbs, C.D.6
  • 15
    • 0035980111 scopus 로고    scopus 로고
    • Membrane targeting by C1 and C2 domains
    • Cho, W. (2001) Membrane targeting by C1 and C2 domains. J. Biol. Chem. 276, 32407-32410
    • (2001) J. Biol. Chem. , vol.276 , pp. 32407-32410
    • Cho, W.1
  • 16
    • 33748324514 scopus 로고    scopus 로고
    • Membrane binding and subcellular targeting of C2 domains
    • Cho, W., and Stahelin, R. V. (2006) Membrane binding and subcellular targeting of C2 domains. Biochim. Biophys. Acta 1761, 838-849
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 838-849
    • Cho, W.1    Stahelin, R.V.2
  • 17
    • 54449098958 scopus 로고    scopus 로고
    • 3in plasma membrane targeting of C2 domains. Molecular dynamics simulation, membrane binding, and cell translocation studies of the PKCα C2 domain
    • 3 in plasma membrane targeting of C2 domains. Molecular dynamics simulation, membrane binding, and cell translocation studies of the PKCα C2 domain. J. Biol. Chem. 283, 26047-26058
    • (2008) J. Biol. Chem. , vol.283 , pp. 26047-26058
    • Manna, D.1    Bhardwaj, N.2    Vora, M.S.3    Stahelin, R.V.4    Lu, H.5    Cho, W.6
  • 18
    • 17444403210 scopus 로고    scopus 로고
    • The C2 domain of PKCδ is a phosphotyrosine binding domain
    • Benes, C. H., Wu, N., Elia, A. E., Dharia, T., Cantley, L. C., and Soltoff, S. P. (2005) The C2 domain of PKCδ is a phosphotyrosine binding domain. Cell 121, 271-280
    • (2005) Cell , vol.121 , pp. 271-280
    • Benes, C.H.1    Wu, N.2    Elia, A.E.3    Dharia, T.4    Cantley, L.C.5    Soltoff, S.P.6
  • 21
    • 0344443675 scopus 로고    scopus 로고
    • The simultaneous production of phosphatidic acid and diacylglycerol is essential for the translocation of protein kinase Cε to the plasma membrane in RBL-2H3 cells
    • Jose Lopez-Andreo, M., Gomez-Fernandez, J. C., and Corbalan-Garcia, S. (2003) The simultaneous production of phosphatidic acid and diacylglycerol is essential for the translocation of protein kinase Cε to the plasma membrane in RBL-2H3 cells. Mol. Biol. Cell 14, 4885-4895
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4885-4895
    • Jose Lopez-Andreo, M.1    Gomez-Fernandez, J.C.2    Corbalan-Garcia, S.3
  • 23
    • 34250692040 scopus 로고    scopus 로고
    • Protein kinase Cθ(PKCθ). A key player in T cell life and death
    • Hayashi, K., and Altman, A. (2007) Protein kinase Cθ(PKCθ). A key player in T cell life and death. Pharmacol. Res. 55, 537-544
    • (2007) Pharmacol. Res. , vol.55 , pp. 537-544
    • Hayashi, K.1    Altman, A.2
  • 24
    • 85047682875 scopus 로고    scopus 로고
    • Protein kinase Cθ in T cell activation
    • Isakov, N., and Altman, A. (2002) Protein kinase Cθ in T cell activation. Annu. Rev. Immunol. 20, 761-794
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 761-794
    • Isakov, N.1    Altman, A.2
  • 29
    • 34547118860 scopus 로고    scopus 로고
    • Mechanism of diacylglycerol-induced membrane targeting and activation of protein kinase Cθ
    • Melowic, H. R., Stahelin, R. V., Blatner, N. R., Tian, W., Hayashi, K., Altman, A., and Cho, W. (2007) Mechanism of diacylglycerol-induced membrane targeting and activation of protein kinase Cθ. J. Biol. Chem. 282, 21467-21476
    • (2007) J. Biol. Chem. , vol.282 , pp. 21467-21476
    • Melowic, H.R.1    Stahelin, R.V.2    Blatner, N.R.3    Tian, W.4    Hayashi, K.5    Altman, A.6    Cho, W.7
  • 30
    • 0033538433 scopus 로고    scopus 로고
    • Interplay of C1 and C2 domains of protein kinase C-α in its membrane binding and activation
    • Medkova, M., and Cho, W. (1999) Interplay of C1 and C2 domains of protein kinase C-α in its membrane binding and activation. J. Biol. Chem. 274, 19852-19861
    • (1999) J. Biol. Chem. , vol.274 , pp. 19852-19861
    • Medkova, M.1    Cho, W.2
  • 31
    • 0034602963 scopus 로고    scopus 로고
    • Regulation of protein kinase Cα function during T cell activation by Lck-mediated tyrosine phosphorylation
    • Liu, Y., Witte, S., Liu, Y. C., Doyle, M., Elly, C., and Altman, A. (2000) Regulation of protein kinase Cα 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
  • 32
    • 0004097379 scopus 로고
    • 2nd Ed., Elsevier Science Publishers B.V., Amsterdam
    • Kates, M. (1986) Techniques of Lipidology, 2nd Ed., pp. 114-115, Elsevier Science Publishers B.V., Amsterdam
