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Volumn 25, Issue 7, 2005, Pages 2558-2572

Distinct signaling events downstream of mTOR cooperate to mediate the effects of amino acids and insulin on initiation factor 4E-binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; INITIATION FACTOR 4E BINDING PROTEIN; INSULIN; MAMMALIAN TARGET OF RAPAMYCIN; RAPAMYCIN; S6 KINASE;

EID: 15044340650     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.7.2558-2572.2005     Document Type: Article
Times cited : (185)

References (78)
  • 1
    • 0035225023 scopus 로고    scopus 로고
    • The p70 S6 kinase integrates nutrient and growth signals to control translational capacity
    • Avruch, J., C. Belham, Q. Weng, K. Hara, and K. Yonezawa. 2001. The p70 S6 kinase integrates nutrient and growth signals to control translational capacity. Prog. Mol. Subcell. Biol. 26:115-154.
    • (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
  • 2
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia
    • Berra, E., E. Benizri, A. Ginouves, V. Volmat, D. Roux, and J. Pouyssegur. 2003. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia. EMBO J. 22:4082-4090.
    • (2003) EMBO J. , vol.22 , pp. 4082-4090
    • Berra, E.1    Benizri, E.2    Ginouves, A.3    Volmat, V.4    Roux, D.5    Pouyssegur, J.6
  • 3
    • 0142071830 scopus 로고    scopus 로고
    • The TOR-signaling and RAIP motifs play distinct roles in the mTOR-dependent phosphorylation of initiation factor 4E-binding protein 1 in vivo
    • Beugnet, A., X. Wang, and C. G. Proud. 2003. The TOR-signaling and RAIP motifs play distinct roles in the mTOR-dependent phosphorylation of initiation factor 4E-binding protein 1 in vivo. J. Biol. Chem. 278:40722.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40722
    • Beugnet, A.1    Wang, X.2    Proud, C.G.3
  • 4
    • 1642355123 scopus 로고    scopus 로고
    • A novel mTOR-regulated phosphorylation site in elongation factor 2 kinase modulates the activity of the kinase and its binding to calmodulin
    • Browne, G. J., and C. G. Proud. 2004. A novel mTOR-regulated phosphorylation site in elongation factor 2 kinase modulates the activity of the kinase and its binding to calmodulin. Mol. Cell. Biol. 24:2986-2997.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2986-2997
    • Browne, G.J.1    Proud, C.G.2
  • 6
    • 0029831167 scopus 로고    scopus 로고
    • Direct inhibition of the signalling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002
    • Brunn, G. J., J. Williams, C. Sabers, G. Weiderrecht, J. C. Lawrence, and R. T. Abraham. 1996. Direct inhibition of the signalling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002. EMBO J. 15:5256-5267.
    • (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
    • 0033429204 scopus 로고    scopus 로고
    • Nutrients differentially modulate multiple translation factors and their control by insulin
    • Campbell, L. E., X. Wang, and C. G. Proud. 1999. Nutrients differentially modulate multiple translation factors and their control by insulin. Biochem. J. 344:433-441.
    • (1999) Biochem. J. , vol.344 , pp. 433-441
    • Campbell, L.E.1    Wang, X.2    Proud, C.G.3
  • 9
    • 0038482156 scopus 로고    scopus 로고
    • Two motifs in the translational repressor PHAS-I required for efficient phosphorylation by mammalian target of rapamycin and for recognition by raptor
    • Choi, K.-M., L. P. McMahon, and J. C. Lawrence. 2003. Two motifs in the translational repressor PHAS-I required for efficient phosphorylation by mammalian target of rapamycin and for recognition by raptor. J. Biol. Chem. 278:19667-19673.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19667-19673
    • Choi, K.-M.1    McMahon, L.P.2    Lawrence, J.C.3
  • 10
    • 2342489456 scopus 로고    scopus 로고
    • eIF-4E expression and its role in malignancies and metastases
    • De Benedetti, A., and J. R. Graff. 2004. eIF-4E expression and its role in malignancies and metastases. Oncogene 23:3189-3199.
