메뉴 건너뛰기




Volumn 302, Issue 11, 2012, Pages

Leucine and mTORC1: A complex relationship

Author keywords

Autophagy; Mammalian target of rapamycin complex 1; Muscle; Rag guanosine triphosphatase; System A transporter 2; System L transporter 1

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENYLATE KINASE; AMINO ACID TRANSPORTER; CARRIER PROTEIN; CD98 ANTIGEN; GLUTAMINE; GUANOSINE TRIPHOSPHATASE; INOSITOL POLYPHOSPHATE MULTIKINASE; INSULIN; LAT1 PROTEIN; LEUCINE; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE KINASE 3; MUSCLE PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOTRANSFERASE; PROTEIN KINASE B; RAG A PROTEIN; RAG B PROTEIN; RAG C PROTEIN; RAG D PROTEIN; RHEB PROTEIN; SNAT2 PROTEIN; STAT3 PROTEIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE UBR2; UNCLASSIFIED DRUG;

EID: 84861840965     PISSN: 01931849     EISSN: 15221555     Source Type: Journal    
DOI: 10.1152/ajpendo.00525.2011     Document Type: Review
Times cited : (189)

References (114)
  • 1
    • 0033980371 scopus 로고    scopus 로고
    • Orally administered leucine stimulates protein synthesis in skeletal muscle of postabsorptive rats in association with increased eIF4F formation
    • Anthony JC, Anthony TG, Kimball SR, Vary TC, Jefferson LS. Orally administered leucine stimulates protein synthesis in skeletal muscle of postabsorptive rats in association with increased eIF4F formation. J Nutr 130: 139-145, 2000.
    • (2000) J Nutr , vol.130 , pp. 139-145
    • Anthony, J.C.1    Anthony, T.G.2    Kimball, S.R.3    Vary, T.C.4    Jefferson, L.S.5
  • 3
    • 42549118675 scopus 로고    scopus 로고
    • The Tsc/Rheb signaling pathway controls basic amino acid uptake via the Cat1 permease in fission yeast
    • Aspuria PJ, Tamanoi F. The Tsc/Rheb signaling pathway controls basic amino acid uptake via the Cat1 permease in fission yeast. Mol Genet Genomics 279: 441-450, 2008.
    • (2008) Mol Genet Genomics , vol.279 , pp. 441-450
    • Aspuria, P.J.1    Tamanoi, F.2
  • 4
    • 36049043184 scopus 로고    scopus 로고
    • Rheb activates mTOR by antagonizing its endogenous inhibitor, FKBP38
    • Bai X, Ma D, Liu A, Shen X, Wang QJ, Liu Y, Jiang Y. Rheb activates mTOR by antagonizing its endogenous inhibitor, FKBP38. Science 318: 977-980, 2007.
    • (2007) Science , vol.318 , pp. 977-980
    • Bai, X.1    Ma, D.2    Liu, A.3    Shen, X.4    Wang, Q.J.5    Liu, Y.6    Jiang, Y.7
  • 5
    • 69049097269 scopus 로고    scopus 로고
    • Tertiary active transport of amino acids reconstituted by coexpression of System A and L transporters in Xenopus oocytes
    • Baird FE, Bett KJ, MacLean C, Tee AR, Hundal HS, Taylor PM. Tertiary active transport of amino acids reconstituted by coexpression of System A and L transporters in Xenopus oocytes. Am J Physiol Endocrinol Metab 297: E822-E829, 2009.
    • (2009) Am J Physiol Endocrinol Metab , vol.297
    • Baird, F.E.1    Bett, K.J.2    McLean, C.3    Tee, A.R.4    Hundal, H.S.5    Taylor, P.M.6
  • 9
    • 25444457577 scopus 로고    scopus 로고
    • hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase
    • Byfield MP, Murray JT, Backer JM. hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase. J Biol Chem 280: 33076-33082, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 33076-33082
    • Byfield, M.P.1    Murray, J.T.2    Backer, J.M.3
  • 10
    • 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. Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin-and farnesylation-dependent manner. J Biol Chem 278: 32493-32496, 2003.
    • (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
  • 11
    • 0037732600 scopus 로고    scopus 로고
    • LST8 negatively regulates amino acid biosynthesis as a component of the TOR pathway
    • Chen EJ, Kaiser CA. LST8 negatively regulates amino acid biosynthesis as a component of the TOR pathway. J Cell Biol 161: 333-347, 2003.
