메뉴 건너뛰기




Volumn 132, Issue 6, 2002, Pages 831-839

Protein kinase Cδ (PKCδ): Activation mechanisms and functions

Author keywords

Diacylglycerol; Phorbol ester; PKC ; Proteolysis; Tyrosine phosphorylation

Indexed keywords

CASPASE; DIACYLGLYCEROL; MEMBRANE PHOSPHOLIPID; MEMBRANE RECEPTOR; PHORBOL ESTER; PHOSPHATIDYLINOSITIDE; PROTEIN KINASE C DELTA;

EID: 0036947279     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a003294     Document Type: Article
Times cited : (204)

References (147)
  • 1
    • 0024287792 scopus 로고
    • The structure, expression, and properties of additional members of protein kinase C family
    • Ono, Y., Fujii, T, Ogita, K., Kikkawa, U., Igarashi, K., and Nishizuka, Y. (1988) The structure, expression, and properties of additional members of protein kinase C family J. Biol. Chem. 263, 6927-6932
    • (1988) J. Biol. Chem. , vol.263 , pp. 6927-6932
    • Ono, Y.1    Fujii, T.2    Ogita, K.3    Kikkawa, U.4    Igarashi, K.5    Nishizuka, Y.6
  • 3
    • 0025781579 scopus 로고
    • Mouse protein kinase C-δ, the major isoform expressed in mouse hemopoietic cells: Sequence of the cDNA, expression patterns and characterization of the protein
    • Mischak, H., Bodenteich, A., Kolch, W., Goodnight, J., Hofer, F., and Mushinski, J.F. (1991) Mouse protein kinase C-δ, the major isoform expressed in mouse hemopoietic cells: sequence of the cDNA, expression patterns and characterization of the protein. Biochemistry 30, 7925-7931
    • (1991) Biochemistry , vol.30 , pp. 7925-7931
    • Mischak, H.1    Bodenteich, A.2    Kolch, W.3    Goodnight, J.4    Hofer, F.5    Mushinski, J.F.6
  • 5
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka, Y. (1995) Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9, 484-496
    • (1995) FASEB J. , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 7
    • 0033082319 scopus 로고    scopus 로고
    • Protein kinase Cδ
    • Gschwendt, M. (1999) Protein kinase Cδ. Eur. J. Biochem. 259, 555-564
    • (1999) Eur. J. Biochem. , vol.259 , pp. 555-564
    • Gschwendt, M.1
  • 8
    • 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
  • 9
    • 0036952044 scopus 로고    scopus 로고
    • Protein kinase Cθ (PKCθ): A key enzyme in T cell life and death
    • Altman, A. and Villalba, M. (2002) Protein kinase Cθ (PKCθ): A key enzyme in T cell life and death. J. Biochem. 132, 841-846
    • (2002) J. Biochem. , vol.132 , pp. 841-846
    • Altman, A.1    Villalba, M.2
  • 10
    • 0028010010 scopus 로고
    • Assignment of the protein kinase Cδ polypeptide gene (PRKCD) to human chromosome 3 and mouse chromosome 14
    • Huppi, K., Siwarski, D., Goodnight, J., and Mischak, H. (1994) Assignment of the protein kinase Cδ polypeptide gene (PRKCD) to human chromosome 3 and mouse chromosome 14. Genomics 9, 161-162
    • (1994) Genomics , vol.9 , pp. 161-162
    • Huppi, K.1    Siwarski, D.2    Goodnight, J.3    Mischak, H.4
  • 11
    • 17344380849 scopus 로고    scopus 로고
    • Genomic structure and chromosomal localization of the rat protein kinase Cδ-gene
    • Kurkinen, K.M., Keinanen, R.A., Karhu, R., and Koistinaho, J. (2000) Genomic structure and chromosomal localization of the rat protein kinase Cδ-gene. Gene 242, 115-123
    • (2000) Gene , vol.242 , pp. 115-123
    • Kurkinen, K.M.1    Keinanen, R.A.2    Karhu, R.3    Koistinaho, J.4
  • 12
    • 0034820345 scopus 로고    scopus 로고
    • Novel protein kinase Cδ isoform insensitive to caspase-3
    • Sakurai, Y., Onishi, Y., Tanimoto, Y., and Kizaki, H. (2001) Novel protein kinase Cδ isoform insensitive to caspase-3. Biol. Pharm. Bull. 24, 973-977
    • (2001) Biol. Pharm. Bull. , vol.24 , pp. 973-977
    • Sakurai, Y.1    Onishi, Y.2    Tanimoto, Y.3    Kizaki, H.4
  • 13
    • 0034673564 scopus 로고    scopus 로고
    • cDNA cloning of an alternative splicing variant of protein kinase Cδ (PKCδIII), a new truncated form of PKCδ, in rats
    • Ueyama, T., Ren, Y., Ohmori, S., Sakai, K., Tamaki, N., and Saito, N. (2000) cDNA cloning of an alternative splicing variant of protein kinase Cδ (PKCδIII), a new truncated form of PKCδ, in rats. Biochem. Biophys. Res. Commun. 269, 557-563
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 557-563
    • Ueyama, T.1    Ren, Y.2    Ohmori, S.3    Sakai, K.4    Tamaki, N.5    Saito, N.6
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0028979464 scopus 로고
    • Crystal structure of the cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester
    • Zhang, G., Kazanietz, M.G., Blumberg, P.M., and Hurley, J.H. (1995) Crystal structure of the cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester Cell 81, 917-924
    • (1995) Cell , vol.81 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 19
    • 0029785953 scopus 로고    scopus 로고
    • Non-equivalent roles for the first and second zinc fingers of protein kinase Cd. Effect of their ester-induced translocation in NIH 3T3 cells
    • Szallasi, Z., Bogi, K., Gohari, S., Biro, T., Acs, P., and Blumberg, P.M. (1996) Non-equivalent roles for the first and second zinc fingers of protein kinase Cd. Effect of their ester-induced translocation in NIH 3T3 cells. J. Biol. Chem. 271, 18299-18301
    • (1996) J. Biol. Chem. , vol.271 , pp. 18299-18301
    • Szallasi, Z.1    Bogi, K.2    Gohari, S.3    Biro, T.4    Acs, P.5    Blumberg, P.M.6
  • 20
    • 0031014220 scopus 로고    scopus 로고
    • Cysteine-rich regions of protein kinase Cδ are functionally non-equivalent. Differences between cysteine-rich regions of non-calcium-dependent protein kinase Cδ and calcium-dependent protein kinase Cγ
    • Hunn, M. and Quest, A.F.G. (1997) Cysteine-rich regions of protein kinase Cδ are functionally non-equivalent. Differences between cysteine-rich regions of non-calcium-dependent protein kinase Cδ and calcium-dependent protein kinase Cγ. FEBS Lett. 400, 226-232
    • (1997) FEBS Lett. , vol.400 , pp. 226-232
    • Hunn, M.1    Quest, A.F.G.2
  • 21
    • 0034903846 scopus 로고    scopus 로고
    • Toward the identification of selective modulators of protein kinase C (PKC) isozymes: Establishment of a binding assay for PKC isozymes using synthetic C1 peptide receptors and identification of the critical residues in the phorbol ester binding
    • Shindo, M., Irie, K., Nakahara, A., Ohigashi, H., Konishi, H., Kikkawa, U., Fukuda, H., and Wender, P.A. (2001) Toward the identification of selective modulators of protein kinase C (PKC) isozymes: establishment of a binding assay for PKC isozymes using synthetic C1 peptide receptors and identification of the critical residues in the phorbol ester binding. Bioorg. Med. Chem. 9, 2073-2081
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 2073-2081
    • Shindo, M.1    Irie, K.2    Nakahara, A.3    Ohigashi, H.4    Konishi, H.5    Kikkawa, U.6    Fukuda, H.7    Wender, P.A.8
  • 22
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • Nalefski, E.A. and Falke, J.J. (1996) The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci. 5, 2375-2390
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 23
    • 0036230303 scopus 로고    scopus 로고
    • Two-dimensional crystal structures of protein kinase C-δ, its regulatory domain, and the enzyme complexed with myelin basic protein