    • (2004) Oncogene , vol.23 , pp. 3189-3199
    • De Benedetti, A.1    Graff, J.R.2
  • 11
    • 0030013407 scopus 로고    scopus 로고
    • Both rapamycin-sensitive and -insensitive pathways are involved in the phosphorylation of the initiation factor 4E binding protein (4E-BP1) in response to insulin in rat epididymal fat cells
    • Diggle, T. A., S. K. Moule, M. B. Avison, A. Flynn, E. J. Foulstone, C. G. Proud, and R. M. Denton. 1996. Both rapamycin-sensitive and -insensitive pathways are involved in the phosphorylation of the initiation factor 4E binding protein (4E-BP1) in response to insulin in rat epididymal fat cells. Biochem. J. 316:447-453.
    • (1996) Biochem. J. , vol.316 , pp. 447-453
    • Diggle, T.A.1    Moule, S.K.2    Avison, M.B.3    Flynn, A.4    Foulstone, E.J.5    Proud, C.G.6    Denton, R.M.7
  • 12
    • 0346995280 scopus 로고    scopus 로고
    • Differential effects of rapamycin on mammalian target of rapamycin signaling functions in mammalian cells
    • Edinger, A. L., C. M. Linardic, G. G. Chiang, C. B. Thompson, and R. T. Abraham. 2003. Differential effects of rapamycin on mammalian target of rapamycin signaling functions in mammalian cells. Cancer Res. 63:8451-8460.
    • (2003) Cancer Res. , vol.63 , pp. 8451-8460
    • Edinger, A.L.1    Linardic, C.M.2    Chiang, G.G.3    Thompson, C.B.4    Abraham, R.T.5
  • 13
    • 0037452233 scopus 로고    scopus 로고
    • Drug-eluting stents in vascular intervention
    • Fattori, R., and T. Piva. 2003. Drug-eluting stents in vascular intervention. Lancet 361:247-249.
    • (2003) Lancet , vol.361 , pp. 247-249
    • Fattori, R.1    Piva, T.2
  • 14
    • 0348111466 scopus 로고    scopus 로고
    • Ser-64 and Ser-111 in PHAS-I are dispensable for insulin-stimulated dissociation from eIF4E
    • Ferguson, G., I. Mothe-Satney, and J. C. Lawrence, Jr. 2003. Ser-64 and Ser-111 in PHAS-I are dispensable for insulin-stimulated dissociation from eIF4E. J. Biol. Chem. 278:47459-47465.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47459-47465
    • Ferguson, G.1    Mothe-Satney, I.2    Lawrence Jr., J.C.3
  • 15
    • 0027228165 scopus 로고
    • The immunosuppressant rapamycin induces inactivation of p70s6k through dephosphorylation of a novel set of sites
    • Ferrari, S., R. B. Pearson, M. Siegmann, S. C. Kozma, and G. Thomas. 1993. The immunosuppressant rapamycin induces inactivation of p70s6k through dephosphorylation of a novel set of sites. J. Biol. Chem. 268:16091-16094.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16091-16094
    • Ferrari, S.1    Pearson, R.B.2    Siegmann, M.3    Kozma, S.C.4    Thomas, G.5
  • 16
    • 2342545519 scopus 로고    scopus 로고
    • Target of rapamycin (TOR): An integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression
    • Fingar, D. C., and J. Blenis. 2004. Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression. Oncogene 23:3151-3171.
