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Volumn 19, Issue 4, 2000, Pages 496-503

Multiple pathways control protein kinase C phosphorylation

Author keywords

mTOR; PDK1; Phosphatidylinositol 3 kinase; PKC related kinase; Protein kinase C

Indexed keywords

PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE C;

EID: 0034651539     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.4.496     Document Type: Review
Times cited : (517)

References (43)
  • 2
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein-kinase which phosphorylates and activates protein-kinase B-α
    • Alessi, D.R., James, S.R., Downes, C.R., Holmes, A.B., Gaffney, P.R.J., Reese, C.B. and Cohen, P. (1997) Characterization of a 3-phosphoinositide-dependent protein-kinase which phosphorylates and activates protein-kinase B-α. Curr. Biol., 7, 261-269.
    • (1997) Curr. Biol. , vol.7 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.R.3    Holmes, A.B.4    Gaffney, P.R.J.5    Reese, C.B.6    Cohen, P.7
  • 3
    • 0032518467 scopus 로고    scopus 로고
    • 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro
    • Alessi, D.R., Kozlowski, M.T., Weng, Q.P., Morrice, N. and Avruch, J. (1998) 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro. Curr. Biol., 8, 69-81.
    • (1998) Curr. Biol. , vol.8 , pp. 69-81
    • Alessi, D.R.1    Kozlowski, M.T.2    Weng, Q.P.3    Morrice, N.4    Avruch, J.5
  • 4
    • 0033594480 scopus 로고    scopus 로고
    • PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2
    • Balendran, A., Casamayor, A., Deak, M., Paterson, A., Gaffney, P., Currie, R., Downes, C.P. and Alessi, D.R. (1999) PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2. Curr. Biol., 9, 393-404.
    • (1999) Curr. Biol. , vol.9 , pp. 393-404
    • Balendran, A.1    Casamayor, A.2    Deak, M.3    Paterson, A.4    Gaffney, P.5    Currie, R.6    Downes, C.P.7    Alessi, D.R.8
  • 5
    • 0030250879 scopus 로고    scopus 로고
    • Phosphorylation of threonine-638 critically controls the dephosphorylation and inactivation of protein-kinase C-α
    • Bornancin, F. and Parker, P.J. (1996) Phosphorylation of threonine-638 critically controls the dephosphorylation and inactivation of protein-kinase C-α. Curr. Biol., 6, 1114-1123.
    • (1996) Curr. Biol. , vol.6 , pp. 1114-1123
    • Bornancin, F.1    Parker, P.J.2
  • 6
    • 0031021875 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase C-α on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state
    • Bornancin, F. and Parker, P.J. (1997) Phosphorylation of protein kinase C-α on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state. J. Biol. Chem., 272, 3544-3549.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3544-3549
    • Bornancin, F.1    Parker, P.J.2
  • 7
    • 0024121592 scopus 로고
    • Continuous synthesis of two protein kinase C-related proteins after down-regulation by phorbol esters
    • Borner, C. Eppenberger, U., Wyss, R. and Fabbro, D. (1988) Continuous synthesis of two protein kinase C-related proteins after down-regulation by phorbol esters. Proc. Natl Acad. Sci. USA, 85, 2110-2114.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2110-2114
    • Borner, C.1    Eppenberger, U.2    Wyss, R.3    Fabbro, D.4
  • 8
    • 0028108027 scopus 로고
    • Threonine-497 is a critical site for permissive activation of protein kinase Cα
    • Cazaubon, S., Bornancin, F. and Parker, P.J. (1994) Threonine-497 is a critical site for permissive activation of protein kinase Cα. Biochem. J., 301, 443-448.
    • (1994) Biochem. J. , vol.301 , pp. 443-448
    • Cazaubon, S.1    Bornancin, F.2    Parker, P.J.3
  • 10
    • 0028082161 scopus 로고
    • Protein kinase C - A question of specificity
    • Dekker, L.V. and Parker, P.J. (1994) Protein kinase C - a question of specificity. Trends Biochem. Sci., 19, 73-77.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 73-77
    • Dekker, L.V.1    Parker, P.J.2
  • 11
    • 0032585532 scopus 로고    scopus 로고
    • Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1)
    • Dutil, E.M., Toker, A. and Newton, A.C. (1998) Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (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
  • 12
    • 0030875555 scopus 로고    scopus 로고
    • Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C
    • Edwards, A.S. and Newton, A.C. (1997) Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C. J. Biol. Chem., 272, 18382-18390.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18382-18390
    • Edwards, A.S.1    Newton, A.C.2
  • 13
    • 0027228165 scopus 로고
