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Volumn 431, Issue , 2007, Pages 113-142

Methods for Studying Signal-Dependent Regulation of Translation Factor Activity

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 (2 CHLORO 4 IODOANILINO) N CYCLOPROPYLMETHOXY 3,4 DIFLUOROBENZAMIDE; 2 MORPHOLINO 8 PHENYLCHROMONE; 4 (4 FLUOROPHENYL) 2 (4 HYDROXYPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; GUANINE NUCLEOTIDE EXCHANGE FACTOR; INITIATION FACTOR; INITIATION FACTOR 4E BINDING PROTEIN 1; INITIATION FACTOR 4F; MAMMALIAN TARGET OF RAPAMYCIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; RAPAMYCIN; UO 126; WORTMANNIN; ENZYME INHIBITOR; PROTEIN KINASE; TRANSCRIPTION FACTOR;

EID: 38449110890     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(07)31007-0     Document Type: Review
Times cited : (33)

References (76)
  • 1
    • 3242882820 scopus 로고    scopus 로고
    • PI 3-kinase related kinases: "Big" players in stress-induced signaling pathways
    • Abraham R.T. PI 3-kinase related kinases: "Big" players in stress-induced signaling pathways. DNA Repair (Amst.) 3 (2004) 883-887
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 883-887
    • Abraham, R.T.1
  • 2
    • 0028884033 scopus 로고
    • PD-098059 is a specific inhibitor of the activation of mitogen-activated protein kinase in vitro and in vivo
    • Alessi D.R., Cuenda A., Cohen P., Dudley D.T., and Saltiel A.R. PD-098059 is a specific inhibitor of the activation of mitogen-activated protein kinase in vitro and in vivo. J. Biol. Chem. 270 (1995) 27489-27494
    • (1995) J. Biol. Chem. , vol.270 , pp. 27489-27494
    • Alessi, D.R.1    Cuenda, A.2    Cohen, P.3    Dudley, D.T.4    Saltiel, A.R.5
  • 3
    • 0027432424 scopus 로고
    • Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: The role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses
    • Arcaro A., and Wymann M.P. Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: The role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses. Biochem. J. 296 (1993) 297-301
    • (1993) Biochem. J. , vol.296 , pp. 297-301
    • Arcaro, A.1    Wymann, M.P.2
  • 4
    • 0035225023 scopus 로고    scopus 로고
    • The p70 S6 kinase integrates nutrient and growth signals to control translational capacity
    • Avruch J., Belham C., Weng Q., Hara K., and Yonezawa K. The p70 S6 kinase integrates nutrient and growth signals to control translational capacity. Prog. Mol. Subcell. Biol. 26 (2001) 115-154
    • (2001) Prog. Mol. Subcell. Biol. , vol.26 , pp. 115-154
    • Avruch, J.1    Belham, C.2    Weng, Q.3    Hara, K.4    Yonezawa, K.5
  • 5
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: An update
    • Bain J., McLauchlan H., Elliott M., and Cohen P. The specificities of protein kinase inhibitors: An update. Biochem. J. 371 (2003) 199-204
    • (2003) Biochem. J. , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 77 (1976) 248-254
    • (1976) Anal. Biochem. , vol.77 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0029831167 scopus 로고    scopus 로고
    • Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002
    • Brunn G.J., Williams J., Sabers C., Weiderrecht G., Lawrence J.C., and Abraham R.T. Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002. EMBO J. 15 (1996) 5256-5267
    • (1996) EMBO J. , vol.15 , pp. 5256-5267
    • Brunn, G.J.1    Williams, J.2    Sabers, C.3    Weiderrecht, G.4    Lawrence, J.C.5    Abraham, R.T.6
  • 8
    • 23844516065 scopus 로고    scopus 로고
    • The Mnks are novel components in the control of TNFalpha biosynthesis and phosphorylate and regulate hnRNP A1