    • (2004) Oncogene , vol.23 , pp. 3151-3171
    • Fingar, D.C.1    Blenis, J.2
  • 17
    • 0345732640 scopus 로고    scopus 로고
    • mTOR controls cell cycle progression through its cell growth effectors S6K1 and 4E-BP1/eukaryotic translation initiation factor 4E
    • Fingar, D. C., C. J. Richardson, A. R. Tee, L. Cheatham, C. Tsou, and J. Blenis. 2004. mTOR controls cell cycle progression through its cell growth effectors S6K1 and 4E-BP1/eukaryotic translation initiation factor 4E. Mol. Cell. Biol. 24:200-216.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 200-216
    • Fingar, D.C.1    Richardson, C.J.2    Tee, A.R.3    Cheatham, L.4    Tsou, C.5    Blenis, J.6
  • 19
    • 0031730304 scopus 로고    scopus 로고
    • Amino acid effects on translational repressor 4E-BP1 are mediated primarily by L-leucine in isolated adipocytes
    • Fox, H. L., P. T. Pham, S. R. Kimball, L. S. Jefferson, and C. J. Lynch. 1998. Amino acid effects on translational repressor 4E-BP1 are mediated primarily by L-leucine in isolated adipocytes. Am. J. Physiol. 44:C1232-C1238.
    • (1998) Am. J. Physiol. , vol.44
    • Fox, H.L.1    Pham, P.T.2    Kimball, S.R.3    Jefferson, L.S.4    Lynch, C.J.5
  • 23
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras, A.-C., B. Raught, and N. Sonenberg. 2001. Regulation of translation initiation by FRAP/mTOR. Genes Dev. 15:807-826.
    • (2001) Genes Dev. , vol.15 , pp. 807-826
    • Gingras, A.-C.1    Raught, B.2    Sonenberg, N.3
  • 24
    • 0347281686 scopus 로고    scopus 로고
    • Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E
    • Gross, J. D., N. J. Moerke, H. T. von der, A. A. Lugovskoy, A. B. Sachs, J. E. McCarthy, and G. Wagner. 2003. Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E. Cell 115:739-750.
    • (2003) Cell , vol.115 , pp. 739-750
    • Gross, J.D.1    Moerke, N.J.2    Von Der, H.T.3    Lugovskoy, A.A.4    Sachs, A.B.5    McCarthy, J.E.6    Wagner, G.7
  • 27
    • 0032486268 scopus 로고    scopus 로고
    • Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF4E BP1 through a common effector mechanism
    • Hara, K., K. Yonezawa, Q.-P. Weng, M. T. Kozlowski, C. Belham, and J. Avruch. 1998. Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF4E BP1 through a common effector mechanism. J. Biol. Chem. 273:14484-14494.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14484-14494
    • Hara, K.1    Yonezawa, K.2    Weng, Q.-P.3    Kozlowski, M.T.4    Belham, C.5    Avruch, J.6
  • 29
    • 0027936088 scopus 로고
    • Phosphorylation of PHAS-I by MAP kinase. Identification of a site phosphorylated by MAP kinase in vitro and in response to insulin in rat adipocytes
    • Haystead, T. A. J., C. M. M. Haystead, C. Hu, T. A. Lin, and J. C. Lawrence. 1994. Phosphorylation of PHAS-I by MAP kinase. Identification of a site phosphorylated by MAP kinase in vitro and in response to insulin in rat adipocytes. J. Biol. Chem. 269:23185-23191.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23185-23191
    • Haystead, T.A.J.1    Haystead, C.M.M.2    Hu, C.3    Lin, T.A.4    Lawrence, J.C.5
  • 30
    • 0028137771 scopus 로고
    • TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast
    • Helliwell, S. B., P. Wagner, J. Kunz, M. Deuter-Reinhard, R. Henriquez, and M. N. Hall. 1994. TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast. Mol. Biol. Cell 5:105-118.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 105-118
    • Helliwell, S.B.1    Wagner, P.2    Kunz, J.3    Deuter-Reinhard, M.4    Henriquez, R.5    Hall, M.N.6
  • 31
    • 0034646657 scopus 로고    scopus 로고
    • Distinct signalling pathways mediate insulin and phorbol ester-stimulated eIF4F assembly and protein synthesis in HEK 293 cells
    • Herbert, T. P., G. R. Kilhams, I. H. Batty, and C. G. Proud. 2000. Distinct signalling pathways mediate insulin and phorbol ester-stimulated eIF4F 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
  • 32
    • 0037192868 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase pathway regulates the phosphorylation of 4E-BP1 at multiple sites
    • Herbert, T. P., A. R. Tee, and C. G. Proud. 2002. The extracellular signal-regulated kinase pathway regulates the phosphorylation of 4E-BP1 at multiple sites. J. Biol. Chem. 277:11591-11596.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11591-11596
    • Herbert, T.P.1    Tee, A.R.2    Proud, C.G.3
  • 34
    • 0043127125 scopus 로고    scopus 로고
    • Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
    • Inoki, K., Y. Li, T. Xu, and K. L. Guan. 2003. Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Dev. 17:1829-1834.
    • (2003) Genes Dev. , vol.17 , pp. 1829-1834
    • Inoki, K.1    Li, Y.2    Xu, T.3    Guan, K.L.4
  • 35
    • 7944235758 scopus 로고    scopus 로고
    • Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
    • Jacinto, E., R. Loewith, A. Schmidt, S. Lin, M. A. Ruegg, A. Hall, and M. N. Hall. 2004. Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat. Cell Biol. 6:1122-1128.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1122-1128
    • Jacinto, E.1    Loewith, R.2    Schmidt, A.3    Lin, S.4    Ruegg, M.A.5    Hall, A.6    Hall, M.N.7
  • 36
    • 0037623417 scopus 로고    scopus 로고
    • GβL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR
    • Kim, D. H., D. Sarbassov, S. M. Ali, R. R. Latek, K. V. Guntur, H. Erdjument-Bromage, P. Tempst, and D. Sabatini. 2002. GβL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR. Mol. Cell 11:895-904.
    • (2002) Mol. Cell , vol.11 , pp. 895-904
    • Kim, D.H.1    Sarbassov, D.2    Ali, S.M.3    Latek, R.R.4    Guntur, K.V.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.8
  • 37
  • 38
    • 4644252994 scopus 로고    scopus 로고
    • Human cytomegalovirus infection induces rapamycin-insensitive phosphorylation of downstream effectors of mTOR kinase
    • Kudchodkar, S. B., Y. Yu, T. G. Maguire, and J. C. Alwine. 2004. Human cytomegalovirus infection induces rapamycin-insensitive phosphorylation of downstream effectors of mTOR kinase. J. Virol. 78:11030-11039.
    • (2004) J. Virol. , vol.78 , pp. 11030-11039
    • Kudchodkar, S.B.1    Yu, Y.2    Maguire, T.G.3    Alwine, J.C.4
  • 39
    • 0027311858 scopus 로고
    • Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression
    • Kunz, J., R. Henriquez, U. Schneider, M. Deuter-Reinhard, N. R. Movva, and M. N. Hall. 1993. Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression. Cell 73:585-596.
    • (1993) Cell , vol.73 , pp. 585-596
    • Kunz, J.1    Henriquez, R.2    Schneider, U.3    Deuter-Reinhard, M.4    Movva, N.R.5    Hall, M.N.6
  • 40
    • 0041758428 scopus 로고    scopus 로고
    • Tuberous sclerosis: From tubers to mTOR
    • Kwiatkowski, D. J. 2003. Tuberous sclerosis: from tubers to mTOR. Ann. Hum. Genet. 67:87-96.
    • (2003) Ann. Hum. Genet. , vol.67 , pp. 87-96
    • Kwiatkowski, D.J.1
  • 41
    • 0030883848 scopus 로고    scopus 로고
    • PHAS/4E-BPs as regulators of mRNA translation and cell proliferation
    • Lawrence, J. C., and R. T. Abraham. 1997. PHAS/4E-BPs as regulators of mRNA translation and cell proliferation. Trends Biochem. Sci. 22:345-349.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 345-349
    • Lawrence, J.C.1    Abraham, R.T.2
  • 42
    • 0034654298 scopus 로고    scopus 로고
    • Analysis of the cellular functions of PTEN using catalytic domain and C-terminal mutations: Differential effects of C-terminal deletion on signalling pathways downstream of phosphoinositide 3-kinase
    • Leslie, N. R., A. Gray, I. Pass, E. A. Orchiston, and C. P. Downes. 2000. Analysis of the cellular functions of PTEN using catalytic domain and C-terminal mutations: differential effects of C-terminal deletion on signalling pathways downstream of phosphoinositide 3-kinase. Biochem. J. 346(Pt. 3):827-833.
    • (2000) Biochem. J. , vol.346 , Issue.3 PART , pp. 827-833
    • Leslie, N.R.1    Gray, A.2    Pass, I.3    Orchiston, E.A.4    Downes, C.P.5
  • 43
    • 0029912854 scopus 로고    scopus 로고
    • Control of the translational regulators PHAS-I and PHAS-II by insulin and cAMP in 3T3-L1 adipocytes
    • Lin, T. A., and J. C. Lawrence. 1996. Control of the translational regulators PHAS-I and PHAS-II by insulin and cAMP in 3T3-L1 adipocytes. J. Biol. Chem. 271:30199-30204.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30199-30204
    • Lin, T.A.1    Lawrence, J.C.2
  • 45
    • 0037623422 scopus 로고    scopus 로고
    • Rapamycin in combination with cyclosporine or tacrolimus in liver, pancreas, and kidney transplantation
    • MacDonald, A. S. 2003. Rapamycin in combination with cyclosporine or tacrolimus in liver, pancreas, and kidney transplantation. Transplant. Proc. 35:201S-208S.
    • (2003) Transplant. Proc. , vol.35
    • MacDonald, A.S.1
  • 47
    • 0347716759 scopus 로고    scopus 로고
    • Rheb fills a GAP between TSC and TOR
    • Manning, B. D., and L. C. Cantley. 2003. Rheb fills a GAP between TSC and TOR. Trends Biochem. Sci. 28:573-576.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 573-576
    • Manning, B.D.1    Cantley, L.C.2
  • 48
    • 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., A. R. Tee, M. N. Logsdon, J. Blenis, and L. C. Cantley. 2002. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol. Cell 10:151-162.
    • (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
  • 49
    • 0036837863 scopus 로고    scopus 로고
    • The rapamycin-binding domain governs substrate selectivity by the mammalian target of rapamycin
    • McMahon, L. P., K. M. Choi, T. A. Lin, R. T. Abraham, and J. C. Lawrence, Jr. 2002. The rapamycin-binding domain governs substrate selectivity by the mammalian target of rapamycin. Mol. Cell. Biol. 22:7428-7438.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7428-7438
    • McMahon, L.P.1    Choi, K.M.2    Lin, T.A.3    Abraham, R.T.4    Lawrence Jr., J.C.5
  • 50
    • 0036712741 scopus 로고    scopus 로고
    • TSC1-TSC2: A complex tale of PKB-mediated S6K regulation
    • McManus, E. J., and D. R. Alessi. 2002. TSC1-TSC2: a complex tale of PKB-mediated S6K regulation. Nat. Cell Biol. 4:E214-E216.
    • (2002) Nat. Cell Biol. , vol.4
    • McManus, E.J.1    Alessi, D.R.2
  • 51
    • 0034721874 scopus 로고    scopus 로고
    • Mammalian target of rapamycin-dependent phosphorylation of PHAS-1 in four (S/T)P sites detected by phospho-specific antibodies
    • Mothe-Satney, I., G. J. Brunn, L. P. McMahon, C. T. Capaldo, R. T. Abraham, and J. C. Lawrence. 2000. Mammalian target of rapamycin-dependent phosphorylation of PHAS-1 in four (S/T)P sites detected by phospho-specific antibodies. J. Biol. Chem. 275:33836-33843.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33836-33843
    • Mothe-Satney, I.1    Brunn, G.J.2    McMahon, L.P.3    Capaldo, C.T.4    Abraham, R.T.5    Lawrence, J.C.6
  • 52
    • 0034057277 scopus 로고    scopus 로고
    • Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression
    • Mothe-Satney, I., D. Yang, P. T. Fadden, A. J. Haystead, and J. C. Lawrence. 2000. Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression. Mol. Cell. Biol. 20:3558-3567.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3558-3567
    • Mothe-Satney, I.1    Yang, D.2    Fadden, P.T.3    Haystead, A.J.4    Lawrence, J.C.5
  • 57
    • 0035447688 scopus 로고    scopus 로고
    • Glucose exerts a permissive effect on the regulation of the initiation factor 4E binding protein 4E-BP1
    • Patel, J., X. Wang, and C. G. Proud. 2001. Glucose exerts a permissive effect on the regulation of the initiation factor 4E binding protein 4E-BP1. Biochem. J. 358:497-503.