    • Solodukhin, A.S., Caldwell, H.L., Sando, J.J., and Kretsinger, R.H. (2002) Two-dimensional crystal structures of protein kinase C-δ, its regulatory domain, and the enzyme complexed with myelin basic protein. Biophys. J. 82, 2700-2708
    • (2002) Biophys. J. , vol.82 , pp. 2700-2708
    • Solodukhin, A.S.1    Caldwell, H.L.2    Sando, J.J.3    Kretsinger, R.H.4
  • 24
    • 0025858478 scopus 로고
    • Expression and characterization of protein kinase C-δ
    • Olivier, A.R. and Parker, P.J. (1991) Expression and characterization of protein kinase C-δ. Eur. J. Biochem. 200, 805-810
    • (1991) Eur. J. Biochem. , vol.200 , pp. 805-810
    • Olivier, A.R.1    Parker, P.J.2
  • 26
    • 0026519632 scopus 로고
    • Protein kinase C group B members PKC-δ, -ε, -ζ and PKC-L(η). Comparison of properties of recombinant proteins in vitro and in vivo
    • Liyanage, M., Frith, D., Livneh, E., and Stabel, S. (1992) Protein kinase C group B members PKC-δ, -ε, -ζ and PKC-L(η). Comparison of properties of recombinant proteins in vitro and in vivo. Biochem. J. 283, 781-787
    • (1992) Biochem. J. , vol.283 , pp. 781-787
    • Liyanage, M.1    Frith, D.2    Livneh, E.3    Stabel, S.4
  • 27
    • 0028024930 scopus 로고
    • Bombesin, platelet-derived growth factor, and diacylglycerol induce selective membrane association and down-regulation of protein kinase C isotypes in Swiss 3T3 cells
    • Olivier, A.R. and Parker, P.J. (1994) Bombesin, platelet-derived growth factor, and diacylglycerol induce selective membrane association and down-regulation of protein kinase C isotypes in Swiss 3T3 cells. J. Biol. Chem. 269, 2758-2763
    • (1994) J. Biol. Chem. , vol.269 , pp. 2758-2763
    • Olivier, A.R.1    Parker, P.J.2
  • 28
    • 0028340177 scopus 로고
    • Activation of novel protein kinases Cδ and Cε upon mitogenic stimulation of quiescent rat 3Y1 fibroblasts
    • Ohno, S., Mizuno, K., Adachi, Y., Hata, A., Akita, Y., Akimoto, K., Osada, S., Hirai, S., and Suzuki, K. (1994) Activation of novel protein kinases Cδ and Cε upon mitogenic stimulation of quiescent rat 3Y1 fibroblasts. J. Biol. Chem. 269, 17495-17501
    • (1994) J. Biol. Chem. , vol.269 , pp. 17495-17501
    • Ohno, S.1    Mizuno, K.2    Adachi, Y.3    Hata, A.4    Akita, Y.5    Akimoto, K.6    Osada, S.7    Hirai, S.8    Suzuki, K.9
  • 29
    • 0025045877 scopus 로고
    • Purification and characterization of a calcium-unresponsive, phorbol ester/phospholipid-activated protein kinase from porcine spleen
    • Leibersperger, H., Gschwendt, M., and Marks, F. (1990) Purification and characterization of a calcium-unresponsive, phorbol ester/phospholipid-activated protein kinase from porcine spleen. J. Biol. Chem. 265, 16108-16115
    • (1990) J. Biol. Chem. , vol.265 , pp. 16108-16115
    • Leibersperger, H.1    Gschwendt, M.2    Marks, F.3
  • 30
    • 0028936086 scopus 로고
    • Distinct effects of saturated fatty acids on protein kinase C subspecies
    • Kasahara, K. and Kikkawa, U. (1995) Distinct effects of saturated fatty acids on protein kinase C subspecies. J. Biochem. 117, 648-653
    • (1995) J. Biochem. , vol.117 , pp. 648-653
    • Kasahara, K.1    Kikkawa, U.2
  • 31
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L.N., Noble, M.E., and Owen, D.J. (1996) Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 33
    • 0030894024 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase Cδ (PKCδ) at threonine 505 is not a prerequisite for enzymatic activity. Expression of rat PKCδ and an alanine 505 mutant in bacteria in a functional form
    • Stempka, L., Girod, A., Muller, H.J., Rincke, G., Marks, F., Gschwendt, M., and Bossemeyer, D. (1997) Phosphorylation of protein kinase Cδ (PKCδ) at threonine 505 is not a prerequisite for enzymatic activity. Expression of rat PKCδ and an alanine 505 mutant in bacteria in a functional form. 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
  • 34
    • 0344141205 scopus 로고    scopus 로고
    • Requirements of protein kinase Cδ for catalytic function. Role of glutamic acid 500 and autophosphorylation on serine 643
    • Stempka, L., Schnolzer, M., Radke, S., Rincke, G., Marks, F., and Gschwendt, M. (1999) Requirements of protein kinase Cδ for catalytic function. Role of glutamic acid 500 and autophosphorylation on serine 643. J. Biol. Chem. 274, 8886-8892
    • (1999) J. Biol. Chem. , vol.274 , pp. 8886-8892
    • Stempka, L.1    Schnolzer, M.2    Radke, S.3    Rincke, G.4    Marks, F.5    Gschwendt, M.6
  • 35
    • 0034634443 scopus 로고    scopus 로고
    • Further evidence that 3-phosphoinositide-dependent protein kinase-1 (PDK1) is required for the stability and phosphorylation of protein kinase C (PKC) isoforms
    • Balendran, A., Hare, G.R., Kieloch, A., Williams, M.R., and Alessi, D.R. (2000) Further evidence that 3-phosphoinositide-dependent protein kinase-1 (PDK1) is required for the stability and phosphorylation of protein kinase C (PKC) isoforms. FEBS Lett. 484, 217-223
    • (2000) FEBS Lett. , vol.484 , pp. 217-223
    • Balendran, A.1    Hare, G.R.2    Kieloch, A.3    Williams, M.R.4    Alessi, D.R.5
  • 36
    • 0030870169 scopus 로고    scopus 로고
    • Identification of serine 643 of protein kinase C-δ as an important auto-phosphorylation site for its enzymatic activity
    • Li, W., Zhang, J., Bottaro, D.P., and Pierce, J.H. (1997) Identification of serine 643 of protein kinase C-δ as an important auto-phosphorylation site for its enzymatic activity. J. Biol. Chem. 272, 24550-24555
    • (1997) J. Biol. Chem. , vol.272 , pp. 24550-24555
    • Li, W.1    Zhang, J.2    Bottaro, D.P.3    Pierce, J.H.4
  • 37
    • 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
  • 39
    • 0033520995 scopus 로고    scopus 로고
    • Mammalian TOR controls one of two kinase pathways acting upon nPKCδ and nPKCε
    • Parekh, D., Ziegler, W., Yonezawa, K., Hara, K., and Parker, P.J. (1999) Mammalian TOR controls one of two kinase pathways acting upon nPKCδ and nPKCε. J. Biol. Chem. 274, 34758-34564
    • (1999) J. Biol. Chem. , vol.274 , pp. 34758-34564
    • Parekh, D.1    Ziegler, W.2    Yonezawa, K.3    Hara, K.4    Parker, P.J.5
  • 40
    • 0034161545 scopus 로고    scopus 로고
    • Functional interaction between RAFT1/FRAP/mTOR and protein kinase Cδ in the regulation of cap-dependent initiation of translation
    • Kumar, V., Pandey, P., Sabatini, D., Kumar, M., Majumder, P.K., Bharti, A., Carmichael, G., Kufe, D., and Kharbanda, S. (2000) Functional interaction between RAFT1/FRAP/mTOR and protein kinase Cδ in the regulation of cap-dependent initiation of translation. EMBO J. 19, 1087-1097
    • (2000) EMBO J. , vol.19 , pp. 1087-1097
    • Kumar, V.1    Pandey, P.2    Sabatini, D.3    Kumar, M.4    Majumder, P.K.5    Bharti, A.6    Carmichael, G.7    Kufe, D.8    Kharbanda, S.9
  • 42
    • 0027332733 scopus 로고
    • Expression of an oncogenic rasHa gene in murine keratinocytes induces tyrosine phosphorylation and reduced activity of protein kinase Cδ
    • Denning, M.F., Dlugosz, A.A., Howett, M.K., and Yuspa, S.H. (1993) Expression of an oncogenic rasHa gene in murine keratinocytes induces tyrosine phosphorylation and reduced activity of protein kinase Cδ. J. Biol. Chem. 268, 26079-26081
    • (1993) J. Biol. Chem. , vol.268 , pp. 26079-26081
    • Denning, M.F.1    Dlugosz, A.A.2    Howett, M.K.3    Yuspa, S.H.4
