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Volumn 405, Issue 2, 2007, Pages 331-340

Mechanism of membrane redistribution of protein kinase C by its ATP-competitive inhibitors

Author keywords

ATP binding site; Diacylglycerol; Protein kinase C; Protein kinase inhibitor; Translocation

Indexed keywords

DIACYLGLYCEROL; IMMUNOBLOT ANALYSIS; MEMBRANE REDISTRIBUTION; PROTEIN KINASE INHIBITOR;

EID: 34447136068     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070299     Document Type: Article
Times cited : (6)

References (41)
  • 1
    • 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
  • 2
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka, Y. (1992) Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258, 607-614
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 3
    • 0021879854 scopus 로고
    • Interleukin-2 stimulates association of protein kinase C with plasma membrane
    • Farrar, W. L. and Anderson, W. B. (1985) Interleukin-2 stimulates association of protein kinase C with plasma membrane. Nature 315, 233-235
    • (1985) Nature , vol.315 , pp. 233-235
    • Farrar, W.L.1    Anderson, W.B.2
  • 4
    • 0032582525 scopus 로고    scopus 로고
    • Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
    • Oancea, E. and Meyer, T. (1998) Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals. Cell 95, 307-318
    • (1998) Cell , vol.95 , pp. 307-318
    • Oancea, E.1    Meyer, T.2
  • 5
    • 0031466995 scopus 로고    scopus 로고
    • Direct visualization of the translocation of the γ-subspecies of protein kinase C in living cells using fusion proteins with green fluorescent protein
    • Sakai, N., Sasaki, K., Ikegaki, N., Shirai, Y., Ono, Y. and Saito, N. (1997) Direct visualization of the translocation of the γ-subspecies of protein kinase C in living cells using fusion proteins with green fluorescent protein. J. Cell Biol. 139, 1465-1476
    • (1997) J. Cell Biol , vol.139 , pp. 1465-1476
    • Sakai, N.1    Sasaki, K.2    Ikegaki, N.3    Shirai, Y.4    Ono, Y.5    Saito, N.6
  • 6
    • 0031865214 scopus 로고    scopus 로고
    • Three distinct mechanisms for translocation and activation of the δ subspecies of protein kinase C
    • Ohmori, S., Shirai, Y., Sakai, N., Fujii, M., Konishi, H., Kikkawa, U. and Saito, N. (1998) Three distinct mechanisms for translocation and activation of the δ subspecies of protein kinase C. Mol. Cell. Biol. 18, 5263-5271
    • (1998) Mol. Cell. Biol , vol.18 , pp. 5263-5271
    • Ohmori, S.1    Shirai, Y.2    Sakai, N.3    Fujii, M.4    Konishi, H.5    Kikkawa, U.6    Saito, N.7
  • 7
    • 0037124093 scopus 로고    scopus 로고
    • Importance of C1B domain for lipid messenger-induced targeting of protein kinase
    • Kashiwagi, K., Shirai, Y., Kuriyama, M., Sakai, N. and Saito, N. (2002) Importance of C1B domain for lipid messenger-induced targeting of protein kinase C. J. Biol. Chem. 277, 18037-18045
    • (2002) C. J. Biol. Chem , vol.277 , pp. 18037-18045
    • Kashiwagi, K.1    Shirai, Y.2    Kuriyama, M.3    Sakai, N.4    Saito, N.5
  • 8
    • 0037462741 scopus 로고    scopus 로고
    • Mechanisms of regulation of phospholipase D1 by protein kinase Cα
    • Hu, T. and Exton, J. H. (2003) Mechanisms of regulation of phospholipase D1 by protein kinase Cα. J. Biol. Chem. 278, 2348-2355
    • (2003) J. Biol. Chem , vol.278 , pp. 2348-2355
    • Hu, T.1    Exton, J.H.2
  • 9
    • 0037636466 scopus 로고    scopus 로고
    • The regulatory domain of protein kinase Cθ localises to the Golgi complex and induces apoptosis in neuroblastoma and Jurkat cells
    • Schultz, A., Jönsson, J.-I. and Larsson, C. (2003) The regulatory domain of protein kinase Cθ localises to the Golgi complex and induces apoptosis in neuroblastoma and Jurkat cells. Cell Death Differ. 10, 662-675
    • (2003) Cell Death Differ , vol.10 , pp. 662-675
    • Schultz, A.1    Jönsson, J.-I.2    Larsson, C.3
  • 10
    • 0033577576 scopus 로고    scopus 로고
    • PKCε, via its regulatory domain and independently of its catalytic domain, induces neurite-like processes in neuroblastoma cells
    • Zeidman, R., Löfgren, B., Påhlman, S. and Larsson, C. (1999) PKCε, via its regulatory domain and independently of its catalytic domain, induces neurite-like processes in neuroblastoma cells. J. Cell Biol. 145, 713-726
    • (1999) J. Cell Biol , vol.145 , pp. 713-726
    • Zeidman, R.1    Löfgren, B.2    Påhlman, S.3    Larsson, C.4
  • 12
    • 0026548701 scopus 로고
    • Kinetic analysis of protein kinase C inhibition by staurosporine: Evidence that inhibition entails inhibitor binding at a conserved region of the catalytic domain but not competition with substrates
    • Ward, N. E. and O'Brian, C. A. (1992) Kinetic analysis of protein kinase C inhibition by staurosporine: evidence that inhibition entails inhibitor binding at a conserved region of the catalytic domain but not competition with substrates. Mol. Pharmacol. 41, 387-392
    • (1992) Mol. Pharmacol , vol.41 , pp. 387-392
    • Ward, N.E.1    O'Brian, C.A.2
  • 17
    • 24644488646 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human atypical protein kinase C-ι reveals interaction mode of phosphorylation site in turn motif
    • Messerschmidt, A., Madeira, S., Velarde, M., Badeker, M., Benda, C., Jestel, A., Brandstetter, H., Neuefeind, T. and Blaesse, M. (2005) Crystal structure of the catalytic domain of human atypical protein kinase C-ι reveals interaction mode of phosphorylation site in turn motif. J. Mol. Biol. 352, 918-931
    • (2005) J. Mol. Biol , vol.352 , pp. 918-931
    • Messerschmidt, A.1    Madeira, S.2    Velarde, M.3    Badeker, M.4    Benda, C.5    Jestel, A.6    Brandstetter, H.7    Neuefeind, T.8    Blaesse, M.9
  • 18
    • 4644326204 scopus 로고    scopus 로고
    • Autophosphorylation suppresses whereas kinase inhibition augments the translocation of protein kinase Cα in response to diacylglycerol
    • Stensman, H., Rraghunath, A. and Larsson, C. (2004) Autophosphorylation suppresses whereas kinase inhibition augments the translocation of protein kinase Cα in response to diacylglycerol. J. Biol. Chem. 279, 40576-40583
    • (2004) J. Biol. Chem , vol.279 , pp. 40576-40583
    • Stensman, H.1    Rraghunath, A.2    Larsson, C.3
  • 19
    • 0037047310 scopus 로고    scopus 로고
    • Interplay between calcium, diacylglycerol and phosphorylation in the spatial and temporal regulation of PKCα-GFP
    • Tanimura, A., Nezu, A., Morita, T., Hashimoto, N. and Tojyo, Y. (2002) Interplay between calcium, diacylglycerol and phosphorylation in the spatial and temporal regulation of PKCα-GFP. J. Biol. Chem. 277, 29054-29062
    • (2002) J. Biol. Chem , vol.277 , pp. 29054-29062
    • Tanimura, A.1    Nezu, A.2    Morita, T.3    Hashimoto, N.4    Tojyo, Y.5
  • 20
    • 0032500506 scopus 로고    scopus 로고
    • An essential role for autophosphorylation in the dissociation of activated protein kinase C from the plasma membrane
    • Feng, X. and Hannun, Y. A. (1998) An essential role for autophosphorylation in the dissociation of activated protein kinase C from the plasma membrane. J. Biol. Chem. 273, 26870-26874
    • (1998) J. Biol. Chem , vol.273 , pp. 26870-26874
    • Feng, X.1    Hannun, Y.A.2
  • 21
    • 0038758753 scopus 로고    scopus 로고
    • 2 plus vanadate induce reverse translocation of phrbol-ester-activated PKCβII
    • 2 plus vanadate induce reverse translocation of phrbol-ester-activated PKCβII. Cell Struct. Funct. 28, 123-130