    • Buxade M., Parra J.L., Rousseau S., Shpiro N., Marquez R., Morrice N., Bain J., Espel E., and Proud C.G. The Mnks are novel components in the control of TNFalpha biosynthesis and phosphorylate and regulate hnRNP A1. Immunity 23 (2005) 177-189
    • (2005) Immunity , vol.23 , pp. 177-189
    • Buxade, M.1    Parra, J.L.2    Rousseau, S.3    Shpiro, N.4    Marquez, R.5    Morrice, N.6    Bain, J.7    Espel, E.8    Proud, C.G.9
  • 10
    • 0028308412 scopus 로고
    • Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocation
    • Cheatham B., Vlahos C.J., Cheatham L., Wang L., Blenis J., and Kahn C.R. Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocation. Mol. Cell. Biol. 14 (1994) 4902-4911
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4902-4911
    • Cheatham, B.1    Vlahos, C.J.2    Cheatham, L.3    Wang, L.4    Blenis, J.5    Kahn, C.R.6
  • 11
    • 0025282334 scopus 로고
    • Identification of Xenopus S6 protein kinase homologs (pp90rsk) in somatic cells: Phosphorylation and activation during initiation of cell proliferation
    • Chen R.H., and Blenis J. Identification of Xenopus S6 protein kinase homologs (pp90rsk) in somatic cells: Phosphorylation and activation during initiation of cell proliferation. Mol. Cell. Biol. 10 (1990) 3204-3215
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3204-3215
    • Chen, R.H.1    Blenis, J.2
  • 13
    • 0028988138 scopus 로고
    • SB-203580 is a specific inhibitor of a MAP kinase homolog which is activated by cellular stresses and interleukin-1
    • Cuenda A., Rouse J., Doza Y.N., Meier R., Cohen P., Gallagher T.F., Young P.R., and Lee J.C. SB-203580 is a specific inhibitor of a MAP kinase homolog which is activated by cellular stresses and interleukin-1. FEBS Lett. 364 (1995) 229-233
    • (1995) FEBS Lett. , vol.364 , pp. 229-233
    • Cuenda, A.1    Rouse, J.2    Doza, Y.N.3    Meier, R.4    Cohen, P.5    Gallagher, T.F.6    Young, P.R.7    Lee, J.C.8
  • 14
    • 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. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351 (2000) 95-105
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 15
    • 11144252845 scopus 로고    scopus 로고
    • PD98059 and U0126 activate AMP-activated protein kinase by increasing the cellular AMP:ATP ratio and not via inhibition of the MAP kinase pathway
    • Dokladda K., Green K.A., Pan D.A., and Hardie D.G. PD98059 and U0126 activate AMP-activated protein kinase by increasing the cellular AMP:ATP ratio and not via inhibition of the MAP kinase pathway. FEBS Lett. 579 (2005) 236-240
    • (2005) FEBS Lett. , vol.579 , pp. 236-240
    • Dokladda, K.1    Green, K.A.2    Pan, D.A.3    Hardie, D.G.4
  • 19
    • 0034646657 scopus 로고    scopus 로고
    • Distinct signaling pathways mediate insulin and phorbol ester-stimulated eIF4F assembly and protein synthesis in HEK 293 cells
    • Herbert T.P., Kilhams G.R., Batty I.H., and Proud C.G. Distinct signaling pathways mediate insulin and phorbol ester-stimulated eIF4F assembly and protein synthesis in HEK 293 cells. J. Biol. Chem. 275 (2000) 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
  • 20
    • 34247163315 scopus 로고    scopus 로고
    • Regulation of translation elongation and the cotranslational protein targeting pathway
    • Mathews M.B., Sonenberg N., and Hershey J.W.B. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring, NY