  • 44
    • 0028355919 scopus 로고
    • Insulin-stimulated tyrosine phosphorylation of protein kinase Cα: Evidence for direct interaction of the insulin receptor and protein kinase C in cells
    • Liu, F. and Roth, R.A. (1994) Insulin-stimulated tyrosine phosphorylation of protein kinase Cα: evidence for direct interaction of the insulin receptor and protein kinase C in cells. Biochem. Biophys. Res. Commun. 200, 1570-1577
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 1570-1577
    • Liu, F.1    Roth, R.A.2
  • 46
    • 0034602963 scopus 로고    scopus 로고
    • Regulation of protein kinase Cθ 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 Cθ 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
  • 47
    • 0035193041 scopus 로고    scopus 로고
    • Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase C’s via a src kinase pathway
    • Wooten, M.W., Vandenplas, M.L., Seibenhener, M.L., Geetha, T., and Diaz-Meco, M.T. (2001) Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase C’s via a src kinase pathway. Mol. Cell. Biol. 21, 8414-8427
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8414-8427
    • Wooten, M.W.1    Vandenplas, M.L.2    Seibenhener, M.L.3    Geetha, T.4    Diaz-Meco, M.T.5
  • 48
    • 0028851535 scopus 로고
    • Development of a rapid approach to identification of tyrosine phosphorylation sites: Application to PKCδ phosphorylated upon activation of the high affinity receptor for IgE in rat basophilic leukemia cells
    • Szallasi, Z., Denning, M.F., Chang, E.-Y., Rivera, J., Yuspa, S.H., Lehel, C., Olah, Z., Anderson, W.B., and Blumberg, P.M. (1995) Development of a rapid approach to identification of tyrosine phosphorylation sites: application to PKCδ phosphorylated upon activation of the high affinity receptor for IgE in rat basophilic leukemia cells. Biochem. Biophys. Res. Commun. 214, 888-894
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 888-894
    • Szallasi, Z.1    Denning, M.F.2    Chang, E.-Y.3    Rivera, J.4    Yuspa, S.H.5    Lehel, C.6    Olah, Z.7    Anderson, W.B.8    Blumberg, P.M.9
  • 51
    • 0028229299 scopus 로고
    • Tyrosine phosphorylation and stimulation of protein kinase Cδ from porcine spleen by src in vitro. Dependence on the activated state of protein kinase Cδ
    • Gschwendt, M., Kielbassa, K., Kittstein, W., and Marks, F. (1994) Tyrosine phosphorylation and stimulation of protein kinase Cδ from porcine spleen by src in vitro. Dependence on the activated state of protein kinase Cδ. FEBS Lett. 347, 85-89
    • (1994) FEBS Lett. , vol.347 , pp. 85-89
    • Gschwendt, M.1    Kielbassa, K.2    Kittstein, W.3    Marks, F.4
  • 52
    • 0029924152 scopus 로고    scopus 로고
    • Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase Cδ
    • Denning, M.F., Dlugosz, A.A., Threadgill, D.W., Magnuson, T., and Yuspa, S.H. (1996) Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase Cδ. J. Biol. Chem. 271, 5325-5331
    • (1996) J. Biol. Chem. , vol.271 , pp. 5325-5331
    • Denning, M.F.1    Dlugosz, A.A.2    Threadgill, D.W.3    Magnuson, T.4    Yuspa, S.H.5
  • 54
    • 0030976892 scopus 로고    scopus 로고
    • Association between v-Src and protein kinase Cδ in v-Src-transformed fibroblasts
    • Zang, Q., Lu, Z.M., Curto, M., Barile, N., Shalloway, D., and Foster, D.A. (1997) Association between v-Src and protein kinase Cδ in v-Src-transformed fibroblasts. J. Biol. Chem. 272, 13275-13280
    • (1997) J. Biol. Chem. , vol.272 , pp. 13275-13280
    • Zang, Q.1    Lu, Z.M.2    Curto, M.3    Barile, N.4    Shalloway, D.5    Foster, D.A.6
  • 55
    • 0032474741 scopus 로고    scopus 로고
    • Tyrosine phosphorylation-dependent and -independent associations of protein kinase C-δ with Src family kinases in the RBL-2H3 mast cell line: Regulation of Src family kinase activity by protein kinase C-δ
    • Song, J.S., Swann, P.G., Szallasi, Z., Blank, U., Blumberg, P.M., and Rivera, J. (1998) Tyrosine phosphorylation-dependent and -independent associations of protein kinase C-δ with Src family kinases in the RBL-2H3 mast cell line: regulation of Src family kinase activity by protein kinase C-δ. Oncogene 16, 3357-3368
    • (1998) Oncogene , vol.16 , pp. 3357-3368
    • Song, J.S.1    Swann, P.G.2    Szallasi, Z.3    Blank, U.4    Blumberg, P.M.5    Rivera, J.6
  • 56
    • 0032473917 scopus 로고    scopus 로고
    • Activation of protein kinase C delta by the c-Abl tyrosine kinase in response to ionizing radiation
    • Yuan, Z.M., Utsugisawa, T., Ishiko, T., Nakada, S., Huang, Y., Kharbanda, S., Weichselbaum, R., and Kufe, D. (1998) Activation of protein kinase C delta by the c-Abl tyrosine kinase in response to ionizing radiation. Oncogene 16, 1643-1648
    • (1998) Oncogene , vol.16 , pp. 1643-1648
    • Yuan, Z.M.1    Utsugisawa, T.2    Ishiko, T.3    Nakada, S.4    Huang, Y.5    Kharbanda, S.6    Weichselbaum, R.7    Kufe, D.8
  • 57
    • 0034677930 scopus 로고    scopus 로고
    • Interaction between protein kinase Cδ and the c-Abl tyrosine kinase in the cellular response to oxidative stress
    • Sun, X., Wu, F., Datta, R., Kharbanda, S., and Kufe, D. (2000) Interaction between protein kinase Cδ and the c-Abl tyrosine kinase in the cellular response to oxidative stress. J. Biol. Chem. 275, 7470-7473
    • (2000) J. Biol. Chem. , vol.275 , pp. 7470-7473
    • Sun, X.1    Wu, F.2    Datta, R.3    Kharbanda, S.4    Kufe, D.5
  • 58
    • 0034810479 scopus 로고    scopus 로고
    • Carbachol stimulates TYR phosphorylation and association of PKCδ and PYK2 in pancreas
    • Wrenn, R.W. (2001) Carbachol stimulates TYR phosphorylation and association of PKCδ and PYK2 in pancreas. Biochem. Biophys. Res. Commun. 282, 882-886
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 882-886
    • Wrenn, R.W.1
  • 59
    • 0037023769 scopus 로고    scopus 로고
    • Src family kinases phosphorylate protein kinase Cδ on tyrosine residues and modify the neoplastic phenotype of skin keratinocytes
    • Joseloff, E., Cataisson, C., Aamodt, H., Ocheni, H., Blumberg, P., Kraker, A.J., and Yuspa, S.H. (2002) Src family kinases phosphorylate protein kinase Cδ on tyrosine residues and modify the neoplastic phenotype of skin keratinocytes. J. Biol. Chem. 277, 12318-12323
    • (2002) J. Biol. Chem. , vol.277 , pp. 12318-12323
    • Joseloff, E.1    Cataisson, C.2    Aamodt, H.3    Ocheni, H.4    Blumberg, P.5    Kraker, A.J.6    Yuspa, S.H.7
  • 60
    • 0027941342 scopus 로고
    • Stimulation of the platelet-derived growth factor β receptor signaling pathway activates protein kinase C-δ
    • Li, W., Yu, J.-C., Michieli, P., Beeler, J.F., Ellmore, N., Heidaran, M.A., and Pierce, J.H. (1994) Stimulation of the platelet-derived growth factor β receptor signaling pathway activates protein kinase C-δ. Mol. Cell. Biol. 14, 6727-6735
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6727-6735
    • Li, W.1    Yu, J.-C.2    Michieli, P.3    Beeler, J.F.4    Ellmore, N.5    Heidaran, M.A.6    Pierce, J.H.7
  • 61
    • 0029041743 scopus 로고
    • Carbachol, substance P, and phorbol ester promote the tyrosine phosphorylation of protein kinase Cδ in salivary gland epithelial cells
    • Soltoff, S.P. and Toker, A. (1995) Carbachol, substance P, and phorbol ester promote the tyrosine phosphorylation of protein kinase Cδ in salivary gland epithelial cells. J. Biol. Chem. 270, 13490-13495