    • (2003) J Cell Biol , vol.161 , pp. 333-347
    • Chen, E.J.1    Kaiser, C.A.2
  • 12
    • 29244439931 scopus 로고    scopus 로고
    • A leucine-supplemented diet restores the defective postprandial inhibition of proteasome-dependent proteolysis in aged rat skeletal muscle
    • Combaret L, Dardevet D, Rieu I, Pouch MN, Béchet D, Taillandier D, Grizard J, Attaix D. A leucine-supplemented diet restores the defective postprandial inhibition of proteasome-dependent proteolysis in aged rat skeletal muscle. J Physiol 569: 489-499, 2005.
    • (2005) J Physiol , vol.569 , pp. 489-499
    • Combaret, L.1    Dardevet, D.2    Rieu, I.3    Pouch, M.N.4    Béchet, D.5    Taillandier, D.6    Grizard, J.7    Attaix, D.8
  • 13
    • 0033735644 scopus 로고    scopus 로고
    • Stimulation of in vitro rat muscle protein synthesis by leucine decreases with age
    • Dardevet D, Sornet C, Balage M, Grizard J. Stimulation of in vitro rat muscle protein synthesis by leucine decreases with age. J Nutr 130: 2630-2635, 2000.
    • (2000) J Nutr , vol.130 , pp. 2630-2635
    • Dardevet, D.1    Sornet, C.2    Balage, M.3    Grizard, J.4
  • 15
    • 66149097065 scopus 로고    scopus 로고
    • Nutritional and contractile regulation of human skeletal muscle protein synthesis and mTORC1 signaling
    • Drummond MJ, Dreyer HC, Fry CS, Glynn EL, Rasmussen BB. Nutritional and contractile regulation of human skeletal muscle protein synthesis and mTORC1 signaling. J Appl Physiol 106: 1374-1384, 2009.
    • (2009) J Appl Physiol , vol.106 , pp. 1374-1384
    • Drummond, M.J.1    Dreyer, H.C.2    Fry, C.S.3    Glynn, E.L.4    Rasmussen, B.B.5
  • 17
    • 79960014848 scopus 로고    scopus 로고
    • ULK1 inhibits mTORC1 signaling, promotes multisite Raptor phosphorylation and hinders substrate binding
    • Dunlop EA, Hunt Acosta-Jaquez DKHA, Fingar DC, Tee AR. ULK1 inhibits mTORC1 signaling, promotes multisite Raptor phosphorylation and hinders substrate binding. Autophagy 7: 737-747, 2011.
    • (2011) Autophagy , vol.7 , pp. 737-747
    • Dunlop, E.A.1    Hunt Acosta-Jaquez, D.K.H.A.2    Fingar, D.C.3    Tee, A.R.4
  • 18
    • 62749096589 scopus 로고    scopus 로고
    • Mammalian target of rapamycin complex 1: Signalling inputs, substrates and feedback mechanisms
    • Dunlop EA, Tee AR. Mammalian target of rapamycin complex 1: Signalling inputs, substrates and feedback mechanisms. Cell Signalling 21: 827-835, 2009.
    • (2009) Cell Signalling , vol.21 , pp. 827-835
    • Dunlop, E.A.1    Tee, A.R.2
  • 20
    • 0036320205 scopus 로고    scopus 로고
    • Akt maintains cell size and survival by increasing mtor-dependent nutrient uptake
    • Edinger AL, Thompson CB. Akt maintains cell size and survival by increasing mtor-dependent nutrient uptake. Mol Biol Cell 13: 2276-2288, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 2276-2288
    • Edinger, A.L.1    Thompson, C.B.2
  • 22
    • 80053476420 scopus 로고    scopus 로고
    • The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR
    • Egan DJK, Shaw RJ, Guan KL. The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR. Autophagy 7: 643-644, 2011.
    • (2011) Autophagy , vol.7 , pp. 643-644
    • Egan, D.J.K.1    Shaw, R.J.2    Guan, K.L.3
  • 24
    • 34248140159 scopus 로고    scopus 로고
    • Acidosis-sensing glutamine pump SNAT2 determines amino acid levels and mammalian target of rapamycin signalling to protein synthesis in L6 muscle cells
    • Evans K, Nasim Z, Brown J, Butler H, Kauser S, Varoqui H, Erickson JD, Herbert TP, Bevington A. Acidosis-sensing glutamine pump SNAT2 determines amino acid levels and mammalian target of rapamycin signalling to protein synthesis in L6 muscle cells. J Am Soc Nephrol 18: 1426-1436, 2007.
    • (2007) J Am Soc Nephrol , vol.18 , pp. 1426-1436
    • Evans, K.1    Nasim, Z.2    Brown, J.3    Butler, H.4    Kauser, S.5    Varoqui, H.6    Erickson, J.D.7    Herