메뉴 건너뛰기




Volumn 12, Issue 4, 2007, Pages 487-502

The Two TORCs and Akt

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC GMP DEPENDENT PROTEIN KINASE; FK 506 BINDING PROTEIN; GROWTH FACTOR; INITIATION FACTOR 4E BINDING PROTEIN 1; PHOSPHATIDYLINOSITOL KINASE; PROTEIN KINASE B; PROTEIN KINASE C; PROTEIN SERINE KINASE; PROTEIN TORC1; PROTEIN TORC2; RAPAMYCIN; TARGET OF RAPAMYCIN KINASE; THREONINE; UNCLASSIFIED DRUG;

EID: 34047095297     PISSN: 15345807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.devcel.2007.03.020     Document Type: Review
Times cited : (707)

References (154)
  • 2
    • 0347065349 scopus 로고    scopus 로고
    • Cell cycle-regulated phosphorylation of hamartin, the product of the tuberous sclerosis complex 1 gene, by cyclin-dependent kinase 1/cyclin B
    • Astrinidis A., Senapedis W., Coleman T.R., and Henske E.P. Cell cycle-regulated phosphorylation of hamartin, the product of the tuberous sclerosis complex 1 gene, by cyclin-dependent kinase 1/cyclin B. J. Biol. Chem. 278 (2003) 51372-51379
    • (2003) J. Biol. Chem. , vol.278 , pp. 51372-51379
    • Astrinidis, A.1    Senapedis, W.2    Coleman, T.R.3    Henske, E.P.4
  • 5
    • 2942518250 scopus 로고    scopus 로고
    • Lost in translation: dysregulation of cap-dependent translation and cancer
    • Bjornsti M.A., and Houghton P.J. Lost in translation: dysregulation of cap-dependent translation and cancer. Cancer Cell 5 (2004) 519-523
    • (2004) Cancer Cell , vol.5 , pp. 519-523
    • Bjornsti, M.A.1    Houghton, P.J.2
  • 8
    • 0033515625 scopus 로고    scopus 로고
    • A human protein kinase Bγ with regulatory phosphorylation sites in the activation loop and in the C-terminal hydrophobic domain
    • Brodbeck D., Cron P., and Hemmings B.A. A human protein kinase Bγ with regulatory phosphorylation sites in the activation loop and in the C-terminal hydrophobic domain. J. Biol. Chem. 274 (1999) 9133-9136
    • (1999) J. Biol. Chem. , vol.274 , pp. 9133-9136
    • Brodbeck, D.1    Cron, P.2    Hemmings, B.A.3
  • 10
    • 33646143793 scopus 로고    scopus 로고
    • Localization of Rheb to the endomembrane is critical for its signaling function
    • Buerger C., DeVries B., and Stambolic V. Localization of Rheb to the endomembrane is critical for its signaling function. Biochem. Biophys. Res. Commun. 344 (2006) 869-880
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 869-880
    • Buerger, C.1    DeVries, B.2    Stambolic, V.3
  • 11
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering B.M., and Coffer P.J. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376 (1995) 599-602
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.1    Coffer, P.J.2
  • 12
    • 25444457577 scopus 로고    scopus 로고
    • hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase
    • Byfield M.P., Murray J.T., and Backer J.M. hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase. J. Biol. Chem. 280 (2005) 33076-33082
    • (2005) J. Biol. Chem. , vol.280 , pp. 33076-33082
    • Byfield, M.P.1    Murray, J.T.2    Backer, J.M.3
  • 13
    • 0033551070 scopus 로고    scopus 로고
    • New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway
    • Cantley L.C., and Neel B.G. New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc. Natl. Acad. Sci. USA 96 (1999) 4240-4245
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4240-4245
    • Cantley, L.C.1    Neel, B.G.2
  • 14
    • 0041356888 scopus 로고    scopus 로고
    • Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner
    • Castro A.F., Rebhun J.F., Clark G.J., and Quilliam L.A. Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner. J. Biol. Chem. 278 (2003) 32493-32496
    • (2003) J. Biol. Chem. , vol.278 , pp. 32493-32496
    • Castro, A.F.1    Rebhun, J.F.2    Clark, G.J.3    Quilliam, L.A.4
  • 18
    • 0001457668 scopus 로고    scopus 로고
    • Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA
    • Cheng J.Q., Ruggeri B., Klein W.M., Sonoda G., Altomare D.A., Watson D.K., and Testa J.R. Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA. Proc. Natl. Acad. Sci. USA 93 (1996) 3636-3641
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3636-3641
    • Cheng, J.Q.1    Ruggeri, B.2    Klein, W.M.3    Sonoda, G.4    Altomare, D.A.5    Watson, D.K.6    Testa, J.R.7
  • 19
    • 21744434031 scopus 로고    scopus 로고
    • Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation
    • Cheng J., Zhang D., Kim K., Zhao Y., and Su B. Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation. Mol. Cell. Biol. 25 (2005) 5955-5964
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5955-5964
    • Cheng, J.1    Zhang, D.2    Kim, K.3    Zhao, Y.4    Su, B.5
  • 21
    • 0035914388 scopus 로고    scopus 로고
    • Akt1/PKBalpha is required for normal growth but dispensable for maintenance of glucose homeostasis in mice
    • Cho H., Thorvaldsen J.L., Chu Q., Feng F., and Birnbaum M.J. Akt1/PKBalpha is required for normal growth but dispensable for maintenance of glucose homeostasis in mice. J. Biol. Chem. 276 (2001) 38349-38352
    • (2001) J. Biol. Chem. , vol.276 , pp. 38349-38352
    • Cho, H.1    Thorvaldsen, J.L.2    Chu, Q.3    Feng, F.4    Birnbaum, M.J.5
  • 22
    • 3042818799 scopus 로고    scopus 로고
    • Regulation of the TSC pathway by LKB1: evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome
    • Corradetti M.N., Inoki K., Bardeesy N., DePinho R.A., and Guan K.L. Regulation of the TSC pathway by LKB1: evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome. Genes Dev. 18 (2004) 1533-1538
    • (2004) Genes Dev. , vol.18 , pp. 1533-1538
    • Corradetti, M.N.1    Inoki, K.2    Bardeesy, N.3    DePinho, R.A.4    Guan, K.L.5
  • 23
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross D.A., Alessi D.R., Cohen P., Andjelkovich M., and Hemmings B.A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378 (1995) 785-789
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 24
    • 20144362478 scopus 로고    scopus 로고
    • The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability
    • Dames S.A., Mulet J.M., Rathgeb-Szabo K., Hall M.N., and Grzesiek S. The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability. J. Biol. Chem. 280 (2005) 20558-20564
    • (2005) J. Biol. Chem. , vol.280 , pp. 20558-20564
    • Dames, S.A.1    Mulet, J.M.2    Rathgeb-Szabo, K.3    Hall, M.N.4    Grzesiek, S.5
  • 25
    • 0033044355 scopus 로고    scopus 로고
    • eIF4E expression in tumors: its possible role in progression of malignancies
    • De Benedetti A., and Harris A.L. eIF4E expression in tumors: its possible role in progression of malignancies. Int. J. Biochem. Cell Biol. 31 (1999) 59-72
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 59-72
    • De Benedetti, A.1    Harris, A.L.2
  • 27
    • 0031870959 scopus 로고    scopus 로고
    • Pten is essential for embryonic development and tumour suppression
    • Di Cristofano A., Pesce B., Cordon-Cardo C., and Pandolfi P.P. Pten is essential for embryonic development and tumour suppression. Nat. Genet. 19 (1998) 348-355
    • (1998) Nat. Genet. , vol.19 , pp. 348-355
    • Di Cristofano, A.1    Pesce, B.2    Cordon-Cardo, C.3    Pandolfi, P.P.4
  • 28
    • 5444233787 scopus 로고    scopus 로고
    • Tsc2 is not a critical target of Akt during normal Drosophila development
    • Dong J., and Pan D. Tsc2 is not a critical target of Akt during normal Drosophila development. Genes Dev. 18 (2004) 2479-2484
    • (2004) Genes Dev. , vol.18 , pp. 2479-2484
    • Dong, J.1    Pan, D.2
  • 30
    • 0037264633 scopus 로고    scopus 로고
    • Targeting RAS signalling pathways in cancer therapy
    • Downward J. Targeting RAS signalling pathways in cancer therapy. Nat. Rev. Cancer 3 (2003) 11-22
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 11-22
    • Downward, J.1
  • 31
    • 0346422440 scopus 로고    scopus 로고
    • FKBP12-rapamycin-associated protein or mammalian target of rapamycin (FRAP/mTOR) localization in the endoplasmic reticulum and the Golgi apparatus
    • Drenan R.M., Liu X., Bertram P.G., and Zheng X.F. FKBP12-rapamycin-associated protein or mammalian target of rapamycin (FRAP/mTOR) localization in the endoplasmic reticulum and the Golgi apparatus. J. Biol. Chem. 279 (2004) 772-778
    • (2004) J. Biol. Chem. , vol.279 , pp. 772-778
    • Drenan, R.M.1    Liu, X.2    Bertram, P.G.3    Zheng, X.F.4
  • 32
    • 0038242819 scopus 로고    scopus 로고
    • TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver
    • Du K., Herzig S., Kulkarni R.N., and Montminy M. TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver. Science 300 (2003) 1574-1577
    • (2003) Science , vol.300 , pp. 1574-1577
    • Du, K.1    Herzig, S.2    Kulkarni, R.N.3    Montminy, M.4
  • 33
    • 33750380920 scopus 로고    scopus 로고
    • Life with a single isoform of Akt: mice lacking Akt2 and Akt3 are viable but display impaired glucose homeostasis and growth deficiencies
    • Dummler B., Tschopp O., Hynx D., Yang Z.Z., Dirnhofer S., and Hemmings B.A. Life with a single isoform of Akt: mice lacking Akt2 and Akt3 are viable but display impaired glucose homeostasis and growth deficiencies. Mol. Cell. Biol. 26 (2006) 8042-8051
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8042-8051
    • Dummler, B.1    Tschopp, O.2    Hynx, D.3    Yang, Z.Z.4    Dirnhofer, S.5    Hemmings, B.A.6
  • 34
    • 33750072949 scopus 로고    scopus 로고
    • mTOR and cancer therapy
    • Easton J.B., and Houghton P.J. mTOR and cancer therapy. Oncogene 25 (2006) 6436-6446
    • (2006) Oncogene , vol.25 , pp. 6436-6446
    • Easton, J.B.1    Houghton, P.J.2
  • 36
    • 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 Blenis J. Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression. Oncogene 23 (2004) 3151-3171
    • (2004) Oncogene , vol.23 , pp. 3151-3171
    • Fingar, D.C.1    Blenis, J.2
  • 37
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke T.F., Yang S., Chan T.O., Datta K., Kazlauskas A., Morrison D.K., Kaplan D.R., and Tsichlis P.N. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81 (1995) 727-736
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6    Kaplan, D.R.7    Tsichlis, P.N.8
  • 40
    • 15944406764 scopus 로고    scopus 로고
    • PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth
    • Gao T., Furnari F., and Newton A.C. PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth. Mol. Cell 18 (2005) 13-24
    • (2005) Mol. Cell , vol.18 , pp. 13-24
