메뉴 건너뛰기




Volumn 288, Issue 4, 2013, Pages 2805-2815

Mammalian target of rapamycin complex 1 (mTORC1) plays a role in pasteurella multocida toxin (PMT)-induced protein synthesis and proliferation in swiss 3T3 cells

Author keywords

[No Author keywords available]

Indexed keywords

CELL MIGRATION; COMPLEX 1; CONCENTRATION-DEPENDENT; DEAMIDATION; DIACYLGLYCEROL; EPIDERMAL GROWTH FACTOR RECEPTORS; G PROTEIN; INDUCED PROTEINS; KNOCK OUTS; MAMMALIAN TARGET; MITOGENIC PROPERTIES; MITOGENS; MTOR SIGNALING; PASTEURELLA MULTOCIDA TOXINS; PHORBOL 12 MYRISTATE 13 ACETATES; PROTEIN SYNTHESIS; RAPAMYCIN; S6 KINASE; SIGNALING PATHWAYS; SPECIFIC INHIBITORS;

EID: 84873879360     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.427351     Document Type: Article
Times cited : (16)

References (56)
  • 1
    • 81555195261 scopus 로고    scopus 로고
    • Cellular and molecular action of the mitogenic protein-deamidating toxin from Pasteurella multocida
    • Wilson, B. A., and Ho, M. (2011) Cellular and molecular action of the mitogenic protein-deamidating toxin from Pasteurella multocida. FEBS J. 278, 4616-4632
    • (2011) FEBS J. , vol.278 , pp. 4616-4632
    • Wilson, B.A.1    Ho, M.2
  • 2
    • 0348225063 scopus 로고    scopus 로고
    • The Pasteurella multocida toxin is encoded within a lysogenic bacteriophage
    • Pullinger, G. D., Bevir, T., and Lax, A. J. (2004) The Pasteurella multocida toxin is encoded within a lysogenic bacteriophage. Mol. Microbiol. 51, 255-269
    • (2004) Mol. Microbiol. , vol.51 , pp. 255-269
    • Pullinger, G.D.1    Bevir, T.2    Lax, A.J.3
  • 3
    • 0025320512 scopus 로고
    • Sequence of the dermonecrotic toxin of Pasteurella multocida ssp. multocida
    • Buys, W. E., Smith, H. E., Kamps, A. M., Kamp, E. M., and Smits, M. A. (1990) Sequence of the dermonecrotic toxin of Pasteurella multocida ssp. multocida. Nucleic Acids Res. 18, 2815-2816
    • (1990) Nucleic Acids Res. , vol.18 , pp. 2815-2816
    • Buys, W.E.1    Smith, H.E.2    Kamps, A.M.3    Kamp, E.M.4    Smits, M.A.5
  • 6
    • 0034798767 scopus 로고    scopus 로고
    • Pasteurella multocida toxin. The mitogenic toxin that stimulates signalling cascades to regulate growth and differentiation
    • Lax, A. J., and Grigoriadis, A. E. (2001) Pasteurella multocida toxin. The mitogenic toxin that stimulates signalling cascades to regulate growth and differentiation. Int. J. Med. Microbiol. 291, 261-268
    • (2001) Int. J. Med. Microbiol. , vol.291 , pp. 261-268
    • Lax, A.J.1    Grigoriadis, A.E.2
  • 8
    • 0031552003 scopus 로고    scopus 로고
    • Nasal infection with Pasteurella multocida causes proliferation of bladder epithelium in gnotobiotic pigs
    • Hoskins, I. C., Thomas, L. H., and Lax, A. J. (1997) Nasal infection with Pasteurella multocida causes proliferation of bladder epithelium in gnotobiotic pigs. Vet. Rec. 140, 22
    • (1997) Vet. Rec. , vol.140 , pp. 22
    • Hoskins, I.C.1    Thomas, L.H.2    Lax, A.J.3
  • 9
    • 34548412807 scopus 로고    scopus 로고
    • Calcineurin-independent inhibition of 3T3-L1 adipogenesis by Pasteurella multocida toxin. Suppression of Notch1, stabilization of α-catenin and pre-adipocyte factor 1
    • Aminova, L. R., and Wilson, B. A. (2007) Calcineurin-independent inhibition of 3T3-L1 adipogenesis by Pasteurella multocida toxin. Suppression of Notch1, stabilization of α-catenin and pre-adipocyte factor 1. Cell Microbiol. 9, 2485-2496
    • (2007) Cell Microbiol , vol.9 , pp. 2485-2496
    • Aminova, L.R.1    Wilson, B.A.2
  • 10
    • 15944390635 scopus 로고    scopus 로고
    • Opinion. Bacterial toxins and cancer. A case to answer?