    • The immunosuppressant rapamycin induces inactivation of p70s6k through dephosphorylation of a novel set of sites
    • Ferrari, S., Pearson, R.B., Siegmann, M., Kozma, S.C. and Thomas, G. (1993) The immunosuppressant rapamycin induces inactivation of p70s6k through dephosphorylation of a novel set of sites. J. Biol. Chem., 268, 16091-16094.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16091-16094
    • Ferrari, S.1    Pearson, R.B.2    Siegmann, M.3    Kozma, S.C.4    Thomas, G.5
  • 14
    • 0025004286 scopus 로고
    • Autophosphorylation of protein kinase C at three separated regions of its primary sequence
    • Flint, A.J., Paladini, R.D. and Koshland, D.E., Jr (1990) Autophosphorylation of protein kinase C at three separated regions of its primary sequence. Science, 249, 408-411.
    • (1990) Science , vol.249 , pp. 408-411
    • Flint, A.J.1    Paladini, R.D.2    Koshland D.E., Jr.3
  • 15
    • 0032579489 scopus 로고    scopus 로고
    • Multiple interactions of PRK1 with RHoA. Functional assignment of the HR1 repeat motif
    • Flynn, P., Mellor, H., Palmer, R., Panayotou, G. and Parker, P.J. (1998) Multiple interactions of PRK1 with RHoA. Functional assignment of the HR1 repeat motif. J. Biol. Chem., 273, 2698-2705.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2698-2705
    • Flynn, P.1    Mellor, H.2    Palmer, R.3    Panayotou, G.4    Parker, P.J.5
  • 17
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S.K. and Hunter, T. (1995) Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J., 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 18
    • 0030475207 scopus 로고    scopus 로고
    • 12-O-Tetradecanoylphorbol-13-acetate-induced dephosphorylation of protein kinase Cα correlates with the presence of a membrane associated protein phosphatase 2A heterotrimer
    • Hansra, G., Bornancin, F., Whelan, R., Hemmings, B.A. and Parker, P.J. (1996) 12-O-Tetradecanoylphorbol-13-acetate-induced dephosphorylation of protein kinase Cα correlates with the presence of a membrane associated protein phosphatase 2A heterotrimer. J. Biol. Chem., 271, 32785-32788.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32785-32788
    • Hansra, G.1    Bornancin, F.2    Whelan, R.3    Hemmings, B.A.4    Parker, P.J.5
  • 19
  • 20
    • 0027322679 scopus 로고
    • Protein kinase C isoenzymes: Divergence in signal transduction?
    • Hug, H. and Sarre, T.F. (1993) Protein kinase C isoenzymes: divergence in signal transduction? Biochem. J., 291, 329-343.
    • (1993) Biochem. J. , vol.291 , pp. 329-343
    • Hug, H.1    Sarre, T.F.2
  • 21
    • 0029965696 scopus 로고    scopus 로고
    • Protein kinase C isozymes and substrates
    • Jaken, S. (1996) Protein kinase C isozymes and substrates. Curr. Opin. Cell Biol., 8, 168-173.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 168-173
    • Jaken, S.1
  • 22
    • 0029615509 scopus 로고
    • Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
    • Keranen, L.M., Dutil, E.M. and Newton, A.C. (1995) Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Curr. Biol., 5, 1394-1403.
    • (1995) Curr. Biol. , vol.5 , pp. 1394-1403
    • Keranen, L.M.1    Dutil, E.M.2    Newton, A.C.3
  • 23
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D., Zheng, J., Teneyck, L., Ashford, V., Xuong, N., Taylor, S. and Sowadski, J. (1991) Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science, 253, 407-414.
    • (1991) Science , vol.253 , pp. 407-414
    • Knighton, D.1    Zheng, J.2    Teneyck, L.3    Ashford, V.4    Xuong, N.5    Taylor, S.6    Sowadski, J.7
  • 24
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
    • Le Good, J.A., Ziegler, W.H., Parekh, D.B., Alessi, D.R., Cohen, P. and Parker, P.J. (1998) Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science, 281, 2042-2045.
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 25
    • 0029757465 scopus 로고    scopus 로고
    • Dephosphorylation of activated protein kinase C contributes to down-regulation by bryostatin
    • Lee, H.W., Smith, L., Pettit, G.R. and Smith, J.B. (1996) Dephosphorylation of activated protein kinase C contributes to down-regulation by bryostatin. Am. J. Physiol., 40, C304-C311.
    • (1996) Am. J. Physiol. , vol.40
    • Lee, H.W.1    Smith, L.2    Pettit, G.R.3    Smith, J.B.4
  • 26
    • 0030870169 scopus 로고    scopus 로고
    • Identification of serine 643 of protein kinase C-δ as an important autophosphorylation site for its enzymatic activity
    • Li, W.Q., Zhang, J.C., Bottaro, D.P., Li, W. and Pierce, J.H. (1997) Identification of serine 643 of protein kinase C-δ as an important autophosphorylation site for its enzymatic activity. J. Biol. Chem., 272, 24550-24555.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24550-24555