    • (2001) Biochem. J. , vol.358 , pp. 497-503
    • Patel, J.1    Wang, X.2    Proud, C.G.3
  • 58
    • 0034629365 scopus 로고    scopus 로고
    • FKBP12-rapamycin-associated protein (FRAP) autophosphorylates at serine 2481 under translationally repressive conditions
    • Peterson, R. T., P. A. Beal, M. J. Comb, and S. L. Schreiber. 2000. FKBP12-rapamycin-associated protein (FRAP) autophosphorylates at serine 2481 under translationally repressive conditions. J. Biol. Chem. 275:7416-7423.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7416-7423
    • Peterson, R.T.1    Beal, P.A.2    Comb, M.J.3    Schreiber, S.L.4
  • 59
    • 0024338805 scopus 로고
    • The two forms of the beta-subunit of initiation factor-2 from reticulocyte lysates arise from proteolytic degradation
    • Price, N. T., S. F. Nakielny, S. J. Clark, and C. G. Proud. 1989. The two forms of the beta-subunit of initiation factor-2 from reticulocyte lysates arise from proteolytic degradation. Biochim. Biophys. Acta 1008:177-182.
    • (1989) Biochim. Biophys. Acta , vol.1008 , pp. 177-182
    • Price, N.T.1    Nakielny, S.F.2    Clark, S.J.3    Proud, C.G.4
  • 60
    • 0036440779 scopus 로고    scopus 로고
    • Regulation of mammalian translation factors by nutrients
    • Proud, C. G. 2002. Regulation of mammalian translation factors by nutrients. Eur. J. Biochem. 269:5338-5349.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5338-5349
    • Proud, C.G.1
  • 61
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
    • Sarbassov, D., S. M. Ali, D. H. Kim, D. A. Guertin, R. R. Latek, H. Erdjument-Bromage, P. Tempst, and D. M. Sabatini. 2004. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr. Biol. 14:1296-1302.
    • (2004) Curr. Biol. , vol.14 , pp. 1296-1302
    • Sarbassov, D.1    Ali, S.M.2    Kim, D.H.3    Guertin, D.A.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 62
    • 0037117409 scopus 로고    scopus 로고
    • Identification of a conserved motif required for mTOR signaling
    • Schalm, S. S., and J. Blenis. 2002. Identification of a conserved motif required for mTOR signaling. Curr. Biol. 12:632-639.
    • (2002) Curr. Biol. , vol.12 , pp. 632-639
    • Schalm, S.S.1    Blenis, J.2
  • 63
    • 0037718389 scopus 로고    scopus 로고
    • TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation and function
    • Schalm, S. S., D. C. Fingar, D. M. Sabatini, and J. Blenis. 2003. TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation and function. Curr. Biol. 13:797-806.
    • (2003) Curr. Biol. , vol.13 , pp. 797-806
    • Schalm, S.S.1    Fingar, D.C.2    Sabatini, D.M.3    Blenis, J.4
  • 64
    • 0027647714 scopus 로고
    • Use of nonreducing SDS-PAGE for monitoring renaturation of recombinant protein synthesis initiation factor, eIF-4 alpha
    • Stern, B. D., M. Wilson, and R. Jagus. 1993. Use of nonreducing SDS-PAGE for monitoring renaturation of recombinant protein synthesis initiation factor, eIF-4 alpha. Protein Expr. Purif. 4:320-327.
    • (1993) Protein Expr. Purif. , vol.4 , pp. 320-327
    • Stern, B.D.1    Wilson, M.2    Jagus, R.3
  • 65
    • 0033833810 scopus 로고    scopus 로고
    • Carboxyl-terminal region conserved among phosphoinositide-kinase-related kinases is indispensable for mTOR function in vivo and in vitro
    • Takahashi, T., K. Hara, H. Inoue, Y. Kawa, C. Tokunaga, S. Hidayat, K. Yoshino, Y. Kuroda, and K. Yonezawa. 2000. Carboxyl-terminal region conserved among phosphoinositide-kinase-related kinases is indispensable for mTOR function in vivo and in vitro. Genes Cells 5:765-775.
    • (2000) Genes Cells , vol.5 , pp. 765-775
    • Takahashi, T.1    Hara, K.2    Inoue, H.3    Kawa, Y.4    Tokunaga, C.5    Hidayat, S.6    Yoshino, K.7    Kuroda, Y.8    Yonezawa, K.9
  • 66
    • 0042326762 scopus 로고    scopus 로고
    • Muscarinic receptor-mediated activation of p70 S6 kinase 1 (S6K1) in 1321N1 astrocytoma cells: Permissive role of phosphoinositide 3-kinase
    • Tang, X., L. Wang, C. G. Proud, and C. P. Downes. 2003. Muscarinic receptor-mediated activation of p70 S6 kinase 1 (S6K1) in 1321N1 astrocytoma cells: permissive role of phosphoinositide 3-kinase. Biochem. J. 374:137-143.
    • (2003) Biochem. J. , vol.374 , pp. 137-143
    • Tang, X.1    Wang, L.2    Proud, C.G.3    Downes, C.P.4
  • 67
    • 0037108750 scopus 로고    scopus 로고
    • Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling
    • Tee, A. R., D. C. Fingar, B. D. Manning, D. J. Kwiatkowski, L. C. Cantley, and J. Blenis. 2002. Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling. Proc. Natl. Acad. Sci. USA 99:13571-13576.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13571-13576
    • Tee, A.R.1    Fingar, D.C.2    Manning, B.D.3    Kwiatkowski, D.J.4    Cantley, L.C.5    Blenis, J.6
  • 68
    • 0042701991 scopus 로고    scopus 로고
    • Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb
    • Tee, A. R., B. D. Manning, P. P. Roux, L. C. Cantley, and J. Blenis. 2003. Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr. Biol. 13:1259-1268.
    • (2003) Curr. Biol. , vol.13 , pp. 1259-1268
    • Tee, A.R.1    Manning, B.D.2    Roux, P.P.3    Cantley, L.C.4    Blenis, J.5
  • 69
    • 0034659730 scopus 로고    scopus 로고
    • DNA damage causes inactivation of translational regulators linked to mTOR signalling
    • Tee, A. R., and C. G. Proud. 2000. DNA damage causes inactivation of translational regulators linked to mTOR signalling. Oncogene 19:3021-3031.
    • (2000) Oncogene , vol.19 , pp. 3021-3031
    • Tee, A.R.1    Proud, C.G.2
  • 70
    • 0036181011 scopus 로고    scopus 로고
    • Caspase cleavage of initiation factor 4E-binding protein 1 yields a dominant inhibitor of cap-dependent translation and reveals a novel regulatory motif
    • Tee, A. R., and C. G. Proud. 2002. Caspase cleavage of initiation factor 4E-binding protein 1 yields a dominant inhibitor of cap-dependent translation and reveals a novel regulatory motif. Mol. Cell. Biol. 22:1674-1683.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1674-1683
    • Tee, A.R.1    Proud, C.G.2
  • 71
    • 0036842351 scopus 로고    scopus 로고
    • Ras/Erk signalling is required for regulation of translation factors linked to mTOR and protein synthesis by hypertrophic agents in cardiomyocytes
    • Wang, L., and C. G. Proud. 2002. Ras/Erk signalling is required for regulation of translation factors linked to mTOR and protein synthesis by hypertrophic agents in cardiomyocytes. Circ. Res. 91:821-829.