    • Lax, A. J. (2005) Opinion. Bacterial toxins and cancer. A case to answer? Nat. Rev. Microbiol. 3, 343-349
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 343-349
    • Lax, A.J.1
  • 12
    • 79960585779 scopus 로고    scopus 로고
    • Enzymatic actions of Pasteurella multocida toxin detected by monoclonal antibodies recognizing the deamidated α subunit of the heterotrimeric GTPase Gq
    • Kamitani, S., Ao, S., Toshima, H., Tachibana, T., Hashimoto, M., Kitadokoro, K., Fukui-Miyazaki, A., Abe, H., and Horiguchi, Y. (2011) Enzymatic actions of Pasteurella multocida toxin detected by monoclonal antibodies recognizing the deamidated α subunit of the heterotrimeric GTPase Gq. FEBS J 278, 2702-2712
    • (2011) FEBS J , vol.278 , pp. 2702-2712
    • Kamitani, S.1    Ao, S.2    Toshima, H.3    Tachibana, T.4    Hashimoto, M.5    Kitadokoro, K.6    Fukui-Miyazaki, A.7    Abe, H.8    Horiguchi, Y.9
  • 13
    • 0025334252 scopus 로고
    • Pasteurella multocida toxin, a potent mitogen, stimulates protein kinase C-dependent and -independent protein phosphorylation in Swiss 3T3 cells
    • Staddon, J. M., Chanter, N., Lax, A. J., Higgins, T. E., and Rozengurt, E. (1990) Pasteurella multocida toxin, a potent mitogen, stimulates protein kinase C-dependent and -independent protein phosphorylation in Swiss 3T3 cells. J. Biol. Chem. 265, 11841-11848
    • (1990) J. Biol. Chem. , vol.265 , pp. 11841-11848
    • Staddon, J.M.1    Chanter, N.2    Lax, A.J.3    Higgins, T.E.4    Rozengurt, E.5
  • 14
    • 0025804531 scopus 로고
    • Pasteurella multocida toxin, a potent mitogen, increases inositol 1,4,5-trisphosphate and mobilizes Ca2+ in Swiss 3T3 cells
    • Staddon, J. M., Barker, C. J., Murphy, A. C., Chanter, N., Lax, A. J., Michell, R. H., and Rozengurt, E. (1991) Pasteurella multocida toxin, a potent mitogen, increases inositol 1,4,5-trisphosphate and mobilizes Ca2+ in Swiss 3T3 cells. J. Biol. Chem. 266, 4840-4847
    • (1991) J. Biol. Chem. , vol.266 , pp. 4840-4847
    • Staddon, J.M.1    Barker, C.J.2    Murphy, A.C.3    Chanter, N.4    Lax, A.J.5    Michell, R.H.6    Rozengurt, E.7
  • 15
    • 0026465679 scopus 로고
    • Pasteurella multocida toxin selectively facilitates phosphatidylinositol 4,5-bisphosphate hydrolysis by bombesin, vasopressin, and endothelin. Requirement for A functional G protein
    • Murphy, A. C., and Rozengurt, E. (1992) Pasteurella multocida toxin selectively facilitates phosphatidylinositol 4,5-bisphosphate hydrolysis by bombesin, vasopressin, and endothelin. Requirement for a functional G protein. J. Biol. Chem. 267, 25296-25303
    • (1992) J. Biol. Chem. , vol.267 , pp. 25296-25303
    • Murphy, A.C.1    Rozengurt, E.2
  • 16
    • 0034695566 scopus 로고    scopus 로고
    • Pasteurella multocida toxin stimulates mitogen-activated protein kinase via Gq/11-dependent transactivation of the epidermal growth factor receptor
    • Seo, B., Choy, E. W., Maudsley, S., Miller, W. E., Wilson, B. A., and Luttrell, L. M. (2000) Pasteurella multocida toxin stimulates mitogen-activated protein kinase via Gq/11-dependent transactivation of the epidermal growth factor receptor. J. Biol. Chem. 275, 2239-2245
    • (2000) J. Biol. Chem. , vol.275 , pp. 2239-2245
    • Seo, B.1    Choy, E.W.2    Maudsley, S.3    Miller, W.E.4    Wilson, B.A.5    Luttrell, L.M.6
  • 17
    • 0035830825 scopus 로고    scopus 로고
    • Pleiotropic effects of Pasteurella multocida toxin are mediated by Gq-dependent and -independent mechanisms. involvement of Gq but not G11
    • Zywietz, A., Gohla, A., Schmelz, M., Schultz, G., and Offermanns, S. (2001) Pleiotropic effects of Pasteurella multocida toxin are mediated by Gq-dependent and -independent mechanisms. involvement of Gq but not G11. J. Biol. Chem. 276, 3840-3845