    • Herbert T.P., and Proud C.G. Regulation of translation elongation and the cotranslational protein targeting pathway. In: Mathews M.B., Sonenberg N., and Hershey J.W.B. (Eds). "Translational Control in Biology and Medicine" (2006), Cold Spring Harbor Laboratory Press, Cold Spring, NY 601-624
    • (2006) "Translational Control in Biology and Medicine" , pp. 601-624
    • Herbert, T.P.1    Proud, C.G.2
  • 21
    • 33644753147 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element
    • Hitti E., Iakovleva T., Brook M., Deppenmeier S., Gruber A.D., Radzioch D., Clark A.R., Blackshear P.J., Kotlyarov A., and Gaestel M. Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element. Mol. Cell Biol. 26 (2006) 2399-2407
    • (2006) Mol. Cell Biol. , vol.26 , pp. 2399-2407
    • Hitti, E.1    Iakovleva, T.2    Brook, M.3    Deppenmeier, S.4    Gruber, A.D.5    Radzioch, D.6    Clark, A.R.7    Blackshear, P.J.8    Kotlyarov, A.9    Gaestel, M.10
  • 22
    • 22544455676 scopus 로고    scopus 로고
    • Identification of S6 kinase 1 as a novel mammalian target of rapamycin (mTOR)-phosphorylating kinase
    • Holz M.K., and Blenis J. Identification of S6 kinase 1 as a novel mammalian target of rapamycin (mTOR)-phosphorylating kinase. J. Biol. Chem. 280 (2005) 26089-26093
    • (2005) J. Biol. Chem. , vol.280 , pp. 26089-26093
    • Holz, M.K.1    Blenis, J.2
  • 24
    • 33749076673 scopus 로고    scopus 로고
    • SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity
    • Jacinto E., Facchinetti V., Liu D., Soto N., Wei S., Jung S.Y., Huang Q., Qin J., and Su B. SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. Cell 127 (2006) 125-137
    • (2006) Cell , vol.127 , pp. 125-137
    • Jacinto, E.1    Facchinetti, V.2    Liu, D.3    Soto, N.4    Wei, S.5    Jung, S.Y.6    Huang, Q.7    Qin, J.8    Su, B.9
  • 25
    • 0033543549 scopus 로고    scopus 로고
    • Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases
    • Kamakura S., Moriguchi T., and Nishida E. Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. J. Biol. Chem. 274 (1999) 26563-26571
    • (1999) J. Biol. Chem. , vol.274 , pp. 26563-26571
    • Kamakura, S.1    Moriguchi, T.2    Nishida, E.3
  • 26
    • 33748743740 scopus 로고    scopus 로고
    • Multiple activation mechanisms of p38alpha mitogen-activated protein kinase
    • Kang Y.J., Seit-Nebi A., Davis R.J., and Han J. Multiple activation mechanisms of p38alpha mitogen-activated protein kinase. J. Biol. Chem. 281 (2006) 26225-26234
    • (2006) J. Biol. Chem. , vol.281 , pp. 26225-26234
    • Kang, Y.J.1    Seit-Nebi, A.2    Davis, R.J.3    Han, J.4
  • 27
    • 0034928792 scopus 로고    scopus 로고
    • Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2
    • Knauf U., Tschopp C., and Gram H. Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2. Mol. Cell. Biol. 21 (2001) 5500-5511
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5500-5511
    • Knauf, U.1    Tschopp, C.2    Gram, H.3
  • 29
    • 0034629345 scopus 로고    scopus 로고
    • The pyridinyl imidazole inhibitor SB203580 blocks phosphoinositide-dependent protein kinase activity, protein kinase B phosphorylation, and retinoblastoma hyperphosphorylation in interleukin-2-stimulated T cells independently of p38 mitogen-activated protein kinase
    • Lali F.V., Hunt A.E., Turner S.J., and Foxwell B.M. The pyridinyl imidazole inhibitor SB203580 blocks phosphoinositide-dependent protein kinase activity, protein kinase B phosphorylation, and retinoblastoma hyperphosphorylation in interleukin-2-stimulated T cells independently of p38 mitogen-activated protein kinase. J. Biol. Chem. 275 (2000) 7395-7402
