메뉴 건너뛰기




Volumn 47, Issue , 2007, Pages 443-467

mTOR pathway as a target in tissue hypertrophy

Author keywords

AKT; Cancer; Muscle; Rapamycin; TSC

Indexed keywords

MAMMALIAN TARGET OF RAPAMYCIN; PROTEIN; PROTEIN TORC1; PROTEIN TORC2; PROTEIN TSC1; TUBERIN; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

EID: 33847079961     PISSN: 03621642     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.pharmtox.47.120505.105359     Document Type: Review
Times cited : (156)

References (106)
  • 1
    • 14844363721 scopus 로고    scopus 로고
    • Signaling by target of rapamycin proteins in cell growth control
    • Inoki K, Ouyang H, Li Y, Guan KL. 2005. Signaling by target of rapamycin proteins in cell growth control. Microbiol. Mol. Biol. Rev. 69:79-100
    • (2005) Microbiol. Mol. Biol. Rev , vol.69 , pp. 79-100
    • Inoki, K.1    Ouyang, H.2    Li, Y.3    Guan, K.L.4
  • 3
    • 0029021621 scopus 로고
    • Identification of tuberin, the tuberous sclerosis-2 product. Tuberin possesses specific Rap1GAP activity
    • Wienecke R, Konig A, DeClue JE. 1995. Identification of tuberin, the tuberous sclerosis-2 product. Tuberin possesses specific Rap1GAP activity. J. Biol. Chem. 270:16409-14
    • (1995) J. Biol. Chem , vol.270 , pp. 16409-16414
    • Wienecke, R.1    Konig, A.2    DeClue, J.E.3
  • 4
    • 0036501277 scopus 로고    scopus 로고
    • A mouse model of TSC1 reveals sex-dependent lethality from liver hemangiomas, and up-regulation of p70S6 kinase activity in Tsc1 null cells
    • Kwiatkowski DJ, Zhang H, Bandura JL, Heiberger KM, Glogauer M, et al. 2002. A mouse model of TSC1 reveals sex-dependent lethality from liver hemangiomas, and up-regulation of p70S6 kinase activity in Tsc1 null cells. Hum. Mol. Genet. 11:525-34
    • (2002) Hum. Mol. Genet , vol.11 , pp. 525-534
    • Kwiatkowski, D.J.1    Zhang, H.2    Bandura, J.L.3    Heiberger, K.M.4    Glogauer, M.5
  • 5
    • 0347988005 scopus 로고    scopus 로고
    • Loss of Tsc1/Tsc2 activates mTOR and disrupts PI3K-akt signaling through downregulation of PDGFR
    • Zhang H, Cicchetti G, Onda H, Koon HB, Asrican K, et al. 2003. Loss of Tsc1/Tsc2 activates mTOR and disrupts PI3K-akt signaling through downregulation of PDGFR. J. Clin. Invest. 112:1223-33
    • (2003) J. Clin. Invest , vol.112 , pp. 1223-1233
    • Zhang, H.1    Cicchetti, G.2    Onda, H.3    Koon, H.B.4    Asrican, K.5
  • 7
    • 33646854721 scopus 로고    scopus 로고
    • TSC1 stabilizes TSC2 by inhibiting the interaction between TSC2 and the HERC1 ubiquitin ligase
    • Chong-Kopera H, Inoki K, Li Y, Zhu T, Garcia-Gonzalo FR, et al. 2006. TSC1 stabilizes TSC2 by inhibiting the interaction between TSC2 and the HERC1 ubiquitin ligase. J. Biol. Chem. 281:8313-16
    • (2006) J. Biol. Chem , vol.281 , pp. 8313-8316
    • Chong-Kopera, H.1    Inoki, K.2    Li, Y.3    Zhu, T.4    Garcia-Gonzalo, F.R.5
  • 8
    • 0346463022 scopus 로고    scopus 로고
    • Pam and its ortholog highwire interact with and may negatively regulate the TSC1, TSC2 complex
    • Murthy V, Han S, Beauchamp RL, Smith N, Haddad LA, et al. 2004. Pam and its ortholog highwire interact with and may negatively regulate the TSC1, TSC2 complex. J. Biol. Chem. 279:1351-58
    • (2004) J. Biol. Chem , vol.279 , pp. 1351-1358
    • Murthy, V.1    Han, S.2    Beauchamp, R.L.3    Smith, N.4    Haddad, L.A.5
  • 9
    • 0036712905 scopus 로고    scopus 로고
    • Tsc tumor suppressor proteins antagonize amino-acid-TOR signaling
    • Gao X, Zhang Y, Arrazola P, Hino O, Kobayashi T, et al. 2002. Tsc tumor suppressor proteins antagonize amino-acid-TOR signaling. Nat. Cell Biol. 4:699-704
    • (2002) Nat. Cell Biol , vol.4 , pp. 699-704
    • Gao, X.1    Zhang, Y.2    Arrazola, P.3    Hino, O.4    Kobayashi, T.5
  • 10
    • 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 AR, Manning BD, Roux PP, Cantley LC, Blenis J. 2003. Tuberous sclerosis complex gene products, tuberin and hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward rheb. Curr. Biol. 13:1259-68
    • (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
  • 11
    • 4444276510 scopus 로고    scopus 로고
    • Biochemical and functional characterizations of small GTPase rheb and TSC2 GAP activity
    • Li Y, Inoki K, Guan KL. 2004. Biochemical and functional characterizations of small GTPase rheb and TSC2 GAP activity. Mol. Cell. Biol. 24:7965-75
    • (2004) Mol. Cell. Biol , vol.24 , pp. 7965-7975
    • Li, Y.1    Inoki, K.2    Guan, K.L.3
  • 12
    • 0038141979 scopus 로고    scopus 로고
    • Rheb is a direct target of the tuberous sclerosis tumor suppressor proteins
    • Zhang Y, Gao X, Saucedo LJ, Ru B, Edgar BA, Pan D. 2003. Rheb is a direct target of the tuberous sclerosis tumor suppressor proteins. Nat. Cell Biol. 5:578-81