    • (2001) J. Biol. Chem. , vol.276 , pp. 3840-3845
    • Zywietz, A.1    Gohla, A.2    Schmelz, M.3    Schultz, G.4    Offermanns, S.5
  • 18
    • 0033913887 scopus 로고    scopus 로고
    • Differential modulation and subsequent blockade of mitogenic signaling and cell cycle progression by Pasteurella multocida toxin
    • Wilson, B. A., Aminova, L. R., Ponferrada, V. G., and Ho, M. (2000) Differential modulation and subsequent blockade of mitogenic signaling and cell cycle progression by Pasteurella multocida toxin. Infect. Immun. 68, 4531-4538
    • (2000) Infect. Immun. , vol.68 , pp. 4531-4538
    • Wilson, B.A.1    Aminova, L.R.2    Ponferrada, V.G.3    Ho, M.4
  • 19
    • 0034877755 scopus 로고    scopus 로고
    • Escherichia coli cytotoxic necrotizing factor and Pasteurella multocida toxin induce focal adhesion kinase autophosphorylation and Src association
    • Thomas, W., Pullinger, G. D., Lax, A. J., and Rozengurt, E. (2001) Escherichia coli cytotoxic necrotizing factor and Pasteurella multocida toxin induce focal adhesion kinase autophosphorylation and Src association. Infect. Immun. 69, 5931-5935
    • (2001) Infect. Immun. , vol.69 , pp. 5931-5935
    • Thomas, W.1    Pullinger, G.D.2    Lax, A.J.3    Rozengurt, E.4
  • 20
    • 27744535465 scopus 로고    scopus 로고
    • Pasteurella multocida toxin-induced activation of RhoA is mediated via two families of Gα proteins, Gαq, and Gα12/13
    • Orth, J. H., Lang, S., Taniguchi, M., and Aktories, K. (2005) Pasteurella multocida toxin-induced activation of RhoA is mediated via two families of Gα proteins, Gαq, and Gα12/13. J. Biol. Chem. 280, 36701-36707
    • (2005) J. Biol. Chem. , vol.280 , pp. 36701-36707
    • Orth, J.H.1    Lang, S.2    Taniguchi, M.3    Aktories, K.4
  • 21
    • 52049091512 scopus 로고    scopus 로고
    • What controls TOR?
    • Jacinto, E. (2008) What controls TOR? IUBMB Life 60, 483-496
    • (2008) IUBMB Life , vol.60 , pp. 483-496
    • Jacinto, E.1
  • 22
    • 67349217986 scopus 로고    scopus 로고
    • Molecular mechanisms of mTOR-mediated translational control
    • Ma, X. M., and Blenis, J. (2009) Molecular mechanisms of mTOR-mediated translational control. Nat. Rev. Mol. Cell Biol. 10, 307-318
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 307-318
    • Ma, X.M.1    Blenis, J.2
  • 23
    • 78650510609 scopus 로고    scopus 로고
    • MTOR. from growth signal integration to cancer, diabetes and ageing
    • Zoncu, R., Efeyan, A., and Sabatini, D. M. (2011) mTOR. From growth signal integration to cancer, diabetes and ageing. Nat. Rev. Mol. Cell Biol. 12, 21-35
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3
  • 24
    • 0030740005 scopus 로고    scopus 로고
    • The modular phosphorylation and activation of p70S6k
    • Pullen, N., and Thomas, G. (1997) The modular phosphorylation and activation of p70S6k. FEBS Lett. 410, 78-82
    • (1997) FEBS Lett. , vol.410 , pp. 78-82
    • Pullen, N.1    Thomas, G.2
  • 25
    • 56249147509 scopus 로고    scopus 로고
    • Rapamycin differentially inhibits S6Ks and 4E-BP1 to mediate cell-typespecific repression of mRNA translation
    • Choo, A. Y., Yoon, S. O., Kim, S. G., Roux, P. P., and Blenis, J. (2008) Rapamycin differentially inhibits S6Ks and 4E-BP1 to mediate cell-typespecific repression of mRNA translation. Proc. Natl. Acad. Sci. U.S.A. 105, 17414-17419
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 17414-17419
    • Choo, A.Y.1    Yoon, S.O.2    Kim, S.G.3    Roux, P.P.4    Blenis, J.5
  • 27
    • 33748752151 scopus 로고    scopus 로고
    • The mammalian target of rapamycin (mTOR) pathway regulates mitochondrial oxygen consumption and oxidative capacity