    • (2000) J. Biol. Chem. , vol.275 , pp. 7395-7402
    • Lali, F.V.1    Hunt, A.E.2    Turner, S.J.3    Foxwell, B.M.4
  • 31
    • 33645078650 scopus 로고    scopus 로고
    • Regulation of membrane traffic by phosphoinositide 3-kinases
    • Lindmo K., and Stenmark H. Regulation of membrane traffic by phosphoinositide 3-kinases. J. Cell Sci. 119 (2006) 605-614
    • (2006) J. Cell Sci. , vol.119 , pp. 605-614
    • Lindmo, K.1    Stenmark, H.2
  • 33
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4gamma and the translational repressors 4E-binding proteins
    • Mader S., Lee H., Pause A., and Sonenberg N. The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4gamma and the translational repressors 4E-binding proteins. Mol. Cell. Biol. 15 (1995) 4990-4997
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 34
    • 11344286593 scopus 로고    scopus 로고
    • MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the G2/M transition and S phase progression in response to UV irradiation
    • Manke I.A., Nguyen A., Lim D., Stewart M.Q., Elia A.E., and Yaffe M.B. MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the G2/M transition and S phase progression in response to UV irradiation. Mol. Cell 17 (2005) 37-48
    • (2005) Mol. Cell , vol.17 , pp. 37-48
    • Manke, I.A.1    Nguyen, A.2    Lim, D.3    Stewart, M.Q.4    Elia, A.E.5    Yaffe, M.B.6
  • 35
    • 0038540963 scopus 로고    scopus 로고
    • United at last: The tuberous sclerosis complex gene products connect the phosphoinositide 3-kinase/Akt pathway to mammalian target of rapamycin (mTOR) signaling
    • Manning B.D., and Cantley L.C. United at last: The tuberous sclerosis complex gene products connect the phosphoinositide 3-kinase/Akt pathway to mammalian target of rapamycin (mTOR) signaling. Biochem. Soc. Trans. 31 (2003) 573-578
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 573-578
    • Manning, B.D.1    Cantley, L.C.2
  • 36
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway
    • Manning B.D., Tee A.R., Logsdon M.N., Blenis J., and Cantley L.C. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol. Cell 10 (2002) 151-162
    • (2002) Mol. Cell , vol.10 , pp. 151-162
    • Manning, B.D.1    Tee, A.R.2    Logsdon, M.N.3    Blenis, J.4    Cantley, L.C.5
  • 37
    • 0028829053 scopus 로고
    • Multiple signaling pathways involved in the stimulation of fatty acid and glycogen synthesis by insulin in rat epididymal fat pads
    • Moule S.K., Edgell N.J., Welsh G.I., Diggle T.A., Foulstone E.J., Heesom K.J., Proud C.G., and Denton R.M. Multiple signaling pathways involved in the stimulation of fatty acid and glycogen synthesis by insulin in rat epididymal fat pads. Biochem. J. 311 (1995) 595-601
    • (1995) Biochem. J. , vol.311 , pp. 595-601
    • Moule, S.K.1    Edgell, N.J.2    Welsh, G.I.3    Diggle, T.A.4    Foulstone, E.J.5    Heesom, K.J.6    Proud, C.G.7    Denton, R.M.8
  • 38
    • 33747792064 scopus 로고    scopus 로고
    • MAPK signaling: ERK5 versus ERK1/2
    • Nishimoto S., and Nishida E. MAPK signaling: ERK5 versus ERK1/2. EMBO Rep. 7 (2006) 782-786
    • (2006) EMBO Rep. , vol.7 , pp. 782-786
    • Nishimoto, S.1    Nishida, E.2
  • 39
    • 4444258507 scopus 로고    scopus 로고
    • Identification and molecular characterization of Mnk1b, a splice variant of human MAP kinase-interacting kinase Mnk1
    • O'Loghlen A., Gonzalez V.M., Pineiro D., Perez-Morgado M.I., Salinas M., and Martin M.E. Identification and molecular characterization of Mnk1b, a splice variant of human MAP kinase-interacting kinase Mnk1. Exp. Cell Res. 299 (2004) 343-355