    • (1995) J. Biol. Chem. , vol.270 , pp. 13490-13495
    • Soltoff, S.P.1    Toker, A.2
  • 62
    • 0031794093 scopus 로고    scopus 로고
    • Protein kinase C-δ activation and tyrosine phosphorylation in platelets
    • Moussazadeh, M. and Haimovich, B. (1998) Protein kinase C-δ activation and tyrosine phosphorylation in platelets. FEBS Lett. 438, 225-230
    • (1998) FEBS Lett. , vol.438 , pp. 225-230
    • Moussazadeh, M.1    Haimovich, B.2
  • 63
    • 0031684848 scopus 로고    scopus 로고
    • Protein kinase C-δ is an important signaling molecule in insulin-like growth factor I receptor-mediated cell transformation
    • Li, W., Jiang, Y.X., Zhang, J., Soon, L., Flechner, L., Kapoor, V., Pierce, J.H., and Wang, L.H. (1998) Protein kinase C-δ is an important signaling molecule in insulin-like growth factor I receptor-mediated cell transformation. Mol. Cell. Biol. 18, 5888-5898
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5888-5898
    • Li, W.1    Jiang, Y.X.2    Zhang, J.3    Soon, L.4    Flechner, L.5    Kapoor, V.6    Pierce, J.H.7    Wang, L.H.8
  • 64
    • 0033387429 scopus 로고    scopus 로고
    • Activation and tyrosine phosphorylation of protein kinase Cδ in response to B cell antigen receptor stimulation
    • Popoff, I.J. and Deans, J.P. (1999) Activation and tyrosine phosphorylation of protein kinase Cδ in response to B cell antigen receptor stimulation. Mol. Immunol. 36, 1005-1016
    • (1999) Mol. Immunol. , vol.36 , pp. 1005-1016
    • Popoff, I.J.1    Deans, J.P.2
  • 65
    • 0033520015 scopus 로고    scopus 로고
    • Protein kinase C-delta is a target of B-cell antigen receptor signaling
    • Barbazuk, S.M. and Gold, M.R. (1999) Protein kinase C-delta is a target of B-cell antigen receptor signaling. Immunol. Lett. 69, 259-267
    • (1999) Immunol. Lett. , vol.69 , pp. 259-267
    • Barbazuk, S.M.1    Gold, M.R.2
  • 66
    • 0034989803 scopus 로고    scopus 로고
    • Modulation of PKCδ tyrosine phosphorylation and activity in salivary and PC-12 cells by Src kinases
    • Benes, C. and Soltoff, S.P. (2001) Modulation of PKCδ tyrosine phosphorylation and activity in salivary and PC-12 cells by Src kinases. Am. J. Physiol. 280, C1498-C510
    • (2001) Am. J. Physiol. , vol.280 , pp. C1498-C1510
    • Benes, C.1    Soltoff, S.P.2
  • 67
    • 0029025924 scopus 로고
    • Tyrosine phosphorylation of protein kinase C-δ in response to the activation of the high-affinity receptor for immunoglobulin E modifies its substrate recognition
    • Haleen-Smith, H., Chang, E.-Y., Szallasi, Z., Blumberg, P.M., and Rivera, J. (1995) Tyrosine phosphorylation of protein kinase C-δ in response to the activation of the high-affinity receptor for immunoglobulin E modifies its substrate recognition. Proc. Natl. Acad. Sci. USA 92, 9112-9116
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9112-9116
    • Haleen-Smith, H.1    Chang, E.-Y.2    Szallasi, Z.3    Blumberg, P.M.4    Rivera, J.5
  • 68
    • 0034634651 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase Cδ on distinct tyrosine residues regulates specific cellular functions
    • Kronfeld, I., Kazimirsky, G., Lorenzo, P.S., Garfield, S.H., Blumberg, P.M., and Brodie, C. (2000) Phosphorylation of protein kinase Cδ on distinct tyrosine residues regulates specific cellular functions. J. Biol. Chem. 275, 35491-35498
    • (2000) J. Biol. Chem. , vol.275 , pp. 35491-35498
    • Kronfeld, I.1    Kazimirsky, G.2    Lorenzo, P.S.3    Garfield, S.H.4    Blumberg, P.M.5    Brodie, C.6
  • 69
    • 0342657745 scopus 로고    scopus 로고
    • Effect of a tyrosine 155 to phenylalanine mutation of protein kinase Cδ on the proliferative and tumorigenic properties of NIH 3T3 fibroblasts
    • Acs, P., Beheshti, M., Szallasi, Z., Li, L., Yuspa, S.H., and Blumberg, P.M. (2000) Effect of a tyrosine 155 to phenylalanine mutation of protein kinase Cδ on the proliferative and tumorigenic properties of NIH 3T3 fibroblasts. Carcinogenesis 21, 887-891
    • (2000) Carcinogenesis , vol.21 , pp. 887-891
    • Acs, P.1    Beheshti, M.2    Szallasi, Z.3    Li, L.4    Yuspa, S.H.5    Blumberg, P.M.6
  • 70
    • 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
  • 72
    • 0035812864 scopus 로고    scopus 로고
    • Oxidant-dependent phosphorylation of p40phox in B lymphocytes
    • Grandvaux, N., Elsen, S., and Vignais, P.V. (2001) Oxidant-dependent phosphorylation of p40phox in B lymphocytes. Biochem. Biophys. Res. Commun. 287, 1009-1016
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 1009-1016
    • Grandvaux, N.1    Elsen, S.2    Vignais, P.V.3
  • 73
    • 0036132855 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase Cδ is essential for its apoptotic effect in response to etoposide
    • Blass, M., Kronfeld, I., Kazimirsky, G., Blumberg, P.M., and Brodie, C. (2001) Tyrosine phosphorylation of protein kinase Cδ is essential for its apoptotic effect in response to etoposide. Mol. Cell. Biol. 22, 182-195
    • (2001) Mol. Cell. Biol. , vol.22 , pp. 182-195
    • Blass, M.1    Kronfeld, I.2    Kazimirsky, G.3    Blumberg, P.M.4    Brodie, C.5
  • 74
    • 0035971197 scopus 로고    scopus 로고
    • CD45 negatively regulates monocytic cell differentiation by inhibiting phorbol 12-myristate13-acetate-dependent activation and tyrosine phosphorylation of protein kinase Cδ
    • Deszo, E.L., Brake D.K., Cengel, K.A., Kelley, K.W., and Freund, G.G. (2001) CD45 negatively regulates monocytic cell differentiation by inhibiting phorbol 12-myristate13-acetate-dependent activation and tyrosine phosphorylation of protein kinase Cδ. J. Biol. Chem. 276, 10212-10217
    • (2001) J. Biol. Chem. , vol.276 , pp. 10212-10217
    • Deszo, E.L.1    Brake, D.K.2    Cengel, K.A.3    Kelley, K.W.4    Freund, G.G.5
  • 75
    • 0034647787 scopus 로고    scopus 로고
    • 2-induced tyrosine phosphorylation of protein kinase Cδ by a mechanism independent of inhibition of protein-tyrosine phosphatase in CHO and COS-7 cells
    • 2-induced tyrosine phosphorylation of protein kinase Cδ by a mechanism independent of inhibition of protein-tyrosine phosphatase in CHO and COS-7 cells. Biochem. Biophys. Res. Commun. 273, 960-966
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 960-966
    • Yamamoto, T.1    Matsuzaki, H.2    Konishi, H.3    Ono, Y.4    Kikkawa, U.5
  • 76
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • Gopalakrishna, R., and Jaken, S. (2000) Protein kinase C signaling and oxidative stress. Free Radic. Biol. Med. 28, 1349-1361
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 79
    • 0030734628 scopus 로고    scopus 로고
    • The proteolytic cleavage of protein kinase C isotypes, which generates kinase and regulatory fragments, correlates with Fas-mediated and 12-O-tetradecanoyl-phorbol-13-acetate-induced apoptosis
    • Mizuno, K., Noda, K., Araki, T., Imaoka, T., Kobayashi, Y., Akita, Y., Shimonaka, M., Kishi, S., and Ohno, S. (1997) The proteolytic cleavage of protein kinase C isotypes, which generates kinase and regulatory fragments, correlates with Fas-mediated and 12-O-tetradecanoyl-phorbol-13-acetate-induced apoptosis. Eur. J. Biochem. 250, 7-18
    • (1997) Eur. J. Biochem. , vol.250 , pp. 7-18