    • (2002) Circ. Res. , vol.91 , pp. 821-829
    • Wang, L.1    Proud, C.G.2
  • 72
    • 0032528917 scopus 로고    scopus 로고
    • Amino acid availability regulates p70 S6 kinase and multiple translation factors
    • Wang, X., L. E. Campbell, C. M. Miller, and C. G. Proud. 1998. Amino acid availability regulates p70 S6 kinase and multiple translation factors. Biochem. J. 334:261-267.
    • (1998) Biochem. J. , vol.334 , pp. 261-267
    • Wang, X.1    Campbell, L.E.2    Miller, C.M.3    Proud, C.G.4
  • 73
    • 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., W. Li, J.-L. Parra, A. Beugnet, and C. G. Proud. 2003. The C-terminus of initiation factor 4E-binding protein 1 contains multiple regulatory features that influence its function and phosphorylation. Mol. Cell. Biol. 23:1546-1557.
    • (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
  • 74
    • 0032785426 scopus 로고    scopus 로고
    • Mutational analysis of sites in the translational regulator, PHAS-I, that are selectively phosphorylated by mTOR
    • Yang, D., G. J. Brunn, and J. C. Lawrence. 1999. Mutational analysis of sites in the translational regulator, PHAS-I, that are selectively phosphorylated by mTOR. FEBS Lett. 453:387-390.
    • (1999) FEBS Lett. , vol.453 , pp. 387-390
    • Yang, D.1    Brunn, G.J.2    Lawrence, J.C.3
  • 76
    • 0029071264 scopus 로고
    • TOR kinase domains are required for two distinct functions, only one of which is inhibited by rapamycin
    • Zheng, X. F., D. Florentino, J. Chen, G. R. Crabtree, and S. L. Schreiber. 1995. TOR kinase domains are required for two distinct functions, only one of which is inhibited by rapamycin. Cell 82:121-130.
    • (1995) Cell , vol.82 , pp. 121-130
    • Zheng, X.F.1    Florentino, D.2    Chen, J.3    Crabtree, G.R.4    Schreiber, S.L.5
  • 77
    • 0034654174 scopus 로고    scopus 로고
    • Modulation of hypoxia-inducible factor 1α expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: Implications for tumor angiogenesis and therapeutics
    • Zhong, H., K. Chiles, D. Feldser, E. Laughner, C. Hanrahan, M. M. Georgescu, J. W. Simons, and G. L. Semenza. 2000. Modulation of hypoxia-inducible factor 1α expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: implications for tumor angiogenesis and therapeutics. Cancer Res. 60:1541-1545.
    • (2000) Cancer Res. , vol.60 , pp. 1541-1545
    • Zhong, H.1    Chiles, K.2    Feldser, D.3    Laughner, E.4    Hanrahan, C.5    Georgescu, M.M.6    Simons, J.W.7    Semenza, G.L.8
  • 78
    • 0032738763 scopus 로고    scopus 로고
    • Rapamycin inhibits hepatic stellate cell proliferation in vitro and limits fibrogenesis in an in vivo model of liver fibrosis
    • Zhu, J., J. Wu, E. Frizell, S. L. Liu, R. Bashey, R. Rubin, P. Norton, and M. A. Zern. 1999. Rapamycin inhibits hepatic stellate cell proliferation in vitro and limits fibrogenesis in an in vivo model of liver fibrosis. Gastroenterology 117:1198-1204.
    • (1999) Gastroenterology , vol.117 , pp. 1198-1204
    • Zhu, J.1    Wu, J.2    Frizell, E.3    Liu, S.L.4    Bashey, R.5    Rubin, R.6    Norton, P.7    Zern, M.A.8


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