    • (2004) Exp. Cell Res. , vol.299 , pp. 343-355
    • O'Loghlen, A.1    Gonzalez, V.M.2    Pineiro, D.3    Perez-Morgado, M.I.4    Salinas, M.5    Martin, M.E.6
  • 40
    • 27844500638 scopus 로고    scopus 로고
    • Features of the catalytic domains and C termini of the MAPK signal-integrating kinases Mnk1 and Mnk2 determine their differing activities and regulatory properties
    • Parra J.L., Buxade M., and Proud C.G. Features of the catalytic domains and C termini of the MAPK signal-integrating kinases Mnk1 and Mnk2 determine their differing activities and regulatory properties. J. Biol. Chem. 280 (2005) 37623-37633
    • (2005) J. Biol. Chem. , vol.280 , pp. 37623-37633
    • Parra, J.L.1    Buxade, M.2    Proud, C.G.3
  • 42
    • 11144356304 scopus 로고    scopus 로고
    • S6K1(-/-)/S6K2(-/-) mice exhibit perinatal lethality and rapamycin-sensitive 5′-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated 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. S6K1(-/-)/S6K2(-/-) mice exhibit perinatal lethality and rapamycin-sensitive 5′-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent S6 kinase pathway. Mol. Cell Biol. 24 (2004) 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
  • 43
    • 0033529549 scopus 로고    scopus 로고
    • Generation of constitutively active p90 ribosomal S6 kinase in vivo. Implications for the mitogen-activated protein kinase-activated protein kinase family
    • Poteet-Smith C.E., Smith J.A., Lannigan D.A., Freed T.A., and Sturgill T.W. Generation of constitutively active p90 ribosomal S6 kinase in vivo. Implications for the mitogen-activated protein kinase-activated protein kinase family. J. Biol. Chem. 274 (1999) 22135-22138
    • (1999) J. Biol. Chem. , vol.274 , pp. 22135-22138
    • Poteet-Smith, C.E.1    Smith, J.A.2    Lannigan, D.A.3    Freed, T.A.4    Sturgill, T.W.5
  • 44
    • 21744446249 scopus 로고    scopus 로고
    • Activation of protein synthesis in cardiomyocytes by the hypertrophic agent phenylephrine requires the activation of ERK and involves phosphorylation of tuberous sclerosis complex 2 (TSC2)
    • Rolfe M., McLeod L.E., Pratt P.F., and Proud C.G. Activation of protein synthesis in cardiomyocytes by the hypertrophic agent phenylephrine requires the activation of ERK and involves phosphorylation of tuberous sclerosis complex 2 (TSC2). Biochem. J. 388 (2005) 973-984
    • (2005) Biochem. J. , vol.388 , pp. 973-984
    • Rolfe, M.1    McLeod, L.E.2    Pratt, P.F.3    Proud, C.G.4
  • 45
    • 2942530310 scopus 로고    scopus 로고
    • ERK and p38 MAPK-activated protein kinases: A family of protein kinases with diverse biological functions
    • Roux P.P., and Blenis J. ERK and p38 MAPK-activated protein kinases: A family of protein kinases with diverse biological functions. Microbiol. Mol. Biol. Rev. 68 (2004) 320-344
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 320-344
    • Roux, P.P.1    Blenis, J.2
  • 46
    • 34347242470 scopus 로고    scopus 로고
    • RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation
    • Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J., Sonenberg N., and Blenis J. RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation. J. Biol. Chem. 282 (2007) 14056-14064
    • (2007) J. Biol. Chem. , vol.282 , pp. 14056-14064
    • Roux, P.P.1    Shahbazian, D.2    Vu, H.3    Holz, M.K.4    Cohen, M.S.5    Taunton, J.6    Sonenberg, N.7    Blenis, J.8
  • 49
    • 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. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307 (2005) 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