    • Mizuno, K.1    Noda, K.2    Araki, T.3    Imaoka, T.4    Kobayashi, Y.5    Akita, Y.6    Shimonaka, M.7    Kishi, S.8    Ohno, S.9
  • 80
    • 0032578393 scopus 로고    scopus 로고
    • Proteolytic activation of PKN by caspase-3 or related protease during apoptosis
    • Takahashi, M., Mukai, H., Toshimori, M., Miyamoto, M., and Ono, Y. (1998) Proteolytic activation of PKN by caspase-3 or related protease during apoptosis. Proc. Natl. Acad. Sci. USA 95, 11566-11571
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11566-11571
    • Takahashi, M.1    Mukai, H.2    Toshimori, M.3    Miyamoto, M.4    Ono, Y.5
  • 83
    • 0039765390 scopus 로고    scopus 로고
    • Involvement of protein kinase Cδ (PKCδ) in phorbol ester-induced apoptosis in LNCaP prostate cancer cells. Lack of proteolytic cleavage of PKCδ
    • Fujii, T., Garcia-Bermejo, M.L., Bernabo, J.L., Caamano, J., Ohba, M., Kuroki, T., Li, L., Yuspa, S.H., and Kazanietz, M.G. (2000) Involvement of protein kinase Cδ (PKCδ) in phorbol ester-induced apoptosis in LNCaP prostate cancer cells. Lack of proteolytic cleavage of PKCδ. J. Biol. Chem. 275, 7574-7582
    • (2000) J. Biol. Chem. , vol.275 , pp. 7574-7582
    • Fujii, T.1    Garcia-Bermejo, M.L.2    Bernabo, J.L.3    Caamano, J.4    Ohba, M.5    Kuroki, T.6    Li, L.7    Yuspa, S.H.8    Kazanietz, M.G.9
  • 84
    • 0031907117 scopus 로고    scopus 로고
    • Activation of protein kinase C triggers its ubiquitination and degradation
    • Lu, Z., Liu, D., Hornia, A., Devonish, W., Pagano, M., and Foster, D.A. (1998) Activation of protein kinase C triggers its ubiquitination and degradation. Mol. Cell. Biol. 18, 839-845
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 839-845
    • Lu, Z.1    Liu, D.2    Hornia, A.3    Devonish, W.4    Pagano, M.5    Foster, D.A.6
  • 86
    • 0032491318 scopus 로고    scopus 로고
    • Protein kinase Cδ is activated by caspase-dependent proteolysis during ultraviolet radiation-induced apoptosis of human keratinocytes
    • Denning, M.F., Wang, Y., Nickoloff, B.J., and Wrone-Smith, T. (1998) Protein kinase Cδ is activated by caspase-dependent proteolysis during ultraviolet radiation-induced apoptosis of human keratinocytes. J. Biol. Chem. 273, 29995-30002
    • (1998) J. Biol. Chem. , vol.273 , pp. 29995-30002
    • Denning, M.F.1    Wang, Y.2    Nickoloff, B.J.3    Wrone-Smith, T.4
  • 87
    • 0028144758 scopus 로고
    • Close similarity of baculovirus-expressed n-chimaerin and protein kinase Cα as phorbol ester receptors
    • Areces, L.B., Kazanietz, M.G., and Blumberg, P.M. (1994) Close similarity of baculovirus-expressed n-chimaerin and protein kinase Cα as phorbol ester receptors. J. Biol. Chem. 269, 19553-19558
    • (1994) J. Biol. Chem. , vol.269 , pp. 19553-19558
    • Areces, L.B.1    Kazanietz, M.G.2    Blumberg, P.M.3
  • 90
    • 0025733712 scopus 로고
    • Activation of the PKC-isotypes α, β1, γ, δ and ε by phorbol esters of different biological activities
    • Ryves, W.J., Evans, A.T., Olivier, A.R., Parker, P.J., and Evans, F.J. (1991) Activation of the PKC-isotypes α, β1, γ, δ and ε by phorbol esters of different biological activities. FEBS Lett. 288, 5-9
    • (1991) FEBS Lett. , vol.288 , pp. 5-9
    • Ryves, W.J.1    Evans, A.T.2    Olivier, A.R.3    Parker, P.J.4    Evans, F.J.5
  • 91
    • 0028126624 scopus 로고
    • Bryostatin 1 protects protein kinase C-δ from down-regulation in mouse keratinocytes in parallel with its inhibition of phorbol ester-induced differentiation
    • Szallasi, Z., Denning, M.F., Smith, C.B., Dlugosz, A.A., Yuspa, S.H., Pettit, G.R., and Blumberg, P.M. (1994) Bryostatin 1 protects protein kinase C-δ from down-regulation in mouse keratinocytes in parallel with its inhibition of phorbol ester-induced differentiation. Mol. Pharmacol. 46, 840-850
    • (1994) Mol. Pharmacol. , vol.46 , pp. 840-850
    • Szallasi, Z.1    Denning, M.F.2    Smith, C.B.3    Dlugosz, A.A.4    Yuspa, S.H.5    Pettit, G.R.6    Blumberg, P.M.7
  • 92
    • 0029153047 scopus 로고
    • Loss of protein kinase Cδ from human HaCaT keratinocytes upon ras transfection is mediated by TGFa
    • Geiges, D., Marks, F., and Gschwendt, M. (1995) Loss of protein kinase Cδ from human HaCaT keratinocytes upon ras transfection is mediated by TGFa. Exp. Cell Res. 219, 299-303
    • (1995) Exp. Cell Res. , vol.219 , pp. 299-303
    • Geiges, D.1    Marks, F.2    Gschwendt, M.3
  • 94
    • 0032515055 scopus 로고    scopus 로고
    • Protein kinase Cδ (PKCδ) inhibits the expression of glutamine synthetase in glial cells via the PKCδ regulatory domain and its tyrosine phosphorylation
    • Brodie, C., Bogi, K., Acs, P., Lorenzo, P.S., Baskin, L., and Blumberg, P.M. (1998) Protein kinase Cδ (PKCδ) inhibits the expression of glutamine synthetase in glial cells via the PKCδ regulatory domain and its tyrosine phosphorylation. J. Biol. Chem. 273, 30713-30718
    • (1998) J. Biol. Chem. , vol.273 , pp. 30713-30718
    • Brodie, C.1    Bogi, K.2    Acs, P.3    Lorenzo, P.S.4    Baskin, L.5    Blumberg, P.M.6
  • 95
    • 0035939845 scopus 로고    scopus 로고
    • Involvement of protein kinase Cδ in contact-dependent inhibition of growth in human and murine fibroblasts
    • Heit, I., Wieser, R.J,. Herget, T., Faust, D., Borchert-Stuhltrager, M., Oesch, F., and Dietrich, C. (2001) Involvement of protein kinase Cδ in contact-dependent inhibition of growth in human and murine fibroblasts. Oncogene 20, 5143-5154
    • (2001) Oncogene , vol.20 , pp. 5143-5154
    • Heit, I.1    Wieser, R.J.2    Herget, T.3    Faust, D.4    Borchert-Stuhltrager, M.5    Oesch, F.6    Dietrich, C.7
  • 96
    • 0033591714 scopus 로고    scopus 로고
    • Selective binding of bryostatin analogues to the cysteine rich domains of protein kinase C isozymes
    • Wender, P.A., Lippa, B., Park, C.M., Irie, K., Nakahara, A., and Ohigashi, H. (1999) Selective binding of bryostatin analogues to the cysteine rich domains of protein kinase C isozymes. Bioorg. Med. Chem. Lett. 9, 1687-1690
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 1687-1690
    • Wender, P.A.1    Lippa, B.2    Park, C.M.3    Irie, K.4    Nakahara, A.5    Ohigashi, H.6
  • 97
    • 0029622973 scopus 로고
    • Antisense oligodeoxynucleotide inhibition of δ protein kinase C expression accelerates induced differentiation of murine erythroleukaemia cells
    • Pessino, A., Passalacqua, M., Sparatore, B., Patrone, M., Melloni, E., and Pontremoli, S. (1995) Antisense oligodeoxynucleotide inhibition of δ protein kinase C expression accelerates induced differentiation of murine erythroleukaemia cells. Biochem. J. 312, 549-554
    • (1995) Biochem. J. , vol.312 , pp. 549-554
    • Pessino, A.1    Passalacqua, M.2    Sparatore, B.3    Patrone, M.4    Melloni, E.5    Pontremoli, S.6
  • 98
    • 0030707893 scopus 로고    scopus 로고
    • Antisense oligodeoxynucleotide to PKC-δ blocks α1-adrenergic activation of Na-K-2Cl cotransport
    • Liedtke, C.M., and Cole, T. (1997) Antisense oligodeoxynucleotide to PKC-δ blocks α1-adrenergic activation of Na-K-2Cl cotransport. Am. J. Physiol. 273, C1632-C1640
    • (1997) Am. J. Physiol. , vol.273 , pp. C1632-C1640
    • Liedtke, C.M.1    Cole, T.2
  • 99
    • 0033957772 scopus 로고    scopus 로고
    • PKC signaling in CF/T43 cell line: Regulation of NKCC1 by PKC-δ isotype