    • Gao, T.1    Furnari, F.2    Newton, A.C.3
  • 43
    • 0032520009 scopus 로고    scopus 로고
    • 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway
    • Gingras A.C., Kennedy S.G., O'Leary M.A., Sonenberg N., and Hay N. 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway. Genes Dev. 12 (1998) 502-513
    • (1998) Genes Dev. , vol.12 , pp. 502-513
    • Gingras, A.C.1    Kennedy, S.G.2    O'Leary, M.A.3    Sonenberg, N.4    Hay, N.5
  • 44
    • 0036479747 scopus 로고    scopus 로고
    • Roles of ERBB family receptor tyrosine kinases, and downstream signaling pathways, in the control of cell growth and survival
    • Grant S., Qiao L., and Dent P. Roles of ERBB family receptor tyrosine kinases, and downstream signaling pathways, in the control of cell growth and survival. Front. Biosci. 7 (2002) d376-d389
    • (2002) Front. Biosci. , vol.7
    • Grant, S.1    Qiao, L.2    Dent, P.3
  • 45
    • 27844497945 scopus 로고    scopus 로고
    • FOXO transcription factors at the interface between longevity and tumor suppression
    • Greer E.L., and Brunet A. FOXO transcription factors at the interface between longevity and tumor suppression. Oncogene 24 (2005) 7410-7425
    • (2005) Oncogene , vol.24 , pp. 7410-7425
    • Greer, E.L.1    Brunet, A.2
  • 46
    • 33751348056 scopus 로고    scopus 로고
    • Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCα, but not S6K1
    • Guertin D.A., Stevens D.M., Thoreen C.C., Burds A.A., Kalaany N.Y., Moffat J., Brown M., Fitzgerald K.J., and Sabatini D.M. Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCα, but not S6K1. Dev. Cell 11 (2006) 859-871
    • (2006) Dev. Cell , vol.11 , pp. 859-871
    • Guertin, D.A.1    Stevens, D.M.2    Thoreen, C.C.3    Burds, A.A.4    Kalaany, N.Y.5    Moffat, J.6    Brown, M.7    Fitzgerald, K.J.8    Sabatini, D.M.9
  • 47
  • 48
    • 0041821493 scopus 로고    scopus 로고
    • Interplay between growth factor and nutrient signaling: lessons from Drosophila TOR
    • Hafen E. Interplay between growth factor and nutrient signaling: lessons from Drosophila TOR. Curr. Top. Microbiol. Immunol. 279 (2004) 153-167
    • (2004) Curr. Top. Microbiol. Immunol. , vol.279 , pp. 153-167
    • Hafen, E.1
  • 49
    • 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. Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity. J. Biol. Chem. 280 (2005) 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
  • 51
    • 11844304072 scopus 로고    scopus 로고
    • Restraining PI3K: mTOR signalling goes back to the membrane
    • Harrington L.S., Findlay G.M., and Lamb R.F. Restraining PI3K: mTOR signalling goes back to the membrane. Trends Biochem. Sci. 30 (2005) 35-42
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 35-42
    • Harrington, L.S.1    Findlay, G.M.2    Lamb, R.F.3
  • 53
    • 24944480788 scopus 로고    scopus 로고
    • The Akt-mTOR tango and its relevance to cancer
    • Hay N. The Akt-mTOR tango and its relevance to cancer. Cancer Cell 8 (2005) 179-183
    • (2005) Cancer Cell , vol.8 , pp. 179-183
    • Hay, N.1
  • 54
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay N., and Sonenberg N. Upstream and downstream of mTOR. Genes Dev. 18 (2004) 1926-1945
    • (2004) Genes Dev. , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 55
    • 0028137771 scopus 로고
    • TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast
    • Helliwell S.B., Wagner P., Kunz J., Deuter-Reinhard M., Henriquez R., and Hall M.N. TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast. Mol. Biol. Cell 5 (1994) 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
  • 57
    • 33847174115 scopus 로고    scopus 로고
    • Drosophila TCTP is essential for growth and proliferation through regulation of dRheb GTPase
    • Hsu Y.C., Chern J.J., Cai Y., Liu M., and Choi K.W. Drosophila TCTP is essential for growth and proliferation through regulation of dRheb GTPase. Nature 445 (2007) 785-788
    • (2007) Nature , vol.445 , pp. 785-788
    • Hsu, Y.C.1    Chern, J.J.2    Cai, Y.3    Liu, M.4    Choi, K.W.5
  • 59
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
    • Inoki K., Li Y., Zhu T., Wu J., and Guan K.L. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat. Cell Biol. 4 (2002) 648-657
    • (2002) Nat. Cell Biol. , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.L.5
  • 60
    • 0043127125 scopus 로고    scopus 로고
    • Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
    • Inoki K., Li Y., Xu T., and Guan K.L. Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Dev. 17 (2003) 1829-1834
    • (2003) Genes Dev. , vol.17 , pp. 1829-1834
    • Inoki, K.1    Li, Y.2    Xu, T.3    Guan, K.L.4
  • 61
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki K., Zhu T., and Guan K.L. TSC2 mediates cellular energy response to control cell growth and survival. Cell 115 (2003) 577-590
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 62
    • 33748153690 scopus 로고    scopus 로고
    • TSC2 integrates Wnt and energy signals via a coordinated phosphorylation by AMPK and GSK3 to regulate cell growth
    • Inoki K., Ouyang H., Zhu T., Lindvall C., Wang Y., Zhang X., Yang Q., Bennett C., Harada Y., Stankunas K., et al. TSC2 integrates Wnt and energy signals via a coordinated phosphorylation by AMPK and GSK3 to regulate cell growth. Cell 126 (2006) 955-968