  • 51
    • 0035133659 scopus 로고    scopus 로고
    • The MAP kinase signal-integrating kinase Mnk2 is an eIF4E kinase with high basal activity in mammalian cells
    • Scheper G.C., Morrice N.A., Kleijn M., and Proud C.G. The MAP kinase signal-integrating kinase Mnk2 is an eIF4E kinase with high basal activity in mammalian cells. Mol. Cell. Biol. 21 (2001) 743-754
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 743-754
    • Scheper, G.C.1    Morrice, N.A.2    Kleijn, M.3    Proud, C.G.4
  • 52
    • 0043133828 scopus 로고    scopus 로고
    • The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization
    • Scheper G.C., Parra J.-L., Wilson M.L., van Kollenburg B., Vertegaal A.C.O., Han Z.-G., and Proud C.G. The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization. Mol. Cell. Biol. 23 (2003) 5692-5705
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5692-5705
    • Scheper, G.C.1    Parra, J.-L.2    Wilson, M.L.3    van Kollenburg, B.4    Vertegaal, A.C.O.5    Han, Z.-G.6    Proud, C.G.7
  • 54
    • 21244480367 scopus 로고    scopus 로고
    • The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses
    • Smith E.M., Finn S.G., Tee A.R., Browne G.J., and Proud C.G. The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses. J. Biol. Chem. 280 (2005) 18717-18727
    • (2005) J. Biol. Chem. , vol.280 , pp. 18717-18727
    • Smith, E.M.1    Finn, S.G.2    Tee, A.R.3    Browne, G.J.4    Proud, C.G.5
  • 55
    • 0027647714 scopus 로고
    • Use of nonreducing SDS-PAGE for monitoring renaturation of recombinant protein synthesis initiation factor, eIF-4 alpha
    • Stern B.D., Wilson M., and Jagus R. Use of nonreducing SDS-PAGE for monitoring renaturation of recombinant protein synthesis initiation factor, eIF-4 alpha. Protein Expr. Purif. 4 (1993) 320-327
    • (1993) Protein Expr. Purif. , vol.4 , pp. 320-327
    • Stern, B.D.1    Wilson, M.2    Jagus, R.3
  • 56
    • 0026457201 scopus 로고
    • Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins
    • Stokoe D., Engel K., Campbell D.G., Cohen P., and Gaestel M. Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins. FEBS Lett. 313 (1992) 307-313
    • (1992) FEBS Lett. , vol.313 , pp. 307-313
    • Stokoe, D.1    Engel, K.2    Campbell, D.G.3    Cohen, P.4    Gaestel, M.5
  • 57
    • 0027508290 scopus 로고
    • Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2
    • Sutherland C., Alterio J., Campbell D.G., Le Bourdelles B., Mallet J., Haavik J., and Cohen P. Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2. Eur. J. Biochem. 217 (1993) 715-722
    • (1993) Eur. J. Biochem. , vol.217 , pp. 715-722
    • Sutherland, C.1    Alterio, J.2    Campbell, D.G.3    Le Bourdelles, B.4    Mallet, J.5    Haavik, J.6    Cohen, P.7
  • 58
    • 0028177965 scopus 로고
    • The alpha-isoform of glycogen synthase kinase-3 from rabbit skeletal muscle is inactivated by p70 S6 kinase or MAP kinase-activated protein kinase-1 in vitro
    • Sutherland C., and Cohen P. The alpha-isoform of glycogen synthase kinase-3 from rabbit skeletal muscle is inactivated by p70 S6 kinase or MAP kinase-activated protein kinase-1 in vitro. FEBS Lett. 338 (1994) 37-42
    • (1994) FEBS Lett. , vol.338 , pp. 37-42
    • Sutherland, C.1    Cohen, P.2
  • 59
    • 0033862548 scopus 로고    scopus 로고
    • Phosphorylation of eIF-4E on Ser 209 in response to mitogenic and inflammatory stimuli is faithfully detected by specific antibodies