    • Li, W.Q.1    Zhang, J.C.2    Bottaro, D.P.3    Li, W.4    Pierce, J.H.5
  • 27
    • 0029656153 scopus 로고    scopus 로고
    • Constitutive activation of S6 kinase by deletion of amino-terminal autoinhibitory and rapamycin sensitivity domains
    • Mahalingam, M. and Templeton, D.J. (1996) Constitutive activation of S6 kinase by deletion of amino-terminal autoinhibitory and rapamycin sensitivity domains. Mol. Cell. Biol., 16, 405-413.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 405-413
    • Mahalingam, M.1    Templeton, D.J.2
  • 28
    • 0032570560 scopus 로고    scopus 로고
    • PRK1 is targeted to endosomes by the small GTPase, RhoB
    • Mellor, H., Flynn, P., Nobes, C.D., Hall, A. and Parker, P.J. (1998) PRK1 is targeted to endosomes by the small GTPase, RhoB. J. Biol. Chem., 273, 4811-4814.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4811-4814
    • Mellor, H.1    Flynn, P.2    Nobes, C.D.3    Hall, A.4    Parker, P.J.5
  • 29
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton, A.C. (1997) Regulation of protein kinase C. Curr. Opin. Cell Biol., 9, 161-167.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 30
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Nishizuka, Y. (1986) Studies and perspectives of protein kinase C. Science, 233, 305-312.
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 31
    • 0027999633 scopus 로고
    • Requirement for negative charge on 'activation loop' of protein kinase C
    • Orr, J.W. and Newton, A.C. (1994) Requirement for negative charge on 'activation loop' of protein kinase C. J. Biol. Chem., 269, 27715-27718.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27715-27718
    • Orr, J.W.1    Newton, A.C.2
  • 32
    • 0033520995 scopus 로고    scopus 로고
    • mTOR controls one of two kinase pathways acting upon nPKCδ and nPKCε
    • Parekh, D., Ziegler, W., Yonezawa, K., Hara, K. and Parker, P.J. (1999) mTOR controls one of two kinase pathways acting upon nPKCδ and nPKCε. J. Biol. Chem., 274, 34758-34764.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34758-34764
    • Parekh, D.1    Ziegler, W.2    Yonezawa, K.3    Hara, K.4    Parker, P.J.5
  • 33
    • 0026519372 scopus 로고
    • Studies on the phosphorylation of protein kinase C-α
    • Pears. C., Stabel, S., Cazaubom, S. and Parker, P.J. (1992) Studies on the phosphorylation of protein kinase C-α. Biochem. J., 283, 515-518.
    • (1992) Biochem. J. , vol.283 , pp. 515-518
    • Pears, C.1    Stabel, S.2    Cazaubom, S.3    Parker, P.J.4
  • 34
    • 0030740005 scopus 로고    scopus 로고
    • The modular phosphorylation and activation of p70S6K
    • Pullen, N. and Thomas, G. (1997) The modular phosphorylation and activation of p70S6K. FEBS Lett., 410, 78-82.
    • (1997) FEBS Lett. , vol.410 , pp. 78-82
    • Pullen, N.1    Thomas, G.2
  • 37
    • 0029969880 scopus 로고    scopus 로고
    • Structural aspects of the functional modules in human protein kinase C α deduced from comparative analyses
    • Srinivasan, N., Bax, B., Blundell, T.L. and Parker, P.J. (1996) Structural aspects of the functional modules in human protein kinase C α deduced from comparative analyses. Proteins, 26, 217-235.
    • (1996) Proteins , vol.26 , pp. 217-235
    • Srinivasan, N.1    Bax, B.2    Blundell, T.L.3    Parker, P.J.4
  • 38
    • 0030894024 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase C δ (PKCδ) at threonine 505 is not a prerequisite for enzymatic activity
    • Stempka, L., Girod, A., Muller, H.J., Rincke, G., Marks, F., Gschwendt, M. and Bossemeyer, D. (1997) Phosphorylation of protein kinase C δ (PKCδ) at threonine 505 is not a prerequisite for enzymatic activity. J. Biol. Chem., 272, 6805-6811.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6805-6811
    • Stempka, L.1    Girod, A.2    Muller, H.J.3    Rincke, G.4    Marks, F.5    Gschwendt, M.6    Bossemeyer, D.7
  • 39
    • 0032578999 scopus 로고    scopus 로고
    • Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B
    • Stephens, L. et al. (1998) Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B. Science, 279, 710-714.
    • (1998) Science , vol.279 , pp. 710-714
    • Stephens, L.1
  • 42
    • 0032537024 scopus 로고    scopus 로고
    • Loss of protein kinase C function induces an apoptotic response
    • Whelan, D.H. and Parker, P.J. (1998) Loss of protein kinase C function induces an apoptotic response. Oncogene, 15, 1939-1944.
    • (1998) Oncogene , vol.15 , pp. 1939-1944
    • Whelan, D.H.1    Parker, P.J.2


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