    • (2006) Cell , vol.126 , pp. 955-968
    • Inoki, K.1    Ouyang, H.2    Zhu, T.3    Lindvall, C.4    Wang, Y.5    Zhang, X.6    Yang, Q.7    Bennett, C.8    Harada, Y.9    Stankunas, K.10
  • 63
  • 64
    • 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
  • 65
    • 4544311861 scopus 로고    scopus 로고
    • The TOR pathway interacts with the insulin signaling pathway to regulate C. elegans larval development, metabolism and life span
    • Jia K., Chen D., and Riddle D.L. The TOR pathway interacts with the insulin signaling pathway to regulate C. elegans larval development, metabolism and life span. Development 131 (2004) 3897-3906
    • (2004) Development , vol.131 , pp. 3897-3906
    • Jia, K.1    Chen, D.2    Riddle, D.L.3
  • 66
    • 0042322394 scopus 로고    scopus 로고
    • Autophagy in yeast: a TOR-mediated response to nutrient starvation
    • Kamada Y., Sekito T., and Ohsumi Y. Autophagy in yeast: a TOR-mediated response to nutrient starvation. Curr. Top. Microbiol. Immunol. 279 (2004) 73-84
    • (2004) Curr. Top. Microbiol. Immunol. , vol.279 , pp. 73-84
    • Kamada, Y.1    Sekito, T.2    Ohsumi, Y.3
  • 69
    • 14144252004 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic
    • Kang S., Bader A.G., and Vogt P.K. Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic. Proc. Natl. Acad. Sci. USA 102 (2005) 802-807
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 802-807
    • Kang, S.1    Bader, A.G.2    Vogt, P.K.3
  • 70
    • 0037623417 scopus 로고    scopus 로고
    • GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR
    • Kim D.H., Sarbassov D.D., Ali S.M., Latek R.R., Guntur K.V., Erdjument-Bromage H., Tempst P., and Sabatini D.M. GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR. Mol. Cell 11 (2003) 895-904
    • (2003) Mol. Cell , vol.11 , pp. 895-904
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    Latek, R.R.4    Guntur, K.V.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 72
    • 33749500123 scopus 로고    scopus 로고
    • (Patho)physiological significance of the serum- and glucocorticoid-inducible kinase isoforms
    • Lang F., Bohmer C., Palmada M., Seebohm G., Strutz-Seebohm N., and Vallon V. (Patho)physiological significance of the serum- and glucocorticoid-inducible kinase isoforms. Physiol. Rev. 86 (2006) 1151-1178
    • (2006) Physiol. Rev. , vol.86 , pp. 1151-1178
    • Lang, F.1    Bohmer, C.2    Palmada, M.3    Seebohm, G.4    Strutz-Seebohm, N.5    Vallon, V.6
  • 73
    • 0026583874 scopus 로고
    • The mRNA 5′ cap-binding protein, eIF-4E, cooperates with v-myc or E1A in the transformation of primary rodent fibroblasts
    • Lazaris-Karatzas A., and Sonenberg N. The mRNA 5′ cap-binding protein, eIF-4E, cooperates with v-myc or E1A in the transformation of primary rodent fibroblasts. Mol. Cell. Biol. 12 (1992) 1234-1238
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1234-1238
    • Lazaris-Karatzas, A.1    Sonenberg, N.2
  • 74
    • 0025314596 scopus 로고
    • Malignant transformation by eukaryotic initiation factor subunit that binds to mRNA 5′ cap
    • Lazaris-Karatzas A., Montine K.S., and Sonenberg N. Malignant transformation by eukaryotic initiation factor subunit that binds to mRNA 5′ cap. Nature 345 (1990) 544-547
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 76
    • 0038190932 scopus 로고    scopus 로고
    • The p38 and MK2 kinase cascade phosphorylates tuberin, the tuberous sclerosis 2 gene product, and enhances its interaction with 14-3-3
    • Li Y., Inoki K., Vacratsis P., and Guan K.L. The p38 and MK2 kinase cascade phosphorylates tuberin, the tuberous sclerosis 2 gene product, and enhances its interaction with 14-3-3. J. Biol. Chem. 278 (2003) 13663-13671
    • (2003) J. Biol. Chem. , vol.278 , pp. 13663-13671
    • Li, Y.1    Inoki, K.2    Vacratsis, P.3    Guan, K.L.4
  • 77
    • 32444433450 scopus 로고    scopus 로고
    • Hypoxia-induced energy stress regulates mRNA translation and cell growth
    • Liu L., Cash T.P., Jones R.G., Keith B., Thompson C.B., and Simon M.C. Hypoxia-induced energy stress regulates mRNA translation and cell growth. Mol. Cell 21 (2006) 521-531
    • (2006) Mol. Cell , vol.21 , pp. 521-531
    • Liu, L.1    Cash, T.P.2    Jones, R.G.3    Keith, B.4    Thompson, C.B.5    Simon, M.C.6
  • 79
    • 0037015269 scopus 로고    scopus 로고
    • TOR deficiency in C. elegans causes developmental arrest and intestinal atrophy by inhibition of mRNA translation
    • Long X., Spycher C., Han Z.S., Rose A.M., Muller F., and Avruch J. TOR deficiency in C. elegans causes developmental arrest and intestinal atrophy by inhibition of mRNA translation. Curr. Biol. 12 (2002) 1448-1461
    • (2002) Curr. Biol. , vol.12 , pp. 1448-1461
    • Long, X.1    Spycher, C.2    Han, Z.S.3    Rose, A.M.4    Muller, F.5    Avruch, J.6
  • 80
    • 0042322370 scopus 로고    scopus 로고
    • TOR action in mammalian cells and in Caenorhabditis elegans
    • Long X., Muller F., and Avruch J. TOR action in mammalian cells and in Caenorhabditis elegans. Curr. Top. Microbiol. Immunol. 279 (2004) 115-138