    • Tschopp C., Knauf U., Brauchle M., Zurini M., Ramage P., Glueck D., New L., Han J., and Gram H. Phosphorylation of eIF-4E on Ser 209 in response to mitogenic and inflammatory stimuli is faithfully detected by specific antibodies. Mol. Cell Biol. Res. Commun. 3 (2000) 205-211
    • (2000) Mol. Cell Biol. Res. Commun. , vol.3 , pp. 205-211
    • Tschopp, C.1    Knauf, U.2    Brauchle, M.3    Zurini, M.4    Ramage, P.5    Glueck, D.6    New, L.7    Han, J.8    Gram, H.9
  • 60
    • 3242719457 scopus 로고    scopus 로고
    • Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E but not for cell growth or development
    • Ueda T., Watanabe-Fukunaga R., Fukuyama H., Nagata S., and Fukunaga R. Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E but not for cell growth or development. Mol. Cell Biol. 24 (2004) 6539-6549
    • (2004) Mol. Cell Biol. , vol.24 , pp. 6539-6549
    • Ueda, T.1    Watanabe-Fukunaga, R.2    Fukuyama, H.3    Nagata, S.4    Fukunaga, R.5
  • 63
    • 0036842351 scopus 로고    scopus 로고
    • Ras/Erk signaling is essential for activation of protein synthesis by Gq protein-coupled receptor agonists in adult cardiomyocytes
    • Wang L., and Proud C.G. Ras/Erk signaling is essential for activation of protein synthesis by Gq protein-coupled receptor agonists in adult cardiomyocytes. Circ. Res. 91 (2002) 821-829
    • (2002) Circ. Res. , vol.91 , pp. 821-829
    • Wang, L.1    Proud, C.G.2
  • 64
    • 0037032451 scopus 로고    scopus 로고
    • Regulation of the phosphorylation of elongation factor 2 by MEK-dependent signaling in adult rat cardiomyocytes
    • Wang L., and Proud C.G. Regulation of the phosphorylation of elongation factor 2 by MEK-dependent signaling in adult rat cardiomyocytes. FEBS Lett. 531 (2002) 285-289
    • (2002) FEBS Lett. , vol.531 , pp. 285-289
    • Wang, L.1    Proud, C.G.2
  • 65
    • 15044340650 scopus 로고    scopus 로고
    • Distinct signaling events downstream of mTOR cooperate to mediate the effects of amino acids and insulin on initiation factor 4E-binding proteins
    • Wang X., Beugnet A., Murakami M., Yamanaka S., and Proud C.G. Distinct signaling events downstream of mTOR cooperate to mediate the effects of amino acids and insulin on initiation factor 4E-binding proteins. Mol. Cell Biol. 25 (2005) 2558-2572
    • (2005) Mol. Cell Biol. , vol.25 , pp. 2558-2572
    • Wang, X.1    Beugnet, A.2    Murakami, M.3    Yamanaka, S.4    Proud, C.G.5
  • 66
    • 0032540244 scopus 로고    scopus 로고
    • The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses, and cytokines is mediated by distinct MAP kinase pathways
    • Wang X., Flynn A., Waskiewicz A.J., Webb B.L.J., Vries R.G., Baines I.A., Cooper J., and Proud C.G. The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses, and cytokines is mediated by distinct MAP kinase pathways. J. Biol. Chem. 273 (1998) 9373-9377
    • (1998) J. Biol. Chem. , vol.273 , pp. 9373-9377
    • Wang, X.1    Flynn, A.2    Waskiewicz, A.J.3    Webb, B.L.J.4    Vries, R.G.5    Baines, I.A.6    Cooper, J.7    Proud, C.G.8
  • 67
    • 0037373346 scopus 로고    scopus 로고
    • The C-terminus of initiation factor 4E-binding protein 1 contains multiple regulatory features that influence its function and phosphorylation
    • Wang X., Li W., Parra J.-L., Beugnet A., and Proud C.G. The C-terminus of initiation factor 4E-binding protein 1 contains multiple regulatory features that influence its function and phosphorylation. Mol. Cell. Biol. 23 (2003) 1546-1557
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1546-1557