    • (2003) Cell Struct. Funct , vol.28 , pp. 123-130
    • Takahashi, H.1    Suzuki, K.2    Namiki, H.3
  • 22
    • 0035163570 scopus 로고    scopus 로고
    • Ceramide inhibition of NF-κB activation involves reverse translocation of classical protein kinase C (PKC) isoenzymes: Reqirement for kinase activity and carboxyl-terminal phosphorylation of PKC for ceramide response
    • Signorelli, P., Luberto, C. and Hannun, Y. A. (2001) Ceramide inhibition of NF-κB activation involves reverse translocation of classical protein kinase C (PKC) isoenzymes: reqirement for kinase activity and carboxyl-terminal phosphorylation of PKC for ceramide response. FASEB J. 15, 2401-2414
    • (2001) FASEB J , vol.15 , pp. 2401-2414
    • Signorelli, P.1    Luberto, C.2    Hannun, Y.A.3
  • 23
    • 4143050486 scopus 로고    scopus 로고
    • Protein kinase Cα translocates to the perinuclear region to activate phospholipase D1
    • Hu, T. and Exton, J. H. (2004) Protein kinase Cα translocates to the perinuclear region to activate phospholipase D1. J. Biol. Chem. 279, 35702-35708
    • (2004) J. Biol. Chem , vol.279 , pp. 35702-35708
    • Hu, T.1    Exton, J.H.2
  • 24
    • 3142654821 scopus 로고    scopus 로고
    • Isoenzyme-specific translocation of protein kinase C (PKCβII) and not PKCβI to a juxtanuclear subset of recycling endosomes
    • Becker, P. B. and Hannun, Y. A. (2004) Isoenzyme-specific translocation of protein kinase C (PKCβII) and not PKCβI to a juxtanuclear subset of recycling endosomes. J. Biol. Chem. 279, 28251-28256
    • (2004) J. Biol. Chem , vol.279 , pp. 28251-28256
    • Becker, P.B.1    Hannun, Y.A.2
  • 25
    • 1842582001 scopus 로고    scopus 로고
    • Ceramide-induced apoptosis by translocation, phosphorylation and activation of protein kinase Cδ in the Golgi complex
    • Kajimoto, T., Shirai, Y., Sakai, N., Yamamoto, T., Matsuzaki, H., Kikkawa, U. and Saito, N. (2004) Ceramide-induced apoptosis by translocation, phosphorylation and activation of protein kinase Cδ in the Golgi complex. J. Biol. Chem. 279, 12668-12676
    • (2004) J. Biol. Chem , vol.279 , pp. 12668-12676
    • Kajimoto, T.1    Shirai, Y.2    Sakai, N.3    Yamamoto, T.4    Matsuzaki, H.5    Kikkawa, U.6    Saito, N.7
  • 26
    • 0032568122 scopus 로고    scopus 로고
    • Identification of a BRCA1-associated kinase with potential biological relevance
    • Burke, T. F., Cocke, K. S., Lemke, S. J., Angleton, E., Becker, G. W. and Beckmann, R. P. (1998) Identification of a BRCA1-associated kinase with potential biological relevance. Oncogene 16, 1031-1040
    • (1998) Oncogene , vol.16 , pp. 1031-1040
    • Burke, T.F.1    Cocke, K.S.2    Lemke, S.J.3    Angleton, E.4    Becker, G.W.5    Beckmann, R.P.6
  • 27
    • 1642318398 scopus 로고    scopus 로고
    • Pervanadate-induced reverse translocation and tyrosine phosphorylation of phorbol ester-stimulated protein kinase C βII are mediated by Src-family tyrosine kinases in porcine neutrophils
    • Takahashi, H., Suzuki, K. and Namiki, H. (2004) Pervanadate-induced reverse translocation and tyrosine phosphorylation of phorbol ester-stimulated protein kinase C βII are mediated by Src-family tyrosine kinases in porcine neutrophils. Biochem. Biophys. Res. Commun. 314, 830-837
    • (2004) Biochem. Biophys. Res. Commun , vol.314 , pp. 830-837
    • Takahashi, H.1    Suzuki, K.2    Namiki, H.3
  • 28
    • 0022970190 scopus 로고
    • Quantitative measurement of sn-1,2-diacylglycerols present in platelets, hepatocytes and ras- and sis-transformed normal rat kidney cells
