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Volumn 9, Issue 10, 1999, Pages 522-529

Rapamycin-sensitive phosphorylation of PKC on a carboxy-terminal site by an atypical PKC complex

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[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0033587133     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)80236-X     Document Type: Article
Times cited : (88)

References (32)
  • 1
    • 0026451081 scopus 로고
    • Intracellular signalling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y: Intracellular signalling by hydrolysis of phospholipids and activation of protein kinase C. Science 1992, 258:607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 2
    • 0027322679 scopus 로고
    • Protein kinase C isoenzymes - Divergence in signal transduction
    • Hug H, Sarre TF: Protein kinase C isoenzymes - Divergence in signal transduction. Biochem J 1993, 291:329-343.
    • (1993) Biochem J , vol.291 , pp. 329-343
    • Hug, H.1    Sarre, T.F.2
  • 3
    • 0028082161 scopus 로고
    • Protein kinase C - A question of specificity
    • Dekker LV, Parker PJ: Protein kinase C - A question of specificity. Trends Biochem Sci 1994, 19:73-77.
    • (1994) Trends Biochem Sci , vol.19 , pp. 73-77
    • Dekker, L.V.1    Parker, P.J.2
  • 4
    • 0029615509 scopus 로고
    • Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
    • Keranen LM, Dutil EM, Newton AC: Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Curr Biol 1995, 5:1394-1403.
    • (1995) Curr Biol , vol.5 , pp. 1394-1403
    • Keranen, L.M.1    Dutil, E.M.2    Newton, A.C.3
  • 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, Parker PJ: 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 1997, 272:3544-3549.
    • (1997) J Biol Chem , vol.272 , pp. 3544-3549
    • Bornancin, F.1    Parker, P.J.2
  • 7
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks SK, Hunter T: Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification. FASEB J 1995, 9:576-596.
    • (1995) FASEB J , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 9
    • 0027431089 scopus 로고
    • Molecular-cloning and characterization of PKC(iota), an atypical isoform of protein-kinase-C derived from insulin-secreting cells
    • Selbie LA, Schmitzpeiffer C, Sheng YH, Biden TJ: Molecular-cloning and characterization of PKC(iota), an atypical isoform of protein-kinase-C derived from insulin-secreting cells. J Biol Chem 1993, 268:24296-24302.
    • (1993) J Biol Chem , vol.268 , pp. 24296-24302
    • Selbie, L.A.1    Schmitzpeiffer, C.2    Sheng, Y.H.3    Biden, T.J.4
  • 10
    • 12644301164 scopus 로고    scopus 로고
    • 3-Phosphoinositide-dependent protein kinase-1 (PDK1): Structural and functional homology with the Drosophila DSTPK61 kinase
    • Alessi DR, Deak M, Casamayor A, Caudwell FB, Morrice N, Norman DG, et al.: 3-phosphoinositide-dependent protein kinase-1 (PDK1): Structural and functional homology with the Drosophila DSTPK61 kinase. Curr Biol 1997, 7:776-789.
    • (1997) Curr Biol , vol.7 , pp. 776-789
    • Alessi, D.R.1    Deak, M.2    Casamayor, A.3    Caudwell, F.B.4    Morrice, N.5    Norman, D.G.6
  • 11
    • 0032578999 scopus 로고    scopus 로고
    • Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B
    • Stephens L, Anderson K, Stokoe D, Erdjument-Bromage H, Painter GF, Holmes AB, et al.: Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B. Science 1998, 279:710-714.
    • (1998) Science , vol.279 , pp. 710-714
    • Stephens, L.1    Anderson, K.2    Stokoe, D.3    Erdjument-Bromage, H.4    Painter, G.F.5    Holmes, A.B.6
  • 13
    • 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 DR, Kozlowski MT, Weng QP, Morrice N, Avruch J: 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro. Curr Biol 1998, 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
  • 14
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
    • Le Good JA, Ziegler WH, Parekh DB, Alessi DR, Cohen P, Parker PJ: Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science 1998, 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
  • 17
    • 0030870169 scopus 로고    scopus 로고
    • Identification of serine-643 of protein-kinase C-delta as an important autophosphorylation site for its enzymatic-activity
    • Li WQ, Zhang JC, Bottaro DP, Li W, Pierce JH: Identification of serine-643 of protein-kinase C-delta as an important autophosphorylation site for its enzymatic-activity. J Biol Chem 1997, 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