    • (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
  • 13
    • 0038433304 scopus 로고    scopus 로고
    • Insulin activation of rheb, a mediator of mTOR/S6K/4E-BP signaling, is inhibited by TSC1 and 2
    • Garami A, Zwartkruis FJ, Nobukuni T, Joaquin M, Roccio M, et al. 2003. Insulin activation of rheb, a mediator of mTOR/S6K/4E-BP signaling, is inhibited by TSC1 and 2. Mol. Cell 11:1457-66
    • (2003) Mol. Cell , vol.11 , pp. 1457-1466
    • Garami, A.1    Zwartkruis, F.J.2    Nobukuni, T.3    Joaquin, M.4    Roccio, M.5
  • 14
    • 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, Guan KL. 2003. Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Dev. 17:1829-34
    • (2003) Genes Dev , vol.17 , pp. 1829-1834
    • Inoki, K.1    Li, Y.2    Xu, T.3    Guan, K.L.4
  • 15
    • 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 AF, Rebhun JF, Clark GJ, Quilliam LA. 2003. Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner. J. Biol. Chem. 278:32493-96
    • (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
  • 17
    • 21244456553 scopus 로고    scopus 로고
    • Rheb binding to mTOR is regulated by amino acid sufficiency
    • Long X, Ortiz-Vega S, Lin Y, Avruch J. 2005. Rheb binding to mTOR is regulated by amino acid sufficiency. J. Biol. Chem. 280(25):23433-36
    • (2005) J. Biol. Chem , vol.280 , Issue.25 , pp. 23433-23436
    • Long, X.1    Ortiz-Vega, S.2    Lin, Y.3    Avruch, J.4
  • 18
    • 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 EM, Finn SG, Tee AR, Browne GJ, Proud CG. 2005. 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. 280:18717-27
    • (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
  • 19
    • 27944452168 scopus 로고    scopus 로고
    • Identification of novel single amino acid changes that result in hyperactivation of the unique GTPase, rheb, in fission yeast
    • Urano J, Comiso MJ, Guo L, Aspuria PJ, Deniskin R, et al. 2005. Identification of novel single amino acid changes that result in hyperactivation of the unique GTPase, rheb, in fission yeast. Mol. Microbiol. 58:1074-86
    • (2005) Mol. Microbiol , vol.58 , pp. 1074-1086
    • Urano, J.1    Comiso, M.J.2    Guo, L.3    Aspuria, P.J.4    Deniskin, R.5
  • 22
    • 33644886769 scopus 로고    scopus 로고
    • Nutrients suppress phosphatidylinositol 3-kinase/Akt signaling via raptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation
    • Tzatsos A, Kandror KV. 2006. Nutrients suppress phosphatidylinositol 3-kinase/Akt signaling via raptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation. Mol. Cell. Biol. 26:63-76
    • (2006) Mol. Cell. Biol , vol.26 , pp. 63-76
    • Tzatsos, A.1    Kandror, K.V.2
  • 23
    • 0032520009 scopus 로고    scopus 로고
    • 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the akt(PKB) signaling pathway
    • Gingras AC, Kennedy SG, O'Leary MA, Sonenberg N, Hay N. 1998. 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the akt(PKB) signaling pathway. Genes Dev. 12:502-13
    • (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
  • 24
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by akt and suppresses mTOR signaling
    • Inoki K, Li Y, Zhu T, Wu J, Guan KL. 2002. TSC2 is phosphorylated and inhibited by akt and suppresses mTOR signaling. Nat. Cell Biol. 4:648-57
    • (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
  • 25
    • 0036714127 scopus 로고    scopus 로고
    • Akt regulates growth by directly phosphorylating Tsc2
    • Potter CJ, Pedraza LG, Xu T. 2002. Akt regulates growth by directly phosphorylating Tsc2. Nat. Cell Biol. 4:658-65
    • (2002) Nat. Cell Biol , vol.4 , pp. 658-665
    • Potter, C.J.1    Pedraza, L.G.2    Xu, T.3
  • 26
    • 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 BD, Tee AR, Logsdon MN, Blenis J, Cantley LC. 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 10:151-62
    • (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
  • 27
    • 33646111903 scopus 로고    scopus 로고
    • Activity of TSC2 is inhibited by AKT-mediated phosphorylation and membrane partitioning
    • Cai SL, Tee AR, Short JD, Bergeron JM, Kim J, et al. 2006. Activity of TSC2 is inhibited by AKT-mediated phosphorylation and membrane partitioning. J. Cell Biol. 173:279-89
    • (2006) J. Cell Biol , vol.173 , pp. 279-289
    • Cai, S.L.1    Tee, A.R.2    Short, J.D.3    Bergeron, J.M.4    Kim, J.5
  • 28
    • 5444233787 scopus 로고    scopus 로고
    • Tsc2 is not a critical target of akt during normal Drosophila development
    • Dong J, Pan D. 2004. Tsc2 is not a critical target of akt during normal Drosophila development. Genes Dev. 18:2479-84
    • (2004) Genes Dev , vol.18 , pp. 2479-2484
    • Dong, J.1    Pan, D.2
  • 29
    • 24944464482 scopus 로고    scopus 로고
    • Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasis
    • Ruvinsky I, Sharon N, Lerer T, Cohen H, Stolovich-Rain M, et al. 2005. Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasis. Genes Dev. 19:2199-11
    • (2005) Genes Dev , vol.19 , pp. 2199-2111
    • Ruvinsky, I.1    Sharon, N.2    Lerer, T.3    Cohen, H.4    Stolovich-Rain, M.5
  • 30
    • 0035498939 scopus 로고    scopus 로고
    • Hierarchical phosphorylation of the translation inhibitor 4E-BP1
    • Gingras AC, Raught B, Gygi SP, Niedzwiecka A, Miron M, et al. 2001. Hierarchical phosphorylation of the translation inhibitor 4E-BP1. Genes Dev. 15:2852-64
    • (2001) Genes Dev , vol.15 , pp. 2852-2864
    • Gingras, A.C.1    Raught, B.2    Gygi, S.P.3    Niedzwiecka, A.4    Miron, M.5
  • 31
    • 0037178786 scopus 로고    scopus 로고
    • mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • Kim DH, Sarbassov DD, Ali SM, King JE, Latek RR, et al. 2002. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110:163-75
    • (2002) Cell , vol.110 , pp. 163-175
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    King, J.E.4    Latek, R.R.5
  • 32
    • 0037178781 scopus 로고    scopus 로고
    • Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action
    • Hara K, Maruki Y, Long X, Yoshino K, Oshiro N, et al. 2002. Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action. Cell 110:177-89
    • (2002) Cell , vol.110 , pp. 177-189
    • Hara, K.1    Maruki, Y.2    Long, X.3    Yoshino, K.4    Oshiro, N.5
  • 33
    • 0037117409 scopus 로고    scopus 로고
    • Identification of a conserved motif required for mTOR signaling
    • Schalm SS, Blenis J. 2002. Identification of a conserved motif required for mTOR signaling. Curr. Biol. 12:632-39
    • (2002) Curr. Biol , vol.12 , pp. 632-639
    • Schalm, S.S.1    Blenis, J.2
  • 34
    • 0037507252 scopus 로고    scopus 로고
    • The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif
    • Nojima H, Tokunaga C, Eguchi S, Oshiro N, Hidayat S, et al. 2003. The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif. J. Biol. Chem. 278:15461-64
    • (2003) J. Biol. Chem , vol.278 , pp. 15461-15464
    • Nojima, H.1    Tokunaga, C.2    Eguchi, S.3    Oshiro, N.4    Hidayat, S.5
  • 35
    • 0037718389 scopus 로고    scopus 로고
    • TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation and function
    • Schalm SS, Fingar DC, Sabatini DM, Blenis J. 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
  • 36
    • 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 AR, Proud CG. 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. 22:1674-83
    • (2002) Mol. Cell Biol , vol.22 , pp. 1674-1683
    • Tee, A.R.1    Proud, C.G.2
  • 37
    • 0142071830 scopus 로고    scopus 로고
    • Target of rapamycin (TOR)-signaling and RAIP motifs play distinct roles in the mammalian TOR-dependent phosphorylation of initiation factor 4E-binding protein 1
    • Beugnet A, Wang X, Proud CG. 2003. Target of rapamycin (TOR)-signaling and RAIP motifs play distinct roles in the mammalian TOR-dependent phosphorylation of initiation factor 4E-binding protein 1. J. Biol. Chem. 278:40717-22
    • (2003) J. Biol. Chem , vol.278 , pp. 40717-40722
    • Beugnet, A.1    Wang, X.2    Proud, C.G.3
  • 38
    • 0028239893 scopus 로고
    • RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs
    • Sabatini DM, Erdjument-Bromage H, Lui M, Tempst P, Snyder SH. 1994. RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs. Cell 78:35-43
    • (1994) Cell , vol.78 , pp. 35-43
    • Sabatini, D.M.1    Erdjument-Bromage, H.2    Lui, M.3    Tempst, P.4    Snyder, S.H.5
  • 39
    • 0034629365 scopus 로고    scopus 로고
    • FKBP12-rapamycin- associated protein (FRAP) autophosphorylates at serine 2481 under translationally repressive conditions
    • Peterson RT, Beal PA, Comb MJ, Schreiber SL. 2000. FKBP12-rapamycin- associated protein (FRAP) autophosphorylates at serine 2481 under translationally repressive conditions. J. Biol. Chem. 275:7416-23
    • (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
  • 40
    • 0142057156 scopus 로고    scopus 로고
    • Characterization of eIF3k: A newly discovered subunit of mammalian translation initiation factor eIF3
    • Mayeur GL, Fraser CS, Peiretti F, Block KL, Hershey JWB. 2003. Characterization of eIF3k: A newly discovered subunit of mammalian translation initiation factor eIF3. Eur. J. Biochem. 270:4133-39
    • (2003) Eur. J. Biochem , vol.270 , pp. 4133-4139
    • Mayeur, G.L.1    Fraser, C.S.2    Peiretti, F.3    Block, K.L.4    Hershey, J.W.B.5
  • 41
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras AC, Raught B, Sonenberg N. 2001. Regulation of translation initiation by FRAP/mTOR. Genes Dev. 15:807-26