    • (1986) Techniques of Lipidology , pp. 114-115
    • Kates, M.1
  • 33
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 34
    • 0036947279 scopus 로고    scopus 로고
    • Protein kinase C δ (PKCδ). Activation mechanisms and functions
    • Kikkawa, U., Matsuzaki, H., and Yamamoto, T. (2002) Protein kinase C δ (PKCδ). Activation mechanisms and functions. J. Biochem. 132, 831-839
    • (2002) J. Biochem. , vol.132 , pp. 831-839
    • Kikkawa, U.1    Matsuzaki, H.2    Yamamoto, T.3
  • 35
    • 34547122922 scopus 로고    scopus 로고
    • Ceramide-1-phosphate binds group IVA cytosolic phospholipase a2 via a novel site in the C2 domain
    • Stahelin, R. V., Subramanian, P., Vora, M., Cho, W., and Chalfant, C. E. (2007) Ceramide-1-phosphate binds group IVA cytosolic phospholipase a2 via a novel site in the C2 domain. J. Biol. Chem. 282, 20467-20474
    • (2007) J. Biol. Chem. , vol.282 , pp. 20467-20474
    • Stahelin, R.V.1    Subramanian, P.2    Vora, M.3    Cho, W.4    Chalfant, C.E.5
  • 36
    • 0032491210 scopus 로고    scopus 로고
    • Membrane penetration of cytosolic phospholipase A2 is necessary for its interfacial catalysis and arachidonate specificity
    • Lichtenbergova, L., Yoon, E. T., and Cho, W. (1998) Membrane penetration of cytosolic phospholipase A2 is necessary for its interfacial catalysis and arachidonate specificity. Biochemistry 37, 14128-14136
    • (1998) Biochemistry , vol.37 , pp. 14128-14136
    • Lichtenbergova, L.1    Yoon, E.T.2    Cho, W.3
  • 37
    • 0035830872 scopus 로고    scopus 로고
    • Roles of ionic residues of the C1 domain in protein kinase C-α activation and the origin of phosphatidylserine specificity
    • Bittova, L., Stahelin, R. V., and Cho, W. (2001) Roles of ionic residues of the C1 domain in protein kinase C-α activation and the origin of phosphatidylserine specificity. J. Biol. Chem. 276, 4218-4226
    • (2001) J. Biol. Chem. , vol.276 , pp. 4218-4226
    • Bittova, L.1    Stahelin, R.V.2    Cho, W.3
  • 38
    • 0035901553 scopus 로고    scopus 로고
    • Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions. A surface plasmon resonance study on phospholipases A2
    • Stahelin, R. V., and Cho, W. (2001) Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions. A surface plasmon resonance study on phospholipases A2. Biochemistry 40, 4672-4678
    • (2001) Biochemistry , vol.40 , pp. 4672-4678
    • Stahelin, R.V.1    Cho, W.2
  • 39
    • 0035503913 scopus 로고    scopus 로고
    • Roles of calcium ions in the membrane binding of C2 domains
    • Stahelin, R. V., and Cho, W. (2001) Roles of calcium ions in the membrane binding of C2 domains. Biochem. J. 359, 679-685
    • (2001) Biochem. J. , vol.359 , pp. 679-685
    • Stahelin, R.V.1    Cho, W.2
  • 41
    • 0037135529 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs
    • Stahelin, R. V., Long, F., Diraviyam, K., Bruzik, K. S., Murray, D., and Cho, W. (2002) Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs. J. Biol. Chem. 277, 26379-26388
    • (2002) J. Biol. Chem. , vol.277 , pp. 26379-26388
    • Stahelin, R.V.1    Long, F.2    Diraviyam, K.3    Bruzik, K.S.4    Murray, D.5    Cho, W.6
  • 45
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Lüthy, R., Bowie, J. U., and Eisenberg, D. (1992) Assessment of protein models with three-dimensional profiles. Nature 356, 83-85
    • (1992) Nature , vol.356 , pp. 83-85
    • Lüthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 46
    • 0026319199 scopus 로고
    • Protein folding and association. Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A., and Honig, B. (1991) Protein folding and association. Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 47
    • 0031001510 scopus 로고    scopus 로고
    • CD28 mediates transcriptional upregulation of the interleukin-2 (IL-2) promoter through a composite element containing the CD28RE and NFIL- 2B AP-1 sites
    • Shapiro, V. S., Truitt, K. E., Imboden, J. B., and Weiss, A. (1997) CD28 mediates transcriptional upregulation of the interleukin-2 (IL-2) promoter through a composite element containing the CD28RE and NFIL- 2B AP-1 sites. Mol. Cell Biol. 17, 4051-4058
    • (1997) Mol. Cell Biol. , vol.17 , pp. 4051-4058
    • Shapiro, V.S.1    Truitt, K.E.2    Imboden, J.B.3    Weiss, A.4
  • 48
