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Volumn 249, Issue 1, 1997, Pages 156-160

Phorbol-ester-activated protein kinase C-α lacking phosphorylation at Ser657 is down-regulated by a mechanism involving dephosphorylation

Author keywords

Down regulated; Phorbol ester; Protein kinase C; Protein phosphorylation; Translocation

Indexed keywords

PHORBOL ESTER; PROTEIN KINASE C;

EID: 0030801605     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-2-00156.x     Document Type: Article
Times cited : (18)

References (32)
  • 1
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signalling for sustained cellular responses
    • Nishizuka, Y. (1995) Protein kinase C and lipid signalling for sustained cellular responses, FASEB J. 9, 484-496.
    • (1995) FASEB J. , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 2
    • 0025305538 scopus 로고
    • Protein kinase C pseudosubstrate prototype: Structure-function relationship
    • House, C. & Kemp, B. E. (1990) Protein kinase C pseudosubstrate prototype: structure-function relationship, Cell. Signal. 2, 187-190.
    • (1990) Cell. Signal. , vol.2 , pp. 187-190
    • House, C.1    Kemp, B.E.2
  • 3
    • 0025198526 scopus 로고
    • Mutagenesis of the pseudosubstrate site of PKC leads to activation
    • Pears, C. J., Kour, G., House, C., Kemp, B. E. & Parker, P. J. (1990) Mutagenesis of the pseudosubstrate site of PKC leads to activation, Eur. J. Biochem. 194, 89-94.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 89-94
    • Pears, C.J.1    Kour, G.2    House, C.3    Kemp, B.E.4    Parker, P.J.5
  • 4
    • 0027999633 scopus 로고
    • Requirement for negative charge on 'activation loop' of protein kinase C
    • Orr, J. W. & 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
  • 6
    • 0024340030 scopus 로고
    • Biosynthesis and posttranslational modifications of protein kinase C in human breast cancer cells
    • Borner, C., Filipuzzi, I., Wartmann, M., Eppenberger, U. & Fabbro, D. (1989) Biosynthesis and posttranslational modifications of protein kinase C in human breast cancer cells, J. Biol. Chem. 264, 13902-13909.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13902-13909
    • Borner, C.1    Filipuzzi, I.2    Wartmann, M.3    Eppenberger, U.4    Fabbro, D.5
  • 7
    • 0024805642 scopus 로고
    • Expression of a functional protein kinase C-using a baculovirus vector: Purification and characterization of a single protein kinase C isozyme
    • Patel, G. & Stabel, S. (1989) Expression of a functional protein kinase C-(using a baculovirus vector: Purification and characterization of a single protein kinase C isozyme, Cellular Sign. 1, 227-240.
    • (1989) Cellular Sign. , vol.1 , pp. 227-240
    • Patel, G.1    Stabel, S.2
  • 8
    • 0026519372 scopus 로고
    • Studies on the phosphorylation of protein kinase C-α
    • Pears, C. J., Stabel, S., Cazaubon, S. & 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.J.1    Stabel, S.2    Cazaubon, S.3    Parker, P.J.4
  • 9
    • 0027174835 scopus 로고
    • Unphosphorylated α-PKC exhibits phorbol ester binding but lacks protein kinase activity in vitro
    • Filipuzzi, I., Fabbro, D. & Imber, R. (1993) Unphosphorylated α-PKC exhibits phorbol ester binding but lacks protein kinase activity in vitro, J. Cell. Biochem. 52, 78-83.
    • (1993) J. Cell. Biochem. , vol.52 , pp. 78-83
    • Filipuzzi, I.1    Fabbro, D.2    Imber, R.3
  • 10
    • 0028062105 scopus 로고
    • In vivo regulation of protein kinase C by transphosphorylation followed by autophosphorylation
    • Dutil, E. M., Keranen, L. M., DePaoli-Roach, A. A. & Newton, A. C. (1994) In vivo regulation of protein kinase C by transphosphorylation followed by autophosphorylation, J. Biol. Chem. 269, 29359-29362.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29359-29362
    • Dutil, E.M.1    Keranen, L.M.2    DePaoli-Roach, A.A.3    Newton, A.C.4
  • 11
    • 0028108027 scopus 로고
    • Thr-497 is a critical site for permissive activation of protein kinase C α
    • Cazaubon, S. M., Bornancin, F. & Parker, P. J. (1994) Thr-497 is a critical site for permissive activation of protein kinase C α, Biochem. J. 301, 443-448.
    • (1994) Biochem. J. , vol.301 , pp. 443-448
    • Cazaubon, S.M.1    Bornancin, F.2    Parker, P.J.3
  • 12
    • 0025004286 scopus 로고
    • Autophosphorylation of protein kinase C at three separated regions of its primary sequence
    • Flint, A. J., Paladini, R. D. & 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 Jr., D.E.3
  • 13
    • 0028168528 scopus 로고
    • Phosphorylation of Thr-642 is an early event in the processing of newly synthesized PKC-β1 and is essential for its activation
    • Zhang, J., Wang, L., Schwartz, J., Bond, R. W. & Bishop, W. R. (1994) Phosphorylation of Thr-642 is an early event in the processing of newly synthesized PKC-β1 and is essential for its activation, J. Biol. Chem. 269, 19578-19584.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19578-19584