    • (2001) Genes Dev , vol.15 , pp. 807-826
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 42
    • 27744569843 scopus 로고    scopus 로고
    • mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events
    • Holz MK, Ballif BA, Gygi SP, Blenis J. 2005. mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123:569-80
    • (2005) Cell , vol.123 , pp. 569-580
    • Holz, M.K.1    Ballif, B.A.2    Gygi, S.P.3    Blenis, J.4
  • 43
    • 2942563750 scopus 로고    scopus 로고
    • The in vivo role of PtdIns(3, 4, 5)P3 binding to PDK1 PH domain defined by knockin mutation
    • McManus EJ, Collins BJ, Ashby PR, Prescott AR, Murray-Tait V, et al. 2004. The in vivo role of PtdIns(3, 4, 5)P3 binding to PDK1 PH domain defined by knockin mutation. EMBO J. 23:2071-82
    • (2004) EMBO J , vol.23 , pp. 2071-2082
    • McManus, E.J.1    Collins, B.J.2    Ashby, P.R.3    Prescott, A.R.4    Murray-Tait, V.5
  • 44
    • 0042967831 scopus 로고    scopus 로고
    • In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation
    • Collins BJ, Deak M, Arthur JS, Armit LJ, Alessi DR. 2003. In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation. EMBO J. 22:4202-11
    • (2003) EMBO J , vol.22 , pp. 4202-4211
    • Collins, B.J.1    Deak, M.2    Arthur, J.S.3    Armit, L.J.4    Alessi, D.R.5
  • 45
    • 0034141942 scopus 로고    scopus 로고
    • Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI
    • Raught B, Gingras AC, Gygi SP, Imataka H, Morino S, et al. 2000. Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI. EMBO J. 19:434-44
    • (2000) EMBO J , vol.19 , pp. 434-444
    • Raught, B.1    Gingras, A.C.2    Gygi, S.P.3    Imataka, H.4    Morino, S.5
  • 47
    • 4544220704 scopus 로고    scopus 로고
    • Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
    • Um SH, Frigerio F, Watanabe M, Picard F, Joaquin M, et al. 2004. Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity. Nature 431:200-5
    • (2004) Nature , vol.431 , pp. 200-205
    • Um, S.H.1    Frigerio, F.2    Watanabe, M.3    Picard, F.4    Joaquin, M.5
  • 48
    • 3342958797 scopus 로고    scopus 로고
    • The TSC 1-2 tumor suppressor controls insulin-PI3K signaling via regulation of IRS proteins
    • Harrington LS, Findlay GM, Gray A, Tolkacheva T, Wigfield S, et al. 2004. The TSC 1-2 tumor suppressor controls insulin-PI3K signaling via regulation of IRS proteins. J. Cell Biol. 166:213-23
    • (2004) J. Cell Biol , vol.166 , pp. 213-223
    • Harrington, L.S.1    Findlay, G.M.2    Gray, A.3    Tolkacheva, T.4    Wigfield, S.5
  • 49
    • 4544343980 scopus 로고    scopus 로고
    • Inappropriate activation of the TSC/Rheb/mTOR/S6K cassette induces IRS1/2 depletion, insulin resistance, and cell survival deficiencies
    • Shah OJ, Wang Z, Hunter T. 2004. Inappropriate activation of the TSC/Rheb/mTOR/S6K cassette induces IRS1/2 depletion, insulin resistance, and cell survival deficiencies. Curr. Biol. 14:1650-56
    • (2004) Curr. Biol , vol.14 , pp. 1650-1656
    • Shah, O.J.1    Wang, Z.2    Hunter, T.3
  • 50
    • 33646023695 scopus 로고    scopus 로고
    • Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB
    • Sarbassov DD, Ali SM, Sengupta S, Sheen JH, Hsu PP, et al. 2006. Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB. Mol. Cell 22(2):159-68
    • (2006) Mol. Cell , vol.22 , Issue.2 , pp. 159-168
    • Sarbassov, D.D.1    Ali, S.M.2    Sengupta, S.3    Sheen, J.H.4    Hsu, P.P.5
  • 51
    • 7944235758 scopus 로고    scopus 로고
    • Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
    • Jacinto E, Loewith R, Schmidt A, Lin S, Ruegg MA, et al. 2004. Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat. Cell Biol. 6:1122-28
    • (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
  • 52
    • 0036753494 scopus 로고    scopus 로고
    • Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control
    • Loewith R, Jacinto E, Wullschleger S, Lorberg A, Crespo JL, et al. 2002. Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Mol. Cell 10:457-68
    • (2002) Mol. Cell , vol.10 , pp. 457-468
    • Loewith, R.1    Jacinto, E.2    Wullschleger, S.3    Lorberg, A.4    Crespo, J.L.5
  • 53
    • 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 DD, Ali SM, Kim DH, Guertin DA, Latek RR, et al. 2004. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr. Biol. 14:1296-302
    • (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
  • 54
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov DD, Guertin DA, Ali SM, Sabatini DM. 2005. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307:1098-201
    • (2005) Science , vol.307 , pp. 1098-1201
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 55
    • 28844434558 scopus 로고    scopus 로고
    • mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes
    • Hresko RC, Mueckler M. 2005. mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes. J. Biol. Chem. 280:40406-16
    • (2005) J. Biol. Chem , vol.280 , pp. 40406-40416
    • Hresko, R.C.1    Mueckler, M.2
  • 56
    • 21244458013 scopus 로고    scopus 로고
    • Structure of S6 kinase 1 determines whether raptor-mTOR or rictor-mTOR phosphorylates its hydrophobic motif site
    • Ali SM, Sabatini DM. 2005. Structure of S6 kinase 1 determines whether raptor-mTOR or rictor-mTOR phosphorylates its hydrophobic motif site. J. Biol. Chem. 280:19445-48
    • (2005) J. Biol. Chem , vol.280 , pp. 19445-19448
    • Ali, S.M.1    Sabatini, D.M.2
  • 57
    • 23344448223 scopus 로고    scopus 로고
    • Tor2 directly phosphorylates the AGC kinase Ypk2 to regulate actin polarization
    • Kamada Y, Fujioka Y, Suzuki NN, Inagaki F, Wullschleger S, et al. 2005. Tor2 directly phosphorylates the AGC kinase Ypk2 to regulate actin polarization. Mol. Cell. Biol. 25:7239-48
    • (2005) Mol. Cell. Biol , vol.25 , pp. 7239-7248
    • Kamada, Y.1    Fujioka, Y.2    Suzuki, N.N.3    Inagaki, F.4    Wullschleger, S.5
  • 58
    • 4944222854 scopus 로고    scopus 로고
    • PTEN gene targeting reveals a radiation-induced size checkpoint in human cancer cells
    • Lee C, Kim JS, Waldman T. 2004. PTEN gene targeting reveals a radiation-induced size checkpoint in human cancer cells. Canc. Res. 64:6906-14
    • (2004) Canc. Res , vol.64 , pp. 6906-6914
    • Lee, C.1    Kim, J.S.2    Waldman, T.3
  • 59
    • 0242268407 scopus 로고    scopus 로고
    • mTor is required for hypertrophy of pten-deficient neuronal soma in vivo
    • Kwon CH, Zhu X, Zhang J, Baker SJ. 2003. mTor is required for hypertrophy of pten-deficient neuronal soma in vivo. Proc. Natl. Acad. Sci. USA 100:12923-28
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12923-12928
    • Kwon, C.H.1    Zhu, X.2    Zhang, J.3    Baker, S.J.4
  • 60
    • 0034982971 scopus 로고    scopus 로고
    • TSC1 and TSC2 tumor suppressors antagonize insulin signaling in cell growth
    • Gao X, Pan D. 2001. TSC1 and TSC2 tumor suppressors antagonize insulin signaling in cell growth. Genes Dev. 15:1383-92
    • (2001) Genes Dev , vol.15 , pp. 1383-1392
    • Gao, X.1    Pan, D.2
  • 61
    • 0037108151 scopus 로고    scopus 로고
    • Lethality of drosophila lacking TSC tumor suppressor function rescued by reducing dS6K signaling
    • Radimerski T, Montagne J, Hemmings-Mieszczak M, Thomas G. 2002. Lethality of drosophila lacking TSC tumor suppressor function rescued by reducing dS6K signaling. Genes Dev. 16:2627-32
    • (2002) Genes Dev , vol.16 , pp. 2627-2632
    • Radimerski, T.1    Montagne, J.2    Hemmings-Mieszczak, M.3    Thomas, G.4
  • 62
    • 33646485688 scopus 로고    scopus 로고
    • TSC1/TSC2 and rheb have different effects on TORC1 and TORC2 activity
    • Yang Q, Inoki K, Kim E, Guan KL. 2006. TSC1/TSC2 and rheb have different effects on TORC1 and TORC2 activity. Proc. Natl. Acad. Sci. USA 103(18):6811-16
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.18 , pp. 6811-6816
    • Yang, Q.1    Inoki, K.2    Kim, E.3    Guan, K.L.4
  • 63
    • 0034312315 scopus 로고    scopus 로고
    • Regulation of cellular growth by the drosophila target of rapamycin dTOR
    • Zhang H, Stallock JP, Ng JC, Reinhard C, Neufeld TP. 2000. Regulation of cellular growth by the drosophila target of rapamycin dTOR. Genes Dev. 14:2712-24
    • (2000) Genes Dev , vol.14 , pp. 2712-2724
    • Zhang, H.1    Stallock, J.P.2    Ng, J.C.3    Reinhard, C.4    Neufeld, T.P.5
  • 64
    • 0034312279 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of dTOR, the drosophila homolog of the target of rapamycin
    • Oldham S, Montagne J, Radimerski T, Thomas G, Hafen E. 2000. Genetic and biochemical characterization of dTOR, the drosophila homolog of the target of rapamycin. Genes Dev. 14:2689-94
    • (2000) Genes Dev , vol.14 , pp. 2689-2694
    • Oldham, S.1    Montagne, J.2    Radimerski, T.3    Thomas, G.4    Hafen, E.5
  • 66
    • 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 SH, Mieulet V, Sticker M, Goss VL, et al. 2004. 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. 24:3112-24
    • (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
  • 67
    • 29144438951 scopus 로고    scopus 로고
    • Inactivation of S6 ribosomal protein gene in T lymphocytes activates a p53-dependent checkpoint response
    • Sulic S, Panic L, Barkic M, Mercep M, Uzelac M, Volarevic S. 2005. Inactivation of S6 ribosomal protein gene in T lymphocytes activates a p53-dependent checkpoint response. Genes Dev. 19:3070-82
    • (2005) Genes Dev , vol.19 , pp. 3070-3082
    • Sulic, S.1    Panic, L.2    Barkic, M.3    Mercep, M.4    Uzelac, M.5    Volarevic, S.6
  • 69