    • Wang, X.1    Li, W.2    Parra, J.-L.3    Beugnet, A.4    Proud, C.G.5
  • 69
    • 33749431713 scopus 로고    scopus 로고
    • The mTOR pathway in the control of protein synthesis
    • Wang X., and Proud C.G. The mTOR pathway in the control of protein synthesis. Physiology (Beth.) 21 (2006) 362-369
    • (2006) Physiology (Beth.) , vol.21 , pp. 362-369
    • Wang, X.1    Proud, C.G.2
  • 70
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated kinases activate the serine/threonine kinases Mnk1 and Mnk2
    • Waskiewicz A.J., Flynn A., Proud C.G., and Cooper J.A. Mitogen-activated kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J. 16 (1997) 1909-1920
    • (1997) EMBO J. , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3    Cooper, J.A.4
  • 71
    • 0032981328 scopus 로고    scopus 로고
    • Phosphorylation of the cap-binding protein eukaryotic translation factor 4E by protein kinase Mnk1 in vivo
    • Waskiewicz A.J., Johnson J.C., Penn B., Mahalingam M., Kimball S.R., and Cooper J.A. Phosphorylation of the cap-binding protein eukaryotic translation factor 4E by protein kinase Mnk1 in vivo. Mol. Cell. Biol. 19 (1999) 1871-1880
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1871-1880
    • Waskiewicz, A.J.1    Johnson, J.C.2    Penn, B.3    Mahalingam, M.4    Kimball, S.R.5    Cooper, J.A.6
  • 72
    • 0032498112 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor eIF2B: Glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin
    • Welsh G.I., Miller C.M., Loughlin A.J., Price N.T., and Proud C.G. Regulation of eukaryotic initiation factor eIF2B: Glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin. FEBS Lett. 421 (1998) 125-130
    • (1998) FEBS Lett. , vol.421 , pp. 125-130
    • Welsh, G.I.1    Miller, C.M.2    Loughlin, A.J.3    Price, N.T.4    Proud, C.G.5
  • 73
    • 0032568921 scopus 로고    scopus 로고
    • Regulation of the p70 S6 kinase by phosphorylation in vivo: Analysis using site-specific anti-phosphopeptide antibodies
    • Weng Q.-P., Kozlowski M., Belham C., Zhang A., Comb M.J., and Avruch J. Regulation of the p70 S6 kinase by phosphorylation in vivo: Analysis using site-specific anti-phosphopeptide antibodies. J. Biol. Chem. 273 (1998) 16621-16629
    • (1998) J. Biol. Chem. , vol.273 , pp. 16621-16629
    • Weng, Q.-P.1    Kozlowski, M.2    Belham, C.3    Zhang, A.4    Comb, M.J.5    Avruch, J.6
  • 74
    • 0035816596 scopus 로고    scopus 로고
    • Characterization of the initiation factor eIF2B complex from mammalian cells as a GDP-dissociation stimulator protein
    • Williams D.D., Loughlin A.J., and Proud C.G. Characterization of the initiation factor eIF2B complex from mammalian cells as a GDP-dissociation stimulator protein. J. Biol. Chem. 276 (2001) 24697-24703
    • (2001) J. Biol. Chem. , vol.276 , pp. 24697-24703
    • Williams, D.D.1    Loughlin, A.J.2    Proud, C.G.3
  • 75
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S., Loewith R., and Hall M.N. TOR signaling in growth and metabolism. Cell 124 (2006) 471-484
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 76
    • 0035831516 scopus 로고    scopus 로고
    • Stress-induced inhibition of ERK1 and ERK2 by direct interaction with p38 MAP kinase
    • Zhang H., Shi X., Hampong M., Blanis L., and Pelech S. Stress-induced inhibition of ERK1 and ERK2 by direct interaction with p38 MAP kinase. J. Biol. Chem. 276 (2001) 6905-6908
    • (2001) J. Biol. Chem. , vol.276 , pp. 6905-6908
    • Zhang, H.1    Shi, X.2    Hampong, M.3    Blanis, L.4    Pelech, S.5


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