    • Zhang, J.1    Wang, L.2    Schwartz, J.3    Bond, R.W.4    Bishop, W.R.5
  • 14
    • 0029615509 scopus 로고
    • PKC is regulated in vivo by three functionally distinct phosphorylations
    • Keranen, L. M., Dutil, E. M. & Newton, A. C. (1995) PKC is regulated in vivo by three functionally distinct phosphorylations, Curr. Biol. 5, 1393-1403.
    • (1995) Curr. Biol. , vol.5 , pp. 1393-1403
    • Keranen, L.M.1    Dutil, E.M.2    Newton, A.C.3
  • 17
    • 0030250879 scopus 로고    scopus 로고
    • Phosphorylation of Thr-638 critically controls the dephosphorylation and inactivation of PKC-α
    • Bornancin, F. & Parker, P. J. (1996) Phosphorylation of Thr-638 critically controls the dephosphorylation and inactivation of PKC-α, Curr. Biol. 9, 1114-1123.
    • (1996) Curr. Biol. , vol.9 , pp. 1114-1123
    • Bornancin, F.1    Parker, P.J.2
  • 18
    • 0029761426 scopus 로고    scopus 로고
    • Replacement of Ser657 of protein kinase C-α by alanine leads to premature down-regulation after phorbol-ester-induced translocation to the membrane
    • Gysin, S. & Imber, R. (1996) Replacement of Ser657 of protein kinase C-α by alanine leads to premature down-regulation after phorbol-ester-induced translocation to the membrane, Eur. J. Biochem. 240, 747-750.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 747-750
    • Gysin, S.1    Imber, R.2
  • 19
    • 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, 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
  • 21
    • 0021674863 scopus 로고
    • Construction and applications of a highly transmissible murine retrovirus shuttle vector
    • Cepko, C. L., Roberts, B. E. & Mulligan, R. C. (1984) Construction and applications of a highly transmissible murine retrovirus shuttle vector, Cell 37, 1053-1062.
    • (1984) Cell , vol.37 , pp. 1053-1062
    • Cepko, C.L.1    Roberts, B.E.2    Mulligan, R.C.3
  • 22
    • 0026097849 scopus 로고
    • Tumor-promoting phorbol ester and activated Ha-ras synergistically reduce the interleukin-3 requirement in a mast cell line
    • Imber, R. & Fabbro, D. (1991) Tumor-promoting phorbol ester and activated Ha-ras synergistically reduce the interleukin-3 requirement in a mast cell line, Cancer Res. 50, 632-638.
    • (1991) Cancer Res. , vol.50 , pp. 632-638
    • Imber, R.1    Fabbro, D.2
  • 23
    • 0017052382 scopus 로고
    • The origin and characteristics of a pig kidney cell strain, LLC-PK1
    • Hull, R. N., Cherry, W. R. & Weaver, G. W. (1976) The origin and characteristics of a pig kidney cell strain, LLC-PK1, In vitro 12, 670-677.
    • (1976) In Vitro , vol.12 , pp. 670-677
    • Hull, R.N.1    Cherry, W.R.2    Weaver, G.W.3
  • 24
    • 0026180277 scopus 로고
    • Overexpression of the α-type of protein kinase (PK) C in LLC-PK1 cells does not lead to a proportional increase in the induction of two 12-O-tetradecanoylphorbol-13-acetate-inducible genes
    • Wartmann, M., Jans, D. A., Parker, P. J., Nagamine, Y., Hemmings, B. A., Jaken, S., Eppenberger, U. & Fabbro, D. (1991) Overexpression of the α-type of protein kinase (PK) C in LLC-PK1 cells does not lead to a proportional increase in the induction of two 12-O-tetradecanoylphorbol-13-acetate-inducible genes, Cell Regul. 2, 491-502.
    • (1991) Cell Regul. , vol.2 , pp. 491-502
    • Wartmann, M.1    Jans, D.A.2    Parker, P.J.3    Nagamine, Y.4    Hemmings, B.A.5    Jaken, S.6    Eppenberger, U.7    Fabbro, D.8
  • 25
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications, Proc. Natl Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 27
    • 0022368131 scopus 로고
    • The cytosolic phorboid receptor correlates with hormone dependency in six mammary carcinoma cell lines
    • Costa, S. D., Fabbro, D., Regazzi, R., Küng, W. & Eppenberger, U. (1985) The cytosolic phorboid receptor correlates with hormone dependency in six mammary carcinoma cell lines, Biochem. Biophys. Res. Commun. 133, 814-822.
    • (1985) Biochem. Biophys. Res. Commun. , vol.133 , pp. 814-822
    • Costa, S.D.1    Fabbro, D.2    Regazzi, R.3    Küng, W.4    Eppenberger, U.5
  • 29
    • 15844387528 scopus 로고    scopus 로고
    • Ceramide inactivates cellular protein kinase Cα
    • Lee, J. Y., Hannun, Y. A. & Obeid, L. M. (1996) Ceramide inactivates cellular protein kinase Cα, J. Biol. Chem. 271, 13169-13174.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13169-13174
    • Lee, J.Y.1    Hannun, Y.A.2    Obeid, L.M.3
  • 32
    • 0030475207 scopus 로고    scopus 로고
    • 12-O-Tetradecanoylphorbol-13-acetate-induced dephosphorylation of protein kinase C-α correlates with the presence of a membrane-associated protein phosphatase 2A heterotrimer
    • Hansra, G., Bornancin, F., Whelan, R., Hemmings, B. A. & Parker, P. J. (1996) 12-O-Tetradecanoylphorbol-13-acetate-induced dephosphorylation of protein kinase C-α 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


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