    • Liedtke, C.M., and Cole, T.S. (2000) PKC signaling in CF/T43 cell line: regulation of NKCC1 by PKC-δ isotype. Biochim. Biophys. Acta 1495, 24-33
    • (2000) Biochim. Biophys. Acta , vol.1495 , pp. 24-33
    • Liedtke, C.M.1    Cole, T.S.2
  • 100
    • 0030941373 scopus 로고    scopus 로고
    • Growth hormone and phorbol esters require specific protein kinase C isoforms to activate mitogen-activated protein kinases in 3T3-F442A cells
    • MacKenzie, S., Fleming, I., Houslay, M.D., Anderson, N.G., and Kilgour, E. (1997) Growth hormone and phorbol esters require specific protein kinase C isoforms to activate mitogen-activated protein kinases in 3T3-F442A cells. Biochem. J. 324, 159-615
    • (1997) Biochem. J. , vol.324 , pp. 159-615
    • MacKenzie, S.1    Fleming, I.2    Houslay, M.D.3    Anderson, N.G.4    Kilgour, E.5
  • 101
    • 0032403566 scopus 로고    scopus 로고
    • Antisense oligonucleotides targeting protein kinase C-α, -βI, or -δ but not -η inhibit lipopolysaccharide-induced nitric oxide synthase expression in RAW 264.7 macrophages: Involvement of a nuclear factor κB-dependent mechanism
    • Chen, C.C., Wang, J.K., and Lin, S.B. (1998) Antisense oligonucleotides targeting protein kinase C-α, -βI, or -δ but not -η inhibit lipopolysaccharide-induced nitric oxide synthase expression in RAW 264.7 macrophages: involvement of a nuclear factor κB-dependent mechanism. J. Immunol. 161, 6206-6214
    • (1998) J. Immunol. , vol.161 , pp. 6206-6214
    • Chen, C.C.1    Wang, J.K.2    Lin, S.B.3
  • 102
    • 0035976925 scopus 로고    scopus 로고
    • Activation and mitochondrial translocation of protein kinase Cδ are necessary for insulin stimulation of pyruvate dehydrogenase complex activity in muscle and liver cells
    • Caruso, M., Maitan, M.A., Bifulco, G., Miele, C., Vigliotta, G., Oriente, F., Formisano, P., and Beguinot, F. (2001) Activation and mitochondrial translocation of protein kinase Cδ are necessary for insulin stimulation of pyruvate dehydrogenase complex activity in muscle and liver cells. J. Biol. Chem. 276, 45088-45097
    • (2001) J. Biol. Chem. , vol.276 , pp. 45088-45097
    • Caruso, M.1    Maitan, M.A.2    Bifulco, G.3    Miele, C.4    Vigliotta, G.5    Oriente, F.6    Formisano, P.7    Beguinot, F.8
  • 104
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S.P., Reddy, H., Caivano, M., and Cohen, P. (2000) Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351, 95-105
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 105
    • 0035851112 scopus 로고    scopus 로고
    • Rottlerin is a mitochondrial uncoupler that decreases cellular ATP levels and indirectly blocks protein kinase Cδ tyrosine phosphorylation
    • Soltoff, S.P. (2001) Rottlerin is a mitochondrial uncoupler that decreases cellular ATP levels and indirectly blocks protein kinase Cδ tyrosine phosphorylation. J. Biol. Chem. 276, 37986-37992
    • (2001) J. Biol. Chem. , vol.276 , pp. 37986-37992
    • Soltoff, S.P.1
  • 106
    • 0034892413 scopus 로고    scopus 로고
    • Rottlerin-independent attenuation of pervanadate-induced tyrosine phosphorylation events by protein kinase C-δ in hemopoietic cells
    • Leitges, M., Elis, W., Gimborn, K., and Huber, M. (2001) Rottlerin-independent attenuation of pervanadate-induced tyrosine phosphorylation events by protein kinase C-δ in hemopoietic cells. Lab. Invest. 81, 1087-1095
    • (2001) Lab. Invest. , vol.81 , pp. 1087-1095
    • Leitges, M.1    Elis, W.2    Gimborn, K.3    Huber, M.4
  • 109
    • 0027418816 scopus 로고
    • Overexpression of protein kinase C-δ and -ε in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity
    • Mischak, H., Goodnight, J., Kolch, W., Martiny-Baron, G., Schaechtle, C., Kazanietz, M.G., Blumberg, P.M., Pierce, J.H., and Mushinski, J.F. (1993) Overexpression of protein kinase C-δ and -ε in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity. J. Biol. Chem. 268, 6090-6096
    • (1993) J. Biol. Chem. , vol.268 , pp. 6090-6096
    • Mischak, H.1    Goodnight, J.2    Kolch, W.3    Martiny-Baron, G.4    Schaechtle, C.5    Kazanietz, M.G.6    Blumberg, P.M.7    Pierce, J.H.8    Mushinski, J.F.9
  • 110
    • 0027292678 scopus 로고
    • Phorbol ester-induced myeloid differentiation is mediated by protein kinase C-α and -δ and not by protein kinase C-βII, -ε, -ζ, and -η
    • Mischak, H., Pierce, J.H., Goodnight, J., Kazanietz, M.G., Blumberg, P.M., and Mushinski, J.F. (1993) Phorbol ester-induced myeloid differentiation is mediated by protein kinase C-α and -δ and not by protein kinase C-βII, -ε, -ζ, and -η. J. Biol. Chem. 268, 20110-20115
    • (1993) J. Biol. Chem. , vol.268 , pp. 20110-20115
    • Mischak, H.1    Pierce, J.H.2    Goodnight, J.3    Kazanietz, M.G.4    Blumberg, P.M.5    Mushinski, J.F.6
  • 111
    • 0030973402 scopus 로고    scopus 로고
    • Protein kinase Cδ inhibits the proliferation of vascular smooth muscle cells by suppressing G1 cyclin expression
    • Fukumoto, S., Nishizawa, Y., Hosoi, M., Koyama, H., Yamakawa, K., Ohno, S., and Morii, H. (1997) Protein kinase Cδ inhibits the proliferation of vascular smooth muscle cells by suppressing G1 cyclin expression. J. Biol. Chem. 272, 13816-13822
    • (1997) J. Biol. Chem. , vol.272 , pp. 13816-13822
    • Fukumoto, S.1    Nishizawa, Y.2    Hosoi, M.3    Koyama, H.4    Yamakawa, K.5    Ohno, S.6    Morii, H.7
  • 112
    • 0031001002 scopus 로고    scopus 로고
    • Enhancement of migration by protein kinase Cα and inhibition of proliferation and cell cycle progression by protein kinase Cδ in capillary endothelial cells
    • Harrington, E.O., Loffler, J., Nelson, P.R., Kent, K.C., Simons, M., and Ware, J.A. (1997) Enhancement of migration by protein kinase Cα and inhibition of proliferation and cell cycle progression by protein kinase Cδ in capillary endothelial cells. J. Biol. Chem. 272, 7390-7397
    • (1997) J. Biol. Chem. , vol.272 , pp. 7390-7397
    • Harrington, E.O.1    Loffler, J.2    Nelson, P.R.3    Kent, K.C.4    Simons, M.5    Ware, J.A.6
  • 113
    • 0031813150 scopus 로고    scopus 로고
    • Induction of differentiation in normal human keratinocytes by adenovirus-mediated introduction of the ε and δ isoforms of protein kinase C
    • Ohba, M., Ishino, K., Kashiwagi, M., Kawabe, S., Chida, K., Huh, N.H., and Kuroki, T. (1998) Induction of differentiation in normal human keratinocytes by adenovirus-mediated introduction of the ε and δ isoforms of protein kinase C. Mol. Cell. Biol. 18, 5199-5207
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5199-5207
    • Ohba, M.1    Ishino, K.2    Kashiwagi, M.3    Kawabe, S.4    Chida, K.5    Huh, N.H.6    Kuroki, T.7
  • 114
    • 0033581954 scopus 로고    scopus 로고
    • Increased protein kinase Cδ in mammary tumor cells: Relationship to transformtion and metastatic progression
    • Kiley, S.C., Clark, K.J., Duddy, S.K., Welch, D.R., and Jaken, S. (1999) Increased protein kinase Cδ in mammary tumor cells: relationship to transformtion and metastatic progression. Oncogene 18, 6748-6757
    • (1999) Oncogene , vol.18 , pp. 6748-6757
    • Kiley, S.C.1    Clark, K.J.2    Duddy, S.K.3    Welch, D.R.4    Jaken, S.5
  • 115
    • 0028243504 scopus 로고
    • Ras-dependent signal transduction is indispensable but not sufficient for the activation of AP1/Jun by PKCδ
    • Hirai, S., Izumi, Y, Higa, K., Kaibuchi, K., Mizuno, K., Osada, S., Suzuki, K., and Ohno, S. (1994) Ras-dependent signal transduction is indispensable but not sufficient for the activation of AP1/Jun by PKCδ. EMBO J. 13, 2331-2340
    • (1994) EMBO J. , vol.13 , pp. 2331-2340
    • Hirai, S.1    Izumi, Y.2    Higa, K.3    Kaibuchi, K.4    Mizuno, K.5    Osada, S.6    Suzuki, K.7    Ohno, S.8
  • 116
    • 0028905280 scopus 로고
    • Characterization of a protein kinase C-δ (PKC-δ) ATP binding mutant. An inactive enzyme that competitively inhibits wild type PKC-δ enzymatic activity
    • Li, W., Yu, J.C., Shin, D.Y., and Pierce, J.H. (1995) Characterization of a protein kinase C-δ (PKC-δ) ATP binding mutant. An inactive enzyme that competitively inhibits wild type PKC-δ enzymatic activity. J. Biol. Chem. 270, 8311-8318
    • (1995) J. Biol. Chem. , vol.270 , pp. 8311-8318
    • Li, W.1    Yu, J.C.2    Shin, D.Y.3    Pierce, J.H.4
  • 117
    • 0345129995 scopus 로고    scopus 로고
    • Novel roles of specific isoforms of protein kinase C in activation of the c-fos serum response element
    • Soh, J.W., Lee, E.H., Prywes, R., and Weinstein, I.B. (1999) Novel roles of specific isoforms of protein kinase C in activation of the c-fos serum response element. Mol. Cell. Biol. 19, 1313-1324
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1313-1324
    • Soh, J.W.1    Lee, E.H.2    Prywes, R.3    Weinstein, I.B.4
  • 118
    • 0031455382 scopus 로고    scopus 로고
    • The catalytic domain of protein kinase Cδ confers protection from down-regulation induced by bryostatin 1
    • Lorenzo, P.S., Bogi, K., Acs, P., Pettit, G.R., and Blumberg, P.M. (1997) The catalytic domain of protein kinase Cδ confers protection from down-regulation induced by bryostatin 1. J. Biol. Chem. 272, 33338-33343
    • (1997) J. Biol. Chem. , vol.272 , pp. 33338-33343
    • Lorenzo, P.S.1    Bogi, K.2    Acs, P.3    Pettit, G.R.4    Blumberg, P.M.5
  • 119
    • 0031033047 scopus 로고    scopus 로고
    • The catalytic domain of protein kinase C-δ in reciprocal δ and ε chimeras mediates phorbol ester-induced macrophage differentiation of mouse promyelocytes
    • Wang, Q.J., Acs, P., Goodnight, J., Giese, T., Blumberg, P.M., Mischak, H., and Mushinski, J.F. (1997) The catalytic domain of protein kinase C-δ in reciprocal δ and ε chimeras mediates phorbol ester-induced macrophage differentiation of mouse promyelocytes. J. Biol. Chem. 272, 76-82
    • (1997) J. Biol. Chem. , vol.272 , pp. 76-82
    • Wang, Q.J.1    Acs, P.2    Goodnight, J.3    Giese, T.4    Blumberg, P.M.5    Mischak, H.6    Mushinski, J.F.7
  • 120
    • 1842404211 scopus 로고    scopus 로고
    • Both the catalytic and regulatory domains of protein kinase C chimeras modulate the proliferative properties of NIH 3T3 cells
    • Acs, P., Wang, Q.J., Bogi, K., Marquez, A.M., Lorenzo, P.S., Biro, T., Szallasi, Z., Mushinski, J.F., and Blumberg P.M. (1997) Both the catalytic and regulatory domains of protein kinase C chimeras modulate the proliferative properties of NIH 3T3 cells. J. Biol. Chem. 272, 28793-28799
    • (1997) J. Biol. Chem. , vol.272 , pp. 28793-28799
    • Acs, P.1    Wang, Q.J.2    Bogi, K.3    Marquez, A.M.4    Lorenzo, P.S.5    Biro, T.6    Szallasi, Z.7    Mushinski, J.F.8    Blumberg, P.M.9
  • 121
    • 0033571747 scopus 로고    scopus 로고
    • Transgenic mice overexpressing protein kinase Cδ in the epidermis are resistant to skin tumor promotion by 12-O-tetrade-canoylphorbol-13-acetate
    • Reddig, P.J., Dreckschmidt, N.E., Ahrens, H., Simsiman, R., Tseng, C.P., Zou, J., Oberley, T.D., and Verma, A.K. (1999) Transgenic mice overexpressing protein kinase Cδ in the epidermis are resistant to skin tumor promotion by 12-O-tetrade-canoylphorbol-13-acetate. Cancer Res. 59, 5710-5718
    • (1999) Cancer Res. , vol.59 , pp. 5710-5718
    • Reddig, P.J.1    Dreckschmidt, N.E.2    Ahrens, H.3    Simsiman, R.4    Tseng, C.P.5    Zou, J.6    Oberley, T.D.7    Verma, A.K.8
  • 122
    • 0037118587 scopus 로고    scopus 로고
    • Protein kinase Cδ-mediated signal to ornithine decarboxylase induction is independent of skin tumor suppression
    • Wheeler, D.L., Reddig, P.J., Dreckschmidt, N.E., Leitges, M., and Verma, A.K. (2001) Protein kinase Cδ-mediated signal to ornithine decarboxylase induction is independent of skin tumor suppression. Oncogene 21, 3620-3630
    • (2001) Oncogene , vol.21 , pp. 3620-3630
    • Wheeler, D.L.1    Reddig, P.J.2    Dreckschmidt, N.E.3    Leitges, M.4    Verma, A.K.5
  • 124
    • 0037171439 scopus 로고    scopus 로고
    • Protein kinase C-δ controls self-antigen-induced B-cell tolerance
    • Mecklenbrauker, I., Saijo, K., Zheng, N.Y., Leitges, M., and Tarakhovsky, A. (2002) Protein kinase C-δ controls self-antigen-induced B-cell tolerance. Nature 416, 860-865
    • (2002) Nature , vol.416 , pp. 860-865
    • Mecklenbrauker, I.1    Saijo, K.2    Zheng, N.Y.3    Leitges, M.4    Tarakhovsky, A.5
  • 127
    • 0032745244 scopus 로고    scopus 로고
    • Antagonistic effects of protein kinase Cα and δ on both transformation and phospholipase D activity mediated by the epidermal growth factor receptor
    • Hornia, A,. Lu, Z., Sukezane, T., Zhong, M., Joseph, T., Frankel, P., and Foster, D.A. (1999) Antagonistic effects of protein kinase Cα and δ on both transformation and phospholipase D activity mediated by the epidermal growth factor receptor. Mol. Cell. Biol. 19, 7672-8760
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7672-8760
    • Hornia, A.1    Lu, Z.2    Sukezane, T.3    Zhong, M.4    Joseph, T.5    Frankel, P.6    Foster, D.A.7
  • 128
    • 0033521742 scopus 로고    scopus 로고
    • PKCδ acts as a growth and tumor suppressor in rat colonic epithelial cells
    • Perletti, G.P., Marras, E., Concari, P., Piccinini, F., and Tashjian, A. H., Jr. (1999) PKCδ acts as a growth and tumor suppressor in rat colonic epithelial cells. Oncogene 18, 1251-1256
    • (1999) Oncogene , vol.18 , pp. 1251-1256
    • Perletti, G.P.1    Marras, E.2    Concari, P.3    Piccinini, F.4    Tashjian, A.H.5
  • 129
  • 130
    • 0033516666 scopus 로고    scopus 로고
    • Protein kinase Cδ is essential for etoposide-induced apoptosis in salivary gland acinar cells
    • Reyland, M.E., Anderson, S.M., Matassa, A.A., Barzen, K.A., and Quissell, D.O. (1999) Protein kinase Cδ is essential for etoposide-induced apoptosis in salivary gland acinar cells. J. Biol. Chem. 274, 19115-19123
    • (1999) J. Biol. Chem. , vol.274 , pp. 19115-19123
    • Reyland, M.E.1    Anderson, S.M.2    Matassa, A.A.3    Barzen, K.A.4    Quissell, D.O.5
  • 132
    • 0037034186 scopus 로고    scopus 로고
    • Downregulating PKCδ provides a PI3K/Akt-independent survival signal that overcomes apoptotic signals generated by c-Src overexpression
    • Zhong, M., Lu, Z., and Foster, D.A. (2002) Downregulating PKCδ provides a PI3K/Akt-independent survival signal that overcomes apoptotic signals generated by c-Src overexpression. Oncogene 21, 1071-1078
    • (2002) Oncogene , vol.21 , pp. 1071-1078
    • Zhong, M.1    Lu, Z.2    Foster, D.A.3
  • 133
    • 0033233483 scopus 로고    scopus 로고
    • Protein kinase Cδ targets mitochondria, alters mitochondrial membrane potential, and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector
    • Li, L., Lorenzo, P.S., Bogi, K., Blumberg, P.M., and Yuspa, S.H. (1999) Protein kinase Cδ targets mitochondria, alters mitochondrial membrane potential, and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector. Mol. Cell. Biol. 19, 8547-8558
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8547-8558
    • Li, L.1    Lorenzo, P.S.2    Bogi, K.3    Blumberg, P.M.4    Yuspa, S.H.5
  • 134
    • 0034698182 scopus 로고    scopus 로고
    • Mitochondrial translocation of protein kinase Cδ in phorbol ester-induced cytochrome c release and apoptosis
    • Majumder, P.K., Pandey, P., Sun, X., Cheng, K., Datta, R., Saxena, S., Kharbanda, S., and Kufe, D. (2000) Mitochondrial translocation of protein kinase Cδ in phorbol ester-induced cytochrome c release and apoptosis. J. Biol. Chem. 275, 21793-21796
    • (2000) J. Biol. Chem. , vol.275 , pp. 21793-21796
    • Majumder, P.K.1    Pandey, P.2    Sun, X.3    Cheng, K.4    Datta, R.5    Saxena, S.6    Kharbanda, S.7    Kufe, D.8
  • 135
    • 0029031232 scopus 로고
    • Selective translocation of protein kinase C-δ in PC12 cells during nerve growth factor-induced neuritogenesis
    • O'Driscoll, K.R., Teng, K.K., Fabbro, D., Greene, L.A., and Weinstein, I.B. (1995) Selective translocation of protein kinase C-δ in PC12 cells during nerve growth factor-induced neuritogenesis. Mol. Biol. Cell 6, 449-458
    • (1995) Mol. Biol. Cell , vol.6 , pp. 449-458
    • O’Driscoll, K.R.1    Teng, K.K.2    Fabbro, D.3    Greene, L.A.4    Weinstein, I.B.5
  • 136
    • 0032588943 scopus 로고    scopus 로고
    • Protein kinase Cδ mediates neurogenic but not mitogenic activation of mitogen-activated protein kinase in neuronal cells
    • Corbit, K.C., Foster, D.A., and Rosner, M.R. (1999) Protein kinase Cδ mediates neurogenic but not mitogenic activation of mitogen-activated protein kinase in neuronal cells. Mol. Cell. Biol. 19, 4209-4218
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4209-4218
    • Corbit, K.C.1    Foster, D.A.2    Rosner, M.R.3
  • 137
    • 17444373968 scopus 로고    scopus 로고
    • A metalloprotease-disintegrin, MDC9/meltrin-γ/ADAM9 and PKCδ are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor
    • Izumi, Y., Hirata, M., Hasuwa, H., Iwamoto, R., Umata, T., Miyado, K., Tamai, Y., Kurisaki, T., Sehara-Fujisawa, A., Ohno, S., and Mekada, E. (1998) A metalloprotease-disintegrin, MDC9/meltrin-γ/ADAM9 and PKCδ are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. EMBO J. 17, 7260-7272
    • (1998) EMBO J. , vol.17 , pp. 7260-7272
    • Izumi, Y.1    Hirata, M.2    Hasuwa, H.3    Iwamoto, R.4    Umata, T.5    Miyado, K.6    Tamai, Y.7    Kurisaki, T.8    Sehara-Fujisawa, A.9    Ohno, S.10    Mekada, E.11
  • 138
    • 0035913886 scopus 로고    scopus 로고
    • PKCδ and ζ mediate IL-4/IL-13-induced germline ε transcription in human B cells: A putative regulation via PU.1 phosphorylation
    • Ikizawa, K., Kajiwara, K., Izuhara, K., and Yanagihara Y. (2001) PKCδ and ζ mediate IL-4/IL-13-induced germline ε transcription in human B cells: a putative regulation via PU.1 phosphorylation. Biochem. Biophys. Res. Commun. 288, 34-41
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 34-41
    • Ikizawa, K.1    Kajiwara, K.2    Izuhara, K.3    Yanagihara, Y.4
  • 139
    • 0029789967 scopus 로고    scopus 로고
    • Protein kinase Cδ activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf
    • Ueda, Y., Hirai, S., Osada, S., Suzuki, A., Mizuno, K., and Ohno, S. (1996) Protein kinase Cδ activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf J. Biol. Chem. 271, 23512-23519
    • (1996) J. Biol. Chem. , vol.271 , pp. 23512-23519
    • Ueda, Y.1    Hirai, S.2    Osada, S.3    Suzuki, A.4    Mizuno, K.5    Ohno, S.6
  • 140
    • 0033974993 scopus 로고    scopus 로고
    • Hyperosmolality induces activation of cPKC and nPKC, a requirement for ERK1/2 activation in NIH/3T3 cells
    • Zhuang, S., Hirai, S.I., and Ohno, S. (2000) Hyperosmolality induces activation of cPKC and nPKC, a requirement for ERK1/2 activation in NIH/3T3 cells. Am. J. Physiol. 278, C102-C109
    • (2000) Am. J. Physiol. , vol.278 , pp. C102-C109
    • Zhuang, S.1    Hirai, S.I.2    Ohno, S.3
  • 141
    • 0034644683 scopus 로고    scopus 로고
    • Phorbol ester-induced expression of airway squamous cell differentiation marker, SPRR1B, is regulated by protein kinase Cδ/Ras/MEKK1/MKK1-dependent/AP-1 signal transduction pathway
    • Vuong, H., Patterson, T., Shapiro, P., Kalvakolanu, D.V., Wu, R., Ma, W.Y., Dong, Z., Kleeberger, S.R., and Reddy, S.P.M. (2000) Phorbol ester-induced expression of airway squamous cell differentiation marker, SPRR1B, is regulated by protein kinase Cδ/Ras/MEKK1/MKK1-dependent/AP-1 signal transduction pathway. J. Biol. Chem. 275, 32250-32259
    • (2000) J. Biol. Chem. , vol.275 , pp. 32250-32259
    • Vuong, H.1    Patterson, T.2    Shapiro, P.3    Kalvakolanu, D.V.4    Wu, R.5    Ma, W.Y.6    Dong, Z.7    Kleeberger, S.R.8    Reddy, S.P.M.9
  • 142
    • 0035931889 scopus 로고    scopus 로고
    • PKCδ mediates ionizing radiation-induced activation of c-Jun NH2-terminal kinase through MKK7 in human thyroid cells
    • Mitsutake, N., Namba, H., Shklyaev, S.S., Tsukazaki, T., Ohtsuru, A., Ohba, M., Kuroki, T., Ayabe, H., and Yamashita, S. (2001) PKCδ mediates ionizing radiation-induced activation of c-Jun NH2-terminal kinase through MKK7 in human thyroid cells. Oncogene 20, 989-996
    • (2001) Oncogene , vol.20 , pp. 989-996
    • Mitsutake, N.1    Namba, H.2    Shklyaev, S.S.3    Tsukazaki, T.4    Ohtsuru, A.5    Ohba, M.6    Kuroki, T.7    Ayabe, H.8    Yamashita, S.9
  • 143
    • 0034680916 scopus 로고    scopus 로고
    • DIK, a novel protein kinase that interacts with protein kinase Cδ. Cloning, characterization, and gene analysis
    • Bähr, C., Rohwer, A., Stempka, L., Rincke, G., Marks, F., and Gschwendt, M. (2000) DIK, a novel protein kinase that interacts with protein kinase Cδ. Cloning, characterization, and gene analysis. J. Biol. Chem. 275, 36350-3635
    • (2000) J. Biol. Chem. , vol.275 , pp. 36350-43635
    • Bähr, C.1    Rohwer, A.2    Stempka, L.3    Rincke, G.4    Marks, F.5    Gschwendt, M.6
  • 144
    • 0029879571 scopus 로고    scopus 로고
    • Differential effects of overexpression of PKCα and PKCδ/ε on cellular E2F activity in late G1 phase
    • Nakaigawa, N., Hirai, S., Mizuno, K., Shuin, T., Hosaka, M., and Ohno, S. (1996) Differential effects of overexpression of PKCα and PKCδ/ε on cellular E2F activity in late G1 phase. Biochem. Biophys. Res. Commun. 222, 95-100
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 95-100
    • Nakaigawa, N.1    Hirai, S.2    Mizuno, K.3    Shuin, T.4    Hosaka, M.5    Ohno, S.6
  • 145
    • 0032437519 scopus 로고    scopus 로고
    • Phorbol ester-induced G1 arrest in BALB/MK-2 mouse keratinocytes is mediated by δ and η isoforms of protein kinase C
    • Ishino, K., Ohba, M., Kashiwagi, M., Kawabe, S., Chida, K., and Kuroki, T. (1998) Phorbol ester-induced G1 arrest in BALB/MK-2 mouse keratinocytes is mediated by δ and η isoforms of protein kinase C. Jpn. J. Cancer Res. 89, 1126-1133
    • (1998) Jpn. J. Cancer Res. , vol.89 , pp. 1126-1133
    • Ishino, K.1    Ohba, M.2    Kashiwagi, M.3    Kawabe, S.4    Chida, K.5    Kuroki, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.