    • Schieke, S. M., Phillips, D., McCoy, J. P., Jr., Aponte, A. M., Shen, R. F., Balaban, R. S., and Finkel, T. (2006) The mammalian target of rapamycin (mTOR) pathway regulates mitochondrial oxygen consumption and oxidative capacity. J. Biol. Chem. 281, 27643-27652
    • (2006) J. Biol. Chem. , vol.281 , pp. 27643-27652
    • Schieke, S.M.1    Phillips, D.2    McCoy Jr., J.P.3    Aponte, A.M.4    Shen, R.F.5    Balaban, R.S.6    Finkel, T.7
  • 29
    • 0018850560 scopus 로고
    • Physiological control of phosphorylation ribosomal protein S6 in Mucor racemosus
    • Larsen, A., and Sypherd, P. S. (1980) Physiological control of phosphorylation ribosomal protein S6 in Mucor racemosus. J. Bacteriol. 141, 20-25
    • (1980) J. Bacteriol. , vol.141 , pp. 20-25
    • Larsen, A.1    Sypherd, P.S.2
  • 30
    • 0016251762 scopus 로고
    • The phosphorylation of liver ribosomal proteins in vivo. Evidence that only a single small subunit protein (S6) is phosphorylated
    • Gressner, A. M., and Wool, I. G. (1974) The phosphorylation of liver ribosomal proteins in vivo. Evidence that only a single small subunit protein (S6) is phosphorylated. J. Biol. Chem. 249, 6917-6925
    • (1974) J. Biol. Chem. , vol.249 , pp. 6917-6925
    • Gressner, A.M.1    Wool, I.G.2
  • 33
    • 84555189440 scopus 로고    scopus 로고
    • Regulation and function of the RSK family of protein kinases
    • Romeo, Y., Zhang, X., and Roux, P. P. (2012) Regulation and function of the RSK family of protein kinases. Biochem. J. 441, 553-569
    • (2012) Biochem. J. , Issue.441 , pp. 553-569
    • Romeo, Y.1    Zhang, X.2    Roux, P.P.3
  • 34
    • 0347318052 scopus 로고    scopus 로고
    • The AMP-activated protein kinase cascade. A unifying system for energy control
    • Carling, D. (2004) The AMP-activated protein kinase cascade. A unifying system for energy control. Trends Biochem. Sci. 29, 18-24
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 18-24
    • Carling, D.1
  • 35
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki, K., Zhu, T., and Guan, K. L. (2003) TSC2 mediates cellular energy response to control cell growth and survival. Cell 115, 577-590
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 37
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov, D. D., Guertin, D. A., Ali, S. M., and Sabatini, D. M. (2005) Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307, 1098-1101
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 39
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide- dependent protein kinase which phosphorylates and activates protein kinase Bα
    • Alessi, D. R., James, S. R., Downes, C. P., Holmes, A. B., Gaffney, P. R., Reese, C. B., and Cohen, P. (1997) Characterization of a 3-phosphoinositide- dependent protein kinase which phosphorylates and activates protein kinase Bα. Curr. Biol. 7, 261-269
    • (1997) Curr. Biol. , vol.7 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.5    Reese, C.B.6    Cohen, P.7
  • 40
    • 25444524850 scopus 로고    scopus 로고
    • Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity
    • Hahn-Windgassen, A., Nogueira, V., Chen, C. C., Skeen, J. E., Sonenberg, N., and Hay, N. (2005) Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity. J. Biol. Chem. 280, 32081-32089
    • (2005) J. Biol. Chem. , vol.280 , pp. 32081-32089
    • Hahn-Windgassen, A.1    Nogueira, V.2    Chen, C.C.3    Skeen, J.E.4    Sonenberg, N.5    Hay, N.6
  • 41
    • 33847718214 scopus 로고    scopus 로고
    • The EGF receptor family. Spearheading a merger of signaling and therapeutics