    • (2004) Curr. Top. Microbiol. Immunol. , vol.279 , pp. 115-138
    • Long, X.1    Muller, F.2    Avruch, J.3
  • 82
    • 21244456553 scopus 로고    scopus 로고
    • Rheb binding to mammalian target of rapamycin (mTOR) is regulated by amino acid sufficiency
    • Long X., Ortiz-Vega S., Lin Y., and Avruch J. Rheb binding to mammalian target of rapamycin (mTOR) is regulated by amino acid sufficiency. J. Biol. Chem. 280 (2005) 23433-23436
    • (2005) J. Biol. Chem. , vol.280 , pp. 23433-23436
    • Long, X.1    Ortiz-Vega, S.2    Lin, Y.3    Avruch, J.4
  • 84
    • 17444431201 scopus 로고    scopus 로고
    • Phosphorylation and functional inactivation of TSC2 by Erk implications for tuberous sclerosis and cancer pathogenesis
    • Ma L., Chen Z., Erdjument-Bromage H., Tempst P., and Pandolfi P.P. Phosphorylation and functional inactivation of TSC2 by Erk implications for tuberous sclerosis and cancer pathogenesis. Cell 121 (2005) 179-193
    • (2005) Cell , vol.121 , pp. 179-193
    • Ma, L.1    Chen, Z.2    Erdjument-Bromage, H.3    Tempst, P.4    Pandolfi, P.P.5
  • 85
    • 0034051278 scopus 로고    scopus 로고
    • Loss of Rhb1, a Rheb-related GTPase in fission yeast, causes growth arrest with a terminal phenotype similar to that caused by nitrogen starvation
    • Mach K.E., Furge K.A., and Albright C.F. Loss of Rhb1, a Rheb-related GTPase in fission yeast, causes growth arrest with a terminal phenotype similar to that caused by nitrogen starvation. Genetics 155 (2000) 611-622
    • (2000) Genetics , vol.155 , pp. 611-622
    • Mach, K.E.1    Furge, K.A.2    Albright, C.F.3
  • 86
    • 0035850916 scopus 로고    scopus 로고
    • Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane
    • Maira S.M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., and Hemmings B.A. Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane. Science 294 (2001) 374-380
    • (2001) Science , vol.294 , pp. 374-380
    • Maira, S.M.1    Galetic, I.2    Brazil, D.P.3    Kaech, S.4    Ingley, E.5    Thelen, M.6    Hemmings, B.A.7
  • 88
    • 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
  • 89
    • 0035578226 scopus 로고    scopus 로고
    • Exogenous amino acids regulate trophectoderm differentiation in the mouse blastocyst through an mTOR-dependent pathway
    • Martin P.M., and Sutherland A.E. Exogenous amino acids regulate trophectoderm differentiation in the mouse blastocyst through an mTOR-dependent pathway. Dev. Biol. 240 (2001) 182-193
    • (2001) Dev. Biol. , vol.240 , pp. 182-193
    • Martin, P.M.1    Sutherland, A.E.2
  • 90
    • 0036021402 scopus 로고    scopus 로고
    • Role of the Tsc1-Tsc2 complex in signaling and transport across the cell membrane in the fission yeast Schizosaccharomyces pombe
    • Matsumoto S., Bandyopadhyay A., Kwiatkowski D.J., Maitra U., and Matsumoto T. Role of the Tsc1-Tsc2 complex in signaling and transport across the cell membrane in the fission yeast Schizosaccharomyces pombe. Genetics 161 (2002) 1053-1063
    • (2002) Genetics , vol.161 , pp. 1053-1063
    • Matsumoto, S.1    Bandyopadhyay, A.2    Kwiatkowski, D.J.3    Maitra, U.4    Matsumoto, T.5
  • 91
    • 4344632329 scopus 로고    scopus 로고
    • Deletion of the intestinal peptide transporter affects insulin and TOR signaling in Caenorhabditis elegans
    • Meissner B., Boll M., Daniel H., and Baumeister R. Deletion of the intestinal peptide transporter affects insulin and TOR signaling in Caenorhabditis elegans. J. Biol. Chem. 279 (2004) 36739-36745
    • (2004) J. Biol. Chem. , vol.279 , pp. 36739-36745
    • Meissner, B.1    Boll, M.2    Daniel, H.3    Baumeister, R.4
  • 95
    • 0042823543 scopus 로고    scopus 로고
    • Genetic analysis of TOR signaling in Drosophila
    • Neufeld T.P. Genetic analysis of TOR signaling in Drosophila. Curr. Top. Microbiol. Immunol. 279 (2004) 139-152
    • (2004) Curr. Top. Microbiol. Immunol. , vol.279 , pp. 139-152
    • Neufeld, T.P.1
  • 97
    • 0036796288 scopus 로고    scopus 로고
    • A homologue of AMP-activated protein kinase in Drosophila melanogaster is sensitive to AMP and is activated by ATP depletion
    • Pan D.A., and Hardie D.G. A homologue of AMP-activated protein kinase in Drosophila melanogaster is sensitive to AMP and is activated by ATP depletion. Biochem. J. 367 (2002) 179-186
    • (2002) Biochem. J. , vol.367 , pp. 179-186
    • Pan, D.A.1    Hardie, D.G.2
  • 99
    • 0034629365 scopus 로고    scopus 로고
    • FKBP12-rapamycin-associated protein (FRAP) autophosphorylates at serine 2481 under translationally repressive conditions
    • Peterson R.T., Beal P.A., Comb M.J., and Schreiber S.L. FKBP12-rapamycin-associated protein (FRAP) autophosphorylates at serine 2481 under translationally repressive conditions. J. Biol. Chem. 275 (2000) 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
  • 102
    • 0242361561 scopus 로고    scopus 로고
    • Oncogenic Ras and Akt signaling contribute to glioblastoma formation by differential recruitment of existing mRNAs to polysomes
    • Rajasekhar V.K., Viale A., Socci N.D., Wiedmann M., Hu X., and Holland E.C. Oncogenic Ras and Akt signaling contribute to glioblastoma formation by differential recruitment of existing mRNAs to polysomes. Mol. Cell 12 (2003) 889-901