    • 0032949353 scopus 로고    scopus 로고
    • Maturation of the myogenic program is induced by postmitotic expression of insulin-like growth factor I
    • Musaro A, Rosenthal N. 1999. Maturation of the myogenic program is induced by postmitotic expression of insulin-like growth factor I. Mol. Cell. Biol. 19:3115-24
    • (1999) Mol. Cell. Biol , vol.19 , pp. 3115-3124
    • Musaro, A.1    Rosenthal, N.2
  • 70
    • 14844336534 scopus 로고    scopus 로고
    • Muscle-specific expression of IGF-1 blocks angiotensin II-induced skeletal muscle wasting
    • Song YH, Li Y, Du J, Mitch WE, Rosenthal N, Delafontaine P. 2005. Muscle-specific expression of IGF-1 blocks angiotensin II-induced skeletal muscle wasting. J. Clin. Invest. 115:451-58
    • (2005) J. Clin. Invest , vol.115 , pp. 451-458
    • Song, Y.H.1    Li, Y.2    Du, J.3    Mitch, W.E.4    Rosenthal, N.5    Delafontaine, P.6
  • 71
    • 0035735902 scopus 로고    scopus 로고
    • Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways
    • Rommel C, Bodine SC, Clarke BA, Rossman R, Nunez L, et al. 2001. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways. Nat. Cell Biol. 3:1009-13
    • (2001) Nat. Cell Biol , vol.3 , pp. 1009-1013
    • Rommel, C.1    Bodine, S.C.2    Clarke, B.A.3    Rossman, R.4    Nunez, L.5
  • 72
    • 0035736260 scopus 로고    scopus 로고
    • Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
    • Bodine SC, Stitt TN, Gonzalez M, Kline WO, Stover GL, et al. 2001. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat. Cell Biol. 3:1014-19
    • (2001) Nat. Cell Biol , vol.3 , pp. 1014-1019
    • Bodine, S.C.1    Stitt, T.N.2    Gonzalez, M.3    Kline, W.O.4    Stover, G.L.5
  • 73
    • 0037047098 scopus 로고    scopus 로고
    • A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification
    • Pallafacchina G, Calabria E, Serrano AL, Kalhovde JM, Schiaffino S. 2002. A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification. Proc. Natl. Acad. Sci. USA 99:9213-18
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9213-9218
    • Pallafacchina, G.1    Calabria, E.2    Serrano, A.L.3    Kalhovde, J.M.4    Schiaffino, S.5
  • 74
    • 18144386162 scopus 로고    scopus 로고
    • Selective activation of AMPK-PGC-1alpha or PKB-TSC2-mTOR signaling can explain specific adaptive responses to endurance or resistance training-like electrical muscle stimulation
    • Atherton PJ, Babraj J, Smith K, Singh J, Rennie MJ, Wackerhage H. 2005. Selective activation of AMPK-PGC-1alpha or PKB-TSC2-mTOR signaling can explain specific adaptive responses to endurance or resistance training-like electrical muscle stimulation. FASEB J. 19:786-88
    • (2005) FASEB J , vol.19 , pp. 786-788
    • Atherton, P.J.1    Babraj, J.2    Smith, K.3    Singh, J.4    Rennie, M.J.5    Wackerhage, H.6
  • 75
    • 20044392290 scopus 로고    scopus 로고
    • Atrophy of S6K1(-/-) skeletal muscle cells reveals distinct mTOR effectors for cell cycle and size control
    • Ohanna M, Sobering AK, Lapointe T, Lorenzo L, Fraud C, et al. 2005. Atrophy of S6K1(-/-) skeletal muscle cells reveals distinct mTOR effectors for cell cycle and size control. Nat. Cell Biol. 7:286-94
    • (2005) Nat. Cell Biol , vol.7 , pp. 286-294
    • Ohanna, M.1    Sobering, A.K.2    Lapointe, T.3    Lorenzo, L.4    Fraud, C.5
  • 76
    • 9444290436 scopus 로고    scopus 로고
    • Impaired anabolic response of muscle protein synthesis is associated with S6K1 dysregulation in elderly humans
    • Guillet C, Prod'homme M, Balage M, Gachon P, Giraudet C, et al. 2004. Impaired anabolic response of muscle protein synthesis is associated with S6K1 dysregulation in elderly humans. FASEB J. 18:1586-87
    • (2004) FASEB J , vol.18 , pp. 1586-1587
    • Guillet, C.1    Prod'homme, M.2    Balage, M.3    Gachon, P.4    Giraudet, C.5
  • 78
    • 3042608187 scopus 로고    scopus 로고
    • Inhibition of mTOR signaling with rapamycin regresses established cardiac hypertrophy induced by pressure overload
    • McMullen JR, Sherwood MC, Tarnavski O, Zhang L, Dorfman AL, et al. 2004. Inhibition of mTOR signaling with rapamycin regresses established cardiac hypertrophy induced by pressure overload. Circulation 109:3050-55
    • (2004) Circulation , vol.109 , pp. 3050-3055
    • McMullen, J.R.1    Sherwood, M.C.2    Tarnavski, O.3    Zhang, L.4    Dorfman, A.L.5
  • 79
    • 0035980049 scopus 로고    scopus 로고
    • Cross-talk between the ERK and p70 S6 kinase (S6K) signaling pathways. MEK-dependent activation of S6K2 in cardiomyocytes
    • Wang L, Gout I, Proud CG. 2001. Cross-talk between the ERK and p70 S6 kinase (S6K) signaling pathways. MEK-dependent activation of S6K2 in cardiomyocytes. J. Biol. Chem. 276:32670-77
    • (2001) J. Biol. Chem , vol.276 , pp. 32670-32677