    • Bublil, E. M., and Yarden, Y. (2007) The EGF receptor family. Spearheading a merger of signaling and therapeutics. Curr. Opin. Cell Biol. 19, 124-134
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 124-134
    • Bublil, E.M.1    Yarden, Y.2
  • 42
    • 0037012652 scopus 로고    scopus 로고
    • Dual actions of the Gαq agonist Pasteurella multocida toxin to promote cardiomyocyte hypertrophy and enhance apoptosis susceptibility
    • Sabri, A., Wilson, B. A., and Steinberg, S. F. (2002) Dual actions of the Gαq agonist Pasteurella multocida toxin to promote cardiomyocyte hypertrophy and enhance apoptosis susceptibility. Circ. Res. 90, 850-857
    • (2002) Circ. Res. , vol.90 , pp. 850-857
    • Sabri, A.1    Wilson, B.A.2    Steinberg, S.F.3
  • 43
    • 0020120451 scopus 로고
    • Preferential utilization of phosphorylated 40-S ribosomal subunits during initiation complex formation
    • Duncan, R., and McConkey, E. H. (1982) Preferential utilization of phosphorylated 40-S ribosomal subunits during initiation complex formation. Eur. J. Biochem. 123, 535-538
    • (1982) Eur. J. Biochem. , vol.123 , pp. 535-538
    • Duncan, R.1    McConkey, E.H.2
  • 44
    • 0032956850 scopus 로고    scopus 로고
    • P70(S6K) controls selective mRNA translation during oocyte maturation and early embryogenesis in Xenopus laevis
    • Schwab, M. S., Kim, S. H., Terada, N., Edfjäll, C., Kozma, S. C., Thomas, G., and Maller, J. L. (1999) p70(S6K) controls selective mRNA translation during oocyte maturation and early embryogenesis in Xenopus laevis. Mol. Cell Biol. 19, 2485-2494
    • (1999) Mol. Cell Biol. , vol.19 , pp. 2485-2494
    • Schwab, M.S.1    Kim, S.H.2    Terada, N.3    Edfjäll, C.4    Kozma, S.C.5    Thomas, G.6    Maller, J.L.7
  • 45
    • 0027415831 scopus 로고
    • Identification of 40 S ribosomal protein S6 phosphorylation sites in Swiss mouse 3T3 fibroblasts stimulated with serum
    • Bandi, H. R., Ferrari, S., Krieg, J., Meyer, H. E., and Thomas, G. (1993) Identification of 40 S ribosomal protein S6 phosphorylation sites in Swiss mouse 3T3 fibroblasts stimulated with serum. J. Biol. Chem. 268, 4530-4533
    • (1993) J. Biol. Chem. , vol.268 , pp. 4530-4533
    • Bandi, H.R.1    Ferrari, S.2    Krieg, J.3    Meyer, H.E.4    Thomas, G.5
  • 47
    • 11144356304 scopus 로고    scopus 로고
    • S6K1-/-/S6K2-/- mice exhibit perinatal lethality and rapamycin-sensitive 5'-terminal oligopyrimidine mRNA translation and reveal a mitogenactivated protein kinase-dependent S6 kinase pathway
    • Pende, M., Um, S. H., Mieulet, V., Sticker, M., Goss, V. L., Mestan, J., Mueller, M., Fumagalli, S., Kozma, S. C., and Thomas, G. (2004) S6K1-/-/S6K2-/- mice exhibit perinatal lethality and rapamycin-sensitive 5'-terminal oligopyrimidine mRNA translation and reveal a mitogenactivated protein kinase-dependent S6 kinase pathway. Mol. Cell Biol. 24, 3112-3124
    • (2004) Mol. Cell Biol. , vol.24 , pp. 3112-3124
    • Pende, M.1    Um, S.H.2    Mieulet, V.3    Sticker, M.4    Goss, V.L.5    Mestan, J.6    Mueller, M.7    Fumagalli, S.8    Kozma, S.C.9    Thomas, G.10
  • 48
    • 61449235398 scopus 로고    scopus 로고
    • Not all substrates are treated equally. Implications for mTOR, rapamycin resistance and cancer therapy
    • Choo, A. Y., and Blenis, J. (2009) Not all substrates are treated equally. Implications for mTOR, rapamycin resistance and cancer therapy. Cell Cycle 8, 567-572
    • (2009) Cell Cycle , vol.8 , pp. 567-572
    • Choo, A.Y.1    Blenis, J.2
  • 49
    • 67650228579 scopus 로고    scopus 로고
    • Rapamycin inhibits mTORC1, but not completely
    • Thoreen, C. C., and Sabatini, D. M. (2009) Rapamycin inhibits mTORC1, but not completely. Autophagy 5, 725-726
    • (2009) Autophagy , vol.5 , pp. 725-726