    • (2003) Mol. Cell , vol.12 , pp. 889-901
    • Rajasekhar, V.K.1    Viale, A.2    Socci, N.D.3    Wiedmann, M.4    Hu, X.5    Holland, E.C.6
  • 103
    • 10044276784 scopus 로고    scopus 로고
    • The hypoxia-induced paralogs Scylla and Charybdis inhibit growth by down-regulating S6K activity upstream of TSC in Drosophila
    • Reiling J.H., and Hafen E. The hypoxia-induced paralogs Scylla and Charybdis inhibit growth by down-regulating S6K activity upstream of TSC in Drosophila. Genes Dev. 18 (2004) 2879-2892
    • (2004) Genes Dev. , vol.18 , pp. 2879-2892
    • Reiling, J.H.1    Hafen, E.2
  • 104
    • 33746927077 scopus 로고    scopus 로고
    • Mitochondrial hexokinases, novel mediators of the antiapoptotic effects of growth factors and Akt
    • Robey R.B., and Hay N. Mitochondrial hexokinases, novel mediators of the antiapoptotic effects of growth factors and Akt. Oncogene 25 (2006) 4683-4696
    • (2006) Oncogene , vol.25 , pp. 4683-4696
    • Robey, R.B.1    Hay, N.2
  • 105
    • 4544384577 scopus 로고    scopus 로고
    • Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase
    • Roux P.P., Ballif B.A., Anjum R., Gygi S.P., and Blenis J. Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase. Proc. Natl. Acad. Sci. USA 101 (2004) 13489-13494
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13489-13494
    • Roux, P.P.1    Ballif, B.A.2    Anjum, R.3    Gygi, S.P.4    Blenis, J.5
  • 106
    • 2442648845 scopus 로고    scopus 로고
    • The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis
    • Ruggero D., Montanaro L., Ma L., Xu W., Londei P., Cordon-Cardo C., and Pandolfi P.P. The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis. Nat. Med. 10 (2004) 484-486
    • (2004) Nat. Med. , vol.10 , pp. 484-486
    • Ruggero, D.1    Montanaro, L.2    Ma, L.3    Xu, W.4    Londei, P.5    Cordon-Cardo, C.6    Pandolfi, P.P.7
  • 108
    • 28244469041 scopus 로고    scopus 로고
    • Redox regulation of the nutrient-sensitive raptor-mTOR pathway and complex
    • Sarbassov D.D., and Sabatini D.M. Redox regulation of the nutrient-sensitive raptor-mTOR pathway and complex. J. Biol. Chem. 280 (2005) 39505-39509
    • (2005) J. Biol. Chem. , vol.280 , pp. 39505-39509
    • Sarbassov, D.D.1    Sabatini, D.M.2
  • 109
    • 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.D., Ali S.M., Kim D.H., Guertin D.A., Latek R.R., Erdjument-Bromage H., Tempst P., and Sabatini D.M. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr. Biol. 14 (2004) 1296-1302
    • (2004) Curr. Biol. , vol.14 , pp. 1296-1302
    • Sarbassov, D.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
  • 110
    • 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
  • 112
    • 0038643484 scopus 로고    scopus 로고
    • Rheb promotes cell growth as a component of the insulin/TOR signalling network
    • Saucedo L.J., Gao X., Chiarelli D.A., Li L., Pan D., and Edgar B.A. Rheb promotes cell growth as a component of the insulin/TOR signalling network. Nat. Cell Biol. 5 (2003) 566-571
    • (2003) Nat. Cell Biol. , vol.5 , pp. 566-571
    • Saucedo, L.J.1    Gao, X.2    Chiarelli, D.A.3    Li, L.4    Pan, D.5    Edgar, B.A.6
  • 113
    • 13844294205 scopus 로고    scopus 로고
    • The human stress-activated protein kinase-interacting 1 gene encodes JNK-binding proteins
    • Schroder W., Bushell G., and Sculley T. The human stress-activated protein kinase-interacting 1 gene encodes JNK-binding proteins. Cell. Signal. 17 (2005) 761-767
    • (2005) Cell. Signal. , vol.17 , pp. 761-767
    • Schroder, W.1    Bushell, G.2    Sculley, T.3
  • 114
    • 0034234924 scopus 로고    scopus 로고
    • A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells
    • Sekulic A., Hudson C.C., Homme J.L., Yin P., Otterness D.M., Karnitz L.M., and Abraham R.T. A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells. Cancer Res. 60 (2000) 3504-3513
    • (2000) Cancer Res. , vol.60 , pp. 3504-3513
    • Sekulic, A.1    Hudson, C.C.2    Homme, J.L.3    Yin, P.4    Otterness, D.M.5    Karnitz, L.M.6    Abraham, R.T.7
  • 117
    • 33748950810 scopus 로고    scopus 로고
    • Multiallelic disruption of the rictor gene in mice reveals that mTOR complex 2 is essential for fetal growth and viability
    • Shiota C., Woo J.T., Lindner J., Shelton K.D., and Magnuson M.A. Multiallelic disruption of the rictor gene in mice reveals that mTOR complex 2 is essential for fetal growth and viability. Dev. Cell 11 (2006) 583-589
    • (2006) Dev. Cell , vol.11 , pp. 583-589
    • Shiota, C.1    Woo, J.T.2    Lindner, J.3    Shelton, K.D.4    Magnuson, M.A.5
  • 120
    • 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
  • 121
    • 33750143574 scopus 로고    scopus 로고
    • Systems biology of AGC kinases in fungi
    • Sobko A. Systems biology of AGC kinases in fungi. Sci. STKE 2006 (2006) re9
    • (2006) Sci. STKE , vol.2006
    • Sobko, A.1
  • 122
    • 21744459535 scopus 로고    scopus 로고
    • Regulation of mTOR and cell growth in response to energy stress by REDD1
    • Sofer A., Lei K., Johannessen C.M., and Ellisen L.W. Regulation of mTOR and cell growth in response to energy stress by REDD1. Mol. Cell. Biol. 25 (2005) 5834-5845
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5834-5845