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee. A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D. G., and Heringa, J. (2000) T-Coffee. A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302, 205-217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 49
    • 0036479136 scopus 로고    scopus 로고
    • Membrane targeting of C2 domains of phospholipase C-α isoforms
    • Ananthanarayanan, B., Das, S., Rhee, S. G., Murray, D., and Cho, W. (2002) Membrane targeting of C2 domains of phospholipase C-α isoforms. J. Biol. Chem. 277, 3568-3575
    • (2002) J. Biol. Chem. , vol.277 , pp. 3568-3575
    • Ananthanarayanan, B.1    Das, S.2    Rhee, S.G.3    Murray, D.4    Cho, W.5
  • 51
    • 0034724201 scopus 로고    scopus 로고
    • NF- κB activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-θ
    • Coudronniere, N., Villalba, M., Englund, N., and Altman, A. (2000) NF- κB activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-θ. Proc. Natl. Acad. Sci. U.S.A. 97, 3394-3399
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3394-3399
    • Coudronniere, N.1    Villalba, M.2    Englund, N.3    Altman, A.4
  • 52
    • 0034031401 scopus 로고    scopus 로고
    • Protein kinase C-θ participates in NF-κB activation induced by CD3-CD28 costimulation through selective activation of I κB kinase β
    • Lin, X., O'Mahony, A., Mu, Y., Geleziunas, R., and Greene, W. C. (2000) Protein kinase C-θ participates in NF-κB activation induced by CD3-CD28 costimulation through selective activation of I κB 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
  • 53
    • 0037092038 scopus 로고    scopus 로고
    • Translocation of PKCθ in T cells is mediated by a nonconventional, PI3K- and Vav-dependent pathway but does not absolutely require phospholipase C
    • Villalba, M., Bi, K., Hu, J., Altman, Y., Bushway, P., Reits, E., Neefjes, J., Baier, G., Abraham, R. T., and Altman, A. (2002) Translocation of PKCθ in T cells is mediated by a nonconventional, PI3K- and Vav-dependent pathway but does not absolutely require phospholipase C. J. Cell Biol. 157, 253-263
    • (2002) J. Cell Biol. , vol.157 , pp. 253-263
    • Villalba, M.1    Bi, K.2    Hu, J.3    Altman, Y.4    Bushway, P.5    Reits, E.6    Neefjes, J.7    Baier, G.8    Abraham, R.T.9    Altman, A.10
  • 54
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks, C. R., Freiberg, B. A., Kupfer, H., Sciaky, N., and Kupfer, A. (1998) Three-dimensional segregation of supramolecular activation clusters in T cells. Nature 395, 82-86
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 55
    • 33646560593 scopus 로고    scopus 로고
    • Diacylglycerol and protein kinase D localization during T lymphocyte activation
    • Spitaler, M., Emslie, E., Wood, C. D., and Cantrell, D. (2006) Diacylglycerol and protein kinase D localization during T lymphocyte activation. Immunity 24, 535-546
    • (2006) Immunity , vol.24 , pp. 535-546
    • Spitaler, M.1    Emslie, E.2    Wood, C.D.3    Cantrell, D.4
  • 58
    • 47949111533 scopus 로고    scopus 로고
    • Physiological role for phosphatidic acid in the translocation of the novel protein kinase C Apl II in Aplysia neurons
    • Farah, C. A., Nagakura, I., Weatherill, D., Fan, X., and Sossin, W. S. (2008) Physiological role for phosphatidic acid in the translocation of the novel protein kinase C Apl II in Aplysia neurons. Mol. Cell Biol. 28, 4719-4733
    • (2008) Mol. Cell Biol. , vol.28 , pp. 4719-4733
    • Farah, C.A.1    Nagakura, I.2    Weatherill, D.3    Fan, X.4    Sossin, W.S.5
  • 59
    • 33847746323 scopus 로고    scopus 로고
    • A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production
    • Dries, D. R., Gallegos, L. L., and Newton, A. C. (2007) A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production. J. Biol. Chem. 282, 826-830
    • (2007) J. Biol. Chem. , vol.282 , pp. 826-830
    • Dries, D.R.1    Gallegos, L.L.2    Newton, A.C.3
  • 60
    • 78650942010 scopus 로고    scopus 로고
    • Crystal structure and allosteric activation of protein kinase C βII
    • Leonard, T. A., Różycki, B., Saidi, L. F., Hummer, G., and Hurley, J. H. (2011) Crystal structure and allosteric activation of protein kinase C βII. Cell 144, 55-66
    • (2011) Cell , vol.144 , pp. 55-66
    • Leonard, T.A.1    Rózycki, B.2    Saidi, L.F.3    Hummer, G.4    Hurley, J.H.5


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