    • Preiss, J., Loomis, C. R., Bishop, W. R., Stein, R., Niedel, J. E. and Bell, R. M. (1986) Quantitative measurement of sn-1,2-diacylglycerols present in platelets, hepatocytes and ras- and sis-transformed normal rat kidney cells. J. Biol. Chem. 261, 8597-8600
    • (1986) J. Biol. Chem , vol.261 , pp. 8597-8600
    • Preiss, J.1    Loomis, C.R.2    Bishop, W.R.3    Stein, R.4    Niedel, J.E.5    Bell, R.M.6
  • 29
    • 0028959121 scopus 로고
    • Identification, activity and structural studies of peptides incorporating the phorbol ester-binding domain of protein kinase C
    • Wender, P. A., Irie, K. and Miller, B. L. (1995) Identification, activity and structural studies of peptides incorporating the phorbol ester-binding domain of protein kinase C. Proc. Natl. Acad. Sci. U.S.A. 92, 239-243
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 239-243
    • Wender, P.A.1    Irie, K.2    Miller, B.L.3
  • 30
    • 0035131424 scopus 로고    scopus 로고
    • Subtype-specific translocation of the δ subtype of protein kinase C and its activation by tyrosine phosphorylation induced by ceramide in HeLa cells
    • Kajimoto, T., Ohmori, S., Shirai, Y., Sakai, N. and Saito, N. (2001) Subtype-specific translocation of the δ subtype of protein kinase C and its activation by tyrosine phosphorylation induced by ceramide in HeLa cells. Mol. Cell. Biol. 21, 1769-1783
    • (2001) Mol. Cell. Biol , vol.21 , pp. 1769-1783
    • Kajimoto, T.1    Ohmori, S.2    Shirai, Y.3    Sakai, N.4    Saito, N.5
  • 32
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • Violin, J. D., Zhang, J., Tsien, R. Y. and Newton, A. C. (2003) A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C. J. Cell Biol. 161, 899-909
    • (2003) J. Cell Biol , vol.161 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2    Tsien, R.Y.3    Newton, A.C.4
  • 33
    • 0035918217 scopus 로고    scopus 로고
    • Nuclear import and export signals enable rapid nucleocytoplasmic shuttling of the atypical protein kinase Cλ
    • Perander, M., Bjørkøy, G. and Johansen, T. (2001) Nuclear import and export signals enable rapid nucleocytoplasmic shuttling of the atypical protein kinase Cλ. J. Biol. Chem. 276, 13015-13024
    • (2001) J. Biol. Chem , vol.276 , pp. 13015-13024
    • Perander, M.1    Bjørkøy, G.2    Johansen, T.3
  • 34
    • 0033538433 scopus 로고    scopus 로고
    • Interplay of C1 and C2 domain of protein kinase C-α in its membrane binding and activation
    • Medkova, M. and Cho, W. (1999) Interplay of C1 and C2 domain of protein kinase C-α in its membrane binding and activation. J. Boil. Chem. 274, 19852-19861
    • (1999) J. Boil. Chem , vol.274 , pp. 19852-19861
    • Medkova, M.1    Cho, W.2
  • 35
    • 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, B. 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, B.V.2    Cho, W.3
  • 37
    • 0026040577 scopus 로고
    • The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus
    • Divecha, N., Banfic, H. and Irvine, R. F. (1991) The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus. EMBO J. 10, 3207-3214
    • (1991) EMBO J , vol.10 , pp. 3207-3214
    • Divecha, N.1    Banfic, H.2    Irvine, R.F.3
  • 39
    • 0037059451 scopus 로고    scopus 로고
    • Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane
    • Baron, C. L. and Malhotra, V. (2002) Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane. Science 295, 325-328
    • (2002) Science , vol.295 , pp. 325-328
    • Baron, C.L.1    Malhotra, V.2
  • 41
    • 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. (2006) A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production. J. Biol. Chem. 282, 826-830
    • (2006) J. Biol. Chem , vol.282 , pp. 826-830
    • Dries, D.R.1    Gallegos, L.L.2    Newton, A.C.3


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