    • Thoreen, C.C.1    Sabatini, D.M.2
  • 50
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • Rhee, S. G. (2001) Regulation of phosphoinositide-specific phospholipase C. Annu. Rev. Biochem. 70, 281-312
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 51
    • 4544253724 scopus 로고    scopus 로고
    • Action of Pasteurella multocida toxin depends on the helical domain of Gαq
    • Orth, J. H., Lang, S., and Aktories, K. (2004) Action of Pasteurella multocida toxin depends on the helical domain of Gαq. J. Biol. Chem. 279, 34150-34155
    • (2004) J. Biol. Chem. , vol.279 , pp. 34150-34155
    • Orth, J.H.1    Lang, S.2    Aktories, K.3
  • 52
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and tumour promotion
    • Nishizuka, Y. (1984) The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature 308, 693-698
    • (1984) Nature , vol.308 , pp. 693-698
    • Nishizuka, Y.1
  • 53
    • 47749127695 scopus 로고    scopus 로고
    • Protein kinase D links Gq-coupled receptors to cAMP response element-binding protein (CREB)-Ser133 phosphorylation in the heart
    • Ozgen, N., Obreztchikova, M., Guo, J., Elouardighi, H., Dorn, G. W., 2nd, Wilson, B. A., and Steinberg, S. F. (2008) Protein kinase D links Gq-coupled receptors to cAMP response element-binding protein (CREB)-Ser133 phosphorylation in the heart. J. Biol. Chem. 283, 17009-17019
    • (2008) J. Biol. Chem. , vol.283 , pp. 17009-17019
    • Ozgen, N.1    Obreztchikova, M.2    Guo, J.3    Elouardighi, H.4    Dorn, I.I.G.W.5    Wilson, B.A.6    Steinberg, S.F.7
  • 54
    • 80051933965 scopus 로고    scopus 로고
    • Dual function of protein kinase C (PKC) in 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced manganese superoxide dismutase (MnSOD) expression. Activation of CREB and FOXO3a by PKC-α phosphorylation and by PKC-mediated inactivation of Akt, respectively
    • Chung, Y. W., Kim, H. K., Kim, I. Y., Yim, M. B., and Chock, P. B. (2011) Dual function of protein kinase C (PKC) in 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced manganese superoxide dismutase (MnSOD) expression. Activation of CREB and FOXO3a by PKC-α phosphorylation and by PKC-mediated inactivation of Akt, respectively. J. Biol. Chem. 286, 29681-29690
    • (2011) J. Biol. Chem. , vol.286 , pp. 29681-29690
    • Chung, Y.W.1    Kim, H.K.2    Kim, I.Y.3    Yim, M.B.4    Chock, P.B.5
  • 55
    • 0034646657 scopus 로고    scopus 로고
    • Distinct signalling pathways mediate insulin and phorbol ester-stimulated eukaryotic initiation factor 4F assembly and protein synthesis in HEK 293 cells
    • Herbert, T. P., Kilhams, G. R., Batty, I. H., and Proud, C. G. (2000) Distinct signalling pathways mediate insulin and phorbol ester-stimulated eukaryotic initiation factor 4F assembly and protein synthesis in HEK 293 cells. J. Biol. Chem. 275, 11249-11256
    • (2000) J. Biol. Chem. , vol.275 , pp. 11249-11256
    • Herbert, T.P.1    Kilhams, G.R.2    Batty, I.H.3    Proud, C.G.4
  • 56
    • 14144254701 scopus 로고    scopus 로고
    • Quantitative phosphorylation profiling of the ERK/p90 ribosomal S6 kinase-signaling cassette and its targets, the tuberous sclerosis tumor suppressors
    • Ballif, B. A., Roux, P. P., Gerber, S. A., MacKeigan, J. P., Blenis, J., and Gygi, S. P. (2005) Quantitative phosphorylation profiling of the ERK/p90 ribosomal S6 kinase-signaling cassette and its targets, the tuberous sclerosis tumor suppressors. Proc. Natl. Acad. Sci. U.S.A. 102, 667-672
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 667-672
    • Ballif, B.A.1    Roux, P.P.2    Gerber, S.A.3    MacKeigan, J.P.4    Blenis, J.5    Gygi, S.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.