    • Sofer, A.1    Lei, K.2    Johannessen, C.M.3    Ellisen, L.W.4
  • 123
    • 33747889727 scopus 로고    scopus 로고
    • Functional distinctions of protein kinase B/Akt isoforms defined by their influence on cell migration
    • Stambolic V., and Woodgett J.R. Functional distinctions of protein kinase B/Akt isoforms defined by their influence on cell migration. Trends Cell Biol. 16 (2006) 461-466
    • (2006) Trends Cell Biol. , vol.16 , pp. 461-466
    • Stambolic, V.1    Woodgett, J.R.2
  • 124
    • 0142011466 scopus 로고    scopus 로고
    • PTEN: from pathology to biology
    • Sulis M.L., and Parsons R. PTEN: from pathology to biology. Trends Cell Biol. 13 (2003) 478-483
    • (2003) Trends Cell Biol. , vol.13 , pp. 478-483
    • Sulis, M.L.1    Parsons, R.2
  • 126
    • 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., Hara K., Inoue H., Kawa Y., Tokunaga C., Hidayat S., Yoshino K., Kuroda Y., and Yonezawa K. Carboxyl-terminal region conserved among phosphoinositide-kinase-related kinases is indispensable for mTOR function in vivo and in vitro. Genes Cells 5 (2000) 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
  • 127
    • 25444450400 scopus 로고    scopus 로고
    • Differential membrane localization of ERas and Rheb, two Ras-related proteins involved in the phosphatidylinositol 3-kinase/mTOR pathway
    • Takahashi K., Nakagawa M., Young S.G., and Yamanaka S. Differential membrane localization of ERas and Rheb, two Ras-related proteins involved in the phosphatidylinositol 3-kinase/mTOR pathway. J. Biol. Chem. 280 (2005) 32768-32774
    • (2005) J. Biol. Chem. , vol.280 , pp. 32768-32774
    • Takahashi, K.1    Nakagawa, M.2    Young, S.G.3    Yamanaka, S.4
  • 128
    • 22944488274 scopus 로고    scopus 로고
    • Drosophila Melted modulates FOXO and TOR activity
    • Teleman A.A., Chen Y.W., and Cohen S.M. Drosophila Melted modulates FOXO and TOR activity. Dev. Cell 9 (2005) 271-281
    • (2005) Dev. Cell , vol.9 , pp. 271-281
    • Teleman, A.A.1    Chen, Y.W.2    Cohen, S.M.3
  • 131
    • 33751190328 scopus 로고    scopus 로고
    • Fission yeast Tor2 links nitrogen signals to cell proliferation and acts downstream of the Rheb GTPase
    • Uritani M., Hidaka H., Hotta Y., Ueno M., Ushimaru T., and Toda T. Fission yeast Tor2 links nitrogen signals to cell proliferation and acts downstream of the Rheb GTPase. Genes Cells 11 (2006) 1367-1379
    • (2006) Genes Cells , vol.11 , pp. 1367-1379
    • Uritani, M.1    Hidaka, H.2    Hotta, Y.3    Ueno, M.4    Ushimaru, T.5    Toda, T.6
  • 132
    • 1842424927 scopus 로고    scopus 로고
    • Tsc1+ and tsc2+ regulate arginine uptake and metabolism in Schizosaccharomyces pombe
    • Van Slegtenhorst M., Carr E., Stoyanova R., Kruger W.D., and Henske E.P. Tsc1+ and tsc2+ regulate arginine uptake and metabolism in Schizosaccharomyces pombe. J. Biol. Chem. 279 (2004) 12706-12713
    • (2004) J. Biol. Chem. , vol.279 , pp. 12706-12713
    • Van Slegtenhorst, M.1    Carr, E.2    Stoyanova, R.3    Kruger, W.D.4    Henske, E.P.5
  • 134
    • 0035202090 scopus 로고    scopus 로고
    • Role of S6 phosphorylation and S6 kinase in cell growth
    • Volarevic S., and Thomas G. Role of S6 phosphorylation and S6 kinase in cell growth. Prog. Nucleic Acid Res. Mol. Biol. 65 (2001) 101-127
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.65 , pp. 101-127
    • Volarevic, S.1    Thomas, G.2
  • 135
    • 0032055131 scopus 로고    scopus 로고
    • Activation of protein kinase B β and γ isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B α
    • Walker K.S., Deak M., Paterson A., Hudson K., Cohen P., and Alessi D.R. Activation of protein kinase B β and γ isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B α. Biochem. J. 331 (1998) 299-308
    • (1998) Biochem. J. , vol.331 , pp. 299-308
    • Walker, K.S.1    Deak, M.2    Paterson, A.3    Hudson, K.4    Cohen, P.5    Alessi, D.R.6
  • 136
    • 33747690458 scopus 로고    scopus 로고
    • Activation of mammalian target of rapamycin (mTOR) by insulin is associated with stimulation of 4EBP1 binding to dimeric mTOR complex 1
    • Wang L., Rhodes C.J., and Lawrence Jr. J.C. Activation of mammalian target of rapamycin (mTOR) by insulin is associated with stimulation of 4EBP1 binding to dimeric mTOR complex 1. J. Biol. Chem. 281 (2006) 24293-24303
    • (2006) J. Biol. Chem. , vol.281 , pp. 24293-24303
    • Wang, L.1    Rhodes, C.J.2    Lawrence Jr., J.C.3
  • 139
    • 0034176579 scopus 로고    scopus 로고
    • The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells
    • Williams M.R., Arthur J.S., Balendran A., van der Kaay J., Poli V., Cohen P., and Alessi D.R. The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells. Curr. Biol. 10 (2000) 439-448
    • (2000) Curr. Biol. , vol.10 , pp. 439-448
    • Williams, M.R.1    Arthur, J.S.2    Balendran, A.3    van der Kaay, J.4    Poli, V.5    Cohen, P.6    Alessi, D.R.7
  • 140
    • 0036841057 scopus 로고    scopus 로고
    • Genomic gain of PIK3CA and increased expression of p110α are associated with progression of dysplasia into invasive squamous cell carcinoma