    • Wang, L.1    Gout, I.2    Proud, C.G.3
  • 80
    • 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, Proud CG. 2002. Ras/Erk signaling is essential for activation of protein synthesis by gq protein-coupled receptor agonists in adult cardiomyocytes. Circ. Res. 91:821-29
    • (2002) Circ. Res , vol.91 , pp. 821-829
    • Wang, L.1    Proud, C.G.2
  • 81
    • 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 PP, Ballif BA, Anjum R, Gygi SP, Blenis J. 2004. Tumor-promoting phorbol esters and activated ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase. Proc. Natl. Acad. Sci. USA 101:13489-94
    • (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
  • 82
    • 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 LE, Pratt PF, Proud CG. 2005. 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. 388:973-84
    • (2005) Biochem. J , vol.388 , pp. 973-984
    • Rolfe, M.1    McLeod, L.E.2    Pratt, P.F.3    Proud, C.G.4
  • 83
    • 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, Pandolfi PP. 2005. Phosphorylation and functional inactivation of TSC2 by erk implications for tuberous sclerosis and cancer pathogenesis. Cell 121:179-93
    • (2005) Cell , vol.121 , pp. 179-193
    • Ma, L.1    Chen, Z.2    Erdjument-Bromage, H.3    Tempst, P.4    Pandolfi, P.P.5
  • 84
    • 0028907314 scopus 로고
    • Role of p70 S6 protein kinase in angiotensin II-induced protein synthesis in vascular smooth muscle cells
    • Giasson E, Meloche S. 1995. Role of p70 S6 protein kinase in angiotensin II-induced protein synthesis in vascular smooth muscle cells. J. Biol. Chem. 270:5225-31
    • (1995) J. Biol. Chem , vol.270 , pp. 5225-5231
    • Giasson, E.1    Meloche, S.2
  • 86
    • 0141863201 scopus 로고    scopus 로고
    • Sirolimus-eluting stents for treatment of patients with long atherosclerotic lesions in small coronary arteries: Double-blind, randomised controlled trial (E-SIRIUS)
    • Schofer J, Schluter M, Gershlick AH, Wijns W, Garcia E, et al. 2003. Sirolimus-eluting stents for treatment of patients with long atherosclerotic lesions in small coronary arteries: double-blind, randomised controlled trial (E-SIRIUS). Lancet 362:1093-99
    • (2003) Lancet , vol.362 , pp. 1093-1099
    • Schofer, J.1    Schluter, M.2    Gershlick, A.H.3    Wijns, W.4    Garcia, E.5
  • 87
    • 0141765805 scopus 로고    scopus 로고
    • Sirolimus-eluting stents versus standard stents in patients with stenosis in a native coronary artery
    • Moses JW, Leon MB, Popma JJ, Fitzgerald PJ, Holmes DR, et al. 2003. Sirolimus-eluting stents versus standard stents in patients with stenosis in a native coronary artery. N. Engl. J. Med. 349:1315-23
    • (2003) N. Engl. J. Med , vol.349 , pp. 1315-1323
    • Moses, J.W.1    Leon, M.B.2    Popma, J.J.3    Fitzgerald, P.J.4    Holmes, D.R.5
  • 88
    • 0344256490 scopus 로고    scopus 로고
    • What's major about adverse cardiac events?
    • Silberberg J. 2003. What's major about adverse cardiac events? Lancet 362:1860
    • (2003) Lancet , vol.362 , pp. 1860
    • Silberberg, J.1
  • 89
    • 33645416990 scopus 로고    scopus 로고
    • Two-year outcomes after sirolimus-eluting stent implantation: Results from the sirolimus-eluting stent in de novo native coronary lesions (SIRIUS) trial
    • Weisz G, Leon MB, Holmes DRJ, Kereiakes DJ, Clark MR, et al. 2006. Two-year outcomes after sirolimus-eluting stent implantation: results from the sirolimus-eluting stent in de novo native coronary lesions (SIRIUS) trial. J. Am. Coll. Cardiol. 47:1350-55
    • (2006) J. Am. Coll. Cardiol , vol.47 , pp. 1350-1355
    • Weisz, G.1    Leon, M.B.2    Holmes, D.R.J.3    Kereiakes, D.J.4    Clark, M.R.5
  • 90
    • 0027181166 scopus 로고
    • Cellular hypertrophy and hyperplasia of airway smooth muscles underlying bronchial asthma. A 3-D morphometric study
    • Ebina M, Takahashi T, Chiba T, Motomiya M. 1993. Cellular hypertrophy and hyperplasia of airway smooth muscles underlying bronchial asthma. A 3-D morphometric study. Am. Rev. Respir. Dis. 148:720-26
    • (1993) Am. Rev. Respir. Dis , vol.148 , pp. 720-726
    • Ebina, M.1    Takahashi, T.2    Chiba, T.3    Motomiya, M.4
  • 91
    • 0037438424 scopus 로고    scopus 로고
    • In vivo and in vitro effects of SAR 943, a rapamycin analogue, on airway inflammation and remodeling
    • Fujitani Y, Trifilieff A. 2003. In vivo and in vitro effects of SAR 943, a rapamycin analogue, on airway inflammation and remodeling. Am. J. Respir. Crit. Care Med. 167:193-98
    • (2003) Am. J. Respir. Crit. Care Med , vol.167 , pp. 193-198
    • Fujitani, Y.1    Trifilieff, A.2
  • 92
    • 0037163033 scopus 로고    scopus 로고