  • 18
    • 0030740005 scopus 로고    scopus 로고
    • The modular phosphorylation and activation of P70S6K
    • Pullen N, Thomas G: The modular phosphorylation and activation of P70S6K. FEBS Lett 1997, 410:78-82.
    • (1997) FEBS Lett , vol.410 , pp. 78-82
    • Pullen, N.1    Thomas, G.2
  • 19
    • 0032143922 scopus 로고    scopus 로고
    • The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation
    • Garcia-Paramio P, Cabrerizo Y, Bornancin F, Parker PJ: The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation. Biochem J 1998, 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
  • 21
    • 0030707562 scopus 로고    scopus 로고
    • TOR signalling and control of cell growth
    • Thomas G, Hall MN: TOR signalling and control of cell growth. Curr Opin Cell Biol 1997, 9:782-787.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 782-787
    • Thomas, G.1    Hall, M.N.2
  • 22
    • 0027228165 scopus 로고
    • The immunosuppressant rapamycin induces inactivation of p70s6k through dephosphorylation of a novel set of sites
    • Ferrari S, Pearson RB, Siegmann M, Kozma SC, Thomas G: The immunosuppressant rapamycin induces inactivation of p70s6k through dephosphorylation of a novel set of sites. J Biol Chem 1993, 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
  • 23
    • 0030250879 scopus 로고    scopus 로고
    • Phosphorylation of threonine-638 critically controls the dephosphorylation and inactivation of protein-kinase C-alpha
    • Bornancin F, Parker P: Phosphorylation of threonine-638 critically controls the dephosphorylation and inactivation of protein-kinase C-alpha. Curr Biol 1996, 6:1114-1123.
    • (1996) Curr Biol , vol.6 , pp. 1114-1123
    • Bornancin, F.1    Parker, P.2
  • 24
    • 0025776523 scopus 로고
    • Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast
    • Heitman J, Movva NR, Hall MN: Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast Science 1991, 253:905-909.
    • (1991) Science , vol.253 , pp. 905-909
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 27
    • 0029828590 scopus 로고    scopus 로고
    • The principal rapamycin-sensitive p70s6k phosphorylation sites, T-229 and T-389, are differentially regulated by rapamycin-insensitive kinase kinases
    • Dennis PB, Pullen N, Kozma SC, Thomas G: The principal rapamycin-sensitive p70s6k phosphorylation sites, T-229 and T-389, are differentially regulated by rapamycin-insensitive kinase kinases. Mol Cell Biol 1996, 16:6242-6251.
    • (1996) Mol Cell Biol , vol.16 , pp. 6242-6251
    • Dennis, P.B.1    Pullen, N.2    Kozma, S.C.3    Thomas, G.4
  • 28
    • 0029656153 scopus 로고    scopus 로고
    • Constitutive activation of S6 kinase by deletion of amino-terminal autoinhibitory and rapamycin sensitivity domains
    • Mahalingam M, Templeton DJ: Constitutive activation of S6 kinase by deletion of amino-terminal autoinhibitory and rapamycin sensitivity domains. Mol Cell Biol 1996, 16:405-413.
    • (1996) Mol Cell Biol , vol.16 , pp. 405-413
    • Mahalingam, M.1    Templeton, D.J.2
  • 29
    • 0032486268 scopus 로고    scopus 로고
    • Amino acid sufficiency and mTOR regulate p70 S6 kinase and elf-4e BP1 through a common effector mechanism
    • Hara K, Yonezawa K, Weng QP, Kozlowski MT, Belham C, Avruch J: Amino acid sufficiency and mTor regulate p70 S6 kinase and elf-4e BP1 through a common effector mechanism. J Biol Chem 1998, 273:14484-14494.
    • (1998) J Biol Chem , vol.273 , pp. 14484-14494
    • Hara, K.1    Yonezawa, K.2    Weng, Q.P.3    Kozlowski, M.T.4    Belham, C.5    Avruch, J.6
  • 30
    • 0026659012 scopus 로고
    • Identification of multiple PKC isoforms in Swiss 3T3 cells - Differential down-regulation by phorbol ester
    • Olivier AR, Parker PJ: Identification of multiple PKC isoforms in Swiss 3T3 cells - Differential down-regulation by phorbol ester. J Cell Physiol 1992, 152:240-244.
    • (1992) J Cell Physiol , vol.152 , pp. 240-244
    • Olivier, A.R.1    Parker, P.J.2
  • 32
    • 0025858478 scopus 로고
    • Expression and characterization of PKC-δ
    • Olivier AR, Parker PJ: Expression and characterization of PKC-δ. Eur J Biochem 1991, 200:805-810.
    • (1991) Eur J Biochem , vol.200 , pp. 805-810
    • Olivier, A.R.1    Parker, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.