    • Woenckhaus J., Steger K., Werner E., Fenic I., Gamerdinger U., Dreyer T., and Stahl U. Genomic gain of PIK3CA and increased expression of p110α are associated with progression of dysplasia into invasive squamous cell carcinoma. J. Pathol. 198 (2002) 335-342
    • (2002) J. Pathol. , vol.198 , pp. 335-342
    • Woenckhaus, J.1    Steger, K.2    Werner, E.3    Fenic, I.4    Gamerdinger, U.5    Dreyer, T.6    Stahl, U.7
  • 141
    • 15044363028 scopus 로고    scopus 로고
    • Recent advances in the protein kinase B signaling pathway
    • Woodgett J.R. Recent advances in the protein kinase B signaling pathway. Curr. Opin. Cell Biol. 17 (2005) 150-157
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 150-157
    • Woodgett, J.R.1
  • 142
    • 24744439255 scopus 로고    scopus 로고
    • Molecular organization of target of rapamycin complex 2
    • Wullschleger S., Loewith R., Oppliger W., and Hall M.N. Molecular organization of target of rapamycin complex 2. J. Biol. Chem. 280 (2005) 30697-30704
    • (2005) J. Biol. Chem. , vol.280 , pp. 30697-30704
    • Wullschleger, S.1    Loewith, R.2    Oppliger, W.3    Hall, M.N.4
  • 143
    • 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
  • 144
    • 0034797345 scopus 로고    scopus 로고
    • Failure to farnesylate Rheb protein contributes to the enrichment of G0/G1 phase cells in the Schizosaccharomyces pombe farnesyltransferase mutant
    • Yang W., Tabancay Jr. A.P., Urano J., and Tamanoi F. Failure to farnesylate Rheb protein contributes to the enrichment of G0/G1 phase cells in the Schizosaccharomyces pombe farnesyltransferase mutant. Mol. Microbiol. 41 (2001) 1339-1347
    • (2001) Mol. Microbiol. , vol.41 , pp. 1339-1347
    • Yang, W.1    Tabancay Jr., A.P.2    Urano, J.3    Tamanoi, F.4
  • 145
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP
    • Yang J., Cron P., Good V.M., Thompson V., Hemmings B.A., and Barford D. Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP. Nat. Struct. Biol. 9 (2002) 940-944
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 940-944
    • Yang, J.1    Cron, P.2    Good, V.M.3    Thompson, V.4    Hemmings, B.A.5    Barford, D.6
  • 146
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • Yang J., Cron P., Thompson V., Good V.M., Hess D., Hemmings B.A., and Barford D. Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Mol. Cell 9 (2002) 1227-1240
    • (2002) Mol. Cell , vol.9 , pp. 1227-1240
    • Yang, J.1    Cron, P.2    Thompson, V.3    Good, V.M.4    Hess, D.5    Hemmings, B.A.6    Barford, D.7
  • 148
    • 27944493875 scopus 로고    scopus 로고
    • Dosage-dependent effects of Akt1/protein kinase Bα (PKBα) and Akt3/PKBγ on thymus, skin, and cardiovascular and nervous system development in mice
    • Yang Z.Z., Tschopp O., Di-Poi N., Bruder E., Baudry A., Dummler B., Wahli W., and Hemmings B.A. Dosage-dependent effects of Akt1/protein kinase Bα (PKBα) and Akt3/PKBγ on thymus, skin, and cardiovascular and nervous system development in mice. Mol. Cell. Biol. 25 (2005) 10407-10418
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10407-10418
    • Yang, Z.Z.1    Tschopp, O.2    Di-Poi, N.3    Bruder, E.4    Baudry, A.5    Dummler, B.6    Wahli, W.7    Hemmings, B.A.8
  • 149
    • 33751079895 scopus 로고    scopus 로고
    • Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity
    • Yang Q., Inoki K., Ikenoue T., and Guan K.L. Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity. Genes Dev. 20 (2006) 2820-2832
    • (2006) Genes Dev. , vol.20 , pp. 2820-2832
    • Yang, Q.1    Inoki, K.2    Ikenoue, T.3    Guan, K.L.4
  • 150
    • 33646485688 scopus 로고    scopus 로고
    • TSC1/TSC2 and Rheb have different effects on TORC1 and TORC2 activity
    • Yang Q., Inoki K., Kim E., and Guan K.L. TSC1/TSC2 and Rheb have different effects on TORC1 and TORC2 activity. Proc. Natl. Acad. Sci. USA 103 (2006) 6811-6816
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6811-6816
    • Yang, Q.1    Inoki, K.2    Kim, E.3    Guan, K.L.4
  • 152
    • 0038141979 scopus 로고    scopus 로고
    • Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins
    • Zhang Y., Gao X., Saucedo L.J., Ru B., Edgar B.A., and Pan D. Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins. Nat. Cell Biol. 5 (2003) 578-581
    • (2003) Nat. Cell Biol. , vol.5 , pp. 578-581
    • Zhang, Y.1    Gao, X.2    Saucedo, L.J.3    Ru, B.4    Edgar, B.A.5    Pan, D.6
  • 153
    • 33750040886 scopus 로고    scopus 로고
    • S6K1 regulates GSK3 under conditions of mTOR-dependent feedback inhibition of Akt
    • Zhang H.H., Lipovsky A.I., Dibble C.C., Sahin M., and Manning B.D. S6K1 regulates GSK3 under conditions of mTOR-dependent feedback inhibition of Akt. Mol. Cell 24 (2006) 185-197
    • (2006) Mol. Cell , vol.24 , pp. 185-197
    • Zhang, H.H.1    Lipovsky, A.I.2    Dibble, C.C.3    Sahin, M.4    Manning, B.D.5
  • 154
    • 33644781670 scopus 로고    scopus 로고
    • Drosophila target of rapamycin kinase functions as a multimer
    • Zhang Y., Billington Jr. C.J., Pan D., and Neufeld T.P. Drosophila target of rapamycin kinase functions as a multimer. Genetics 172 (2006) 355-362
    • (2006) Genetics , vol.172 , pp. 355-362
    • Zhang, Y.1    Billington Jr., C.J.2    Pan, D.3    Neufeld, T.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.