    • Tuberin regulates p70 S6 kinase activation and ribosomal protein S6 phosphorylation. A role for the TSC2 tumor suppressor gene in pulmonary lymphangioleiomyomatosis (LAM)
    • Goncharova EA, Goncharov DA, Eszterhas A, Hunter DS, Glassberg MK, et al. 2002. Tuberin regulates p70 S6 kinase activation and ribosomal protein S6 phosphorylation. A role for the TSC2 tumor suppressor gene in pulmonary lymphangioleiomyomatosis (LAM). J. Biol. Chem. 277:30958-67
    • (2002) J. Biol. Chem , vol.277 , pp. 30958-30967
    • Goncharova, E.A.1    Goncharov, D.A.2    Eszterhas, A.3    Hunter, D.S.4    Glassberg, M.K.5
  • 94
    • 23144467910 scopus 로고    scopus 로고
    • An expanding role for mTOR in cancer
    • Guertin DA, Sabatini DM. 2005. An expanding role for mTOR in cancer. Trends Mol. Med. 11:353-61
    • (2005) Trends Mol. Med , vol.11 , pp. 353-361
    • Guertin, D.A.1    Sabatini, D.M.2
  • 95
    • 0034700456 scopus 로고    scopus 로고
    • Hypoinsulinaemia, glucose intolerance and diminished beta-cell size in S6K1-deficient mice
    • Pende M, Kozma SC, Jaquet M, Oorschot V, Burcelin R, et al. 2000. Hypoinsulinaemia, glucose intolerance and diminished beta-cell size in S6K1-deficient mice. Nature 408:994-97
    • (2000) Nature , vol.408 , pp. 994-997
    • Pende, M.1    Kozma, S.C.2    Jaquet, M.3    Oorschot, V.4    Burcelin, R.5
  • 96
    • 33646351055 scopus 로고    scopus 로고
    • Ablation of PDK1 in pancreatic beta cells induces diabetes as a result of loss of beta cell mass
    • Hashimoto N, Kido Y, Uchida T, Asahara S, Shigeyama Y, et al. 2006. Ablation of PDK1 in pancreatic beta cells induces diabetes as a result of loss of beta cell mass. Nat. Genet. 38:589-93
    • (2006) Nat. Genet , vol.38 , pp. 589-593
    • Hashimoto, N.1    Kido, Y.2    Uchida, T.3    Asahara, S.4    Shigeyama, Y.5
  • 97
    • 23944491271 scopus 로고    scopus 로고
    • Role of mammalian target of rapamycin signaling in compensatory renal hypertrophy
    • Chen JK, Chen J, Neilson EG, Harris RC. 2005. Role of mammalian target of rapamycin signaling in compensatory renal hypertrophy. J. Am. Soc. Nephrol. 16:1384-91
    • (2005) J. Am. Soc. Nephrol , vol.16 , pp. 1384-1391
    • Chen, J.K.1    Chen, J.2    Neilson, E.G.3    Harris, R.C.4
  • 99
    • 33646352217 scopus 로고    scopus 로고
    • Mammalian target of rapamycin pathway blockade slows progression of diabetic kidney disease in rats
    • Lloberas N, Cruzado JM, Franquesa M, Herrero-Fresneda I, Torras J, et al. 2006. Mammalian target of rapamycin pathway blockade slows progression of diabetic kidney disease in rats. J. Am. Soc. Nephrol. 17:1395-404
    • (2006) J. Am. Soc. Nephrol , vol.17 , pp. 1395-1404
    • Lloberas, N.1    Cruzado, J.M.2    Franquesa, M.3    Herrero-Fresneda, I.4    Torras, J.5
  • 100
    • 26944446228 scopus 로고    scopus 로고
    • Gas6 induces Akt/mTOR-mediated mesangial hypertrophy in diabetic nephropathy
    • Nagai K, Matsubara T, Mima A, Sumi E, Kanamori H, et al. 2005. Gas6 induces Akt/mTOR-mediated mesangial hypertrophy in diabetic nephropathy. Kidney Int. 68:552-61
    • (2005) Kidney Int , vol.68 , pp. 552-561
    • Nagai, K.1    Matsubara, T.2    Mima, A.3    Sumi, E.4    Kanamori, H.5
  • 101
    • 4344563878 scopus 로고    scopus 로고
    • Role and regulation of starvation-induced autophagy in the drosophila fat body
    • Scott RC, Schuldiner O, Neufeld TP. 2004. Role and regulation of starvation-induced autophagy in the drosophila fat body. Dev. Cell 7:167-78
    • (2004) Dev. Cell , vol.7 , pp. 167-178
    • Scott, R.C.1    Schuldiner, O.2    Neufeld, T.P.3
  • 102
    • 4344608793 scopus 로고    scopus 로고
    • Programmed autophagy in the drosophila fat body is induced by ecdysone through regulation of the PI3K pathway
    • Rusten TE, Lindmo K, Juhasz G, Sass M, Seglen PO, et al. 2004. Programmed autophagy in the drosophila fat body is induced by ecdysone through regulation of the PI3K pathway. Dev. Cell 7:179-92
    • (2004) Dev. Cell , vol.7 , pp. 179-192
    • Rusten, T.E.1    Lindmo, K.2    Juhasz, G.3    Sass, M.4    Seglen, P.O.5
  • 103
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of huntington disease
    • Ravikumar B, Vacher C, Berger Z, Davies JE, Luo S, et al. 2004. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of huntington disease. Nat. Genet. 36:585-95
    • (2004) Nat. Genet , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3    Davies, J.E.4    Luo, S.5
  • 106
    • 33847025383 scopus 로고    scopus 로고
    • Akt regulates nuclear/cytoplasmic localization of tuberin
    • In press
    • Rosner M, Freilinger A, Hengstschlager M. 2006. Akt regulates nuclear/cytoplasmic localization of tuberin. Oncogene. In press
    • (2006) Oncogene
    • Rosner, M.1    Freilinger, A.2    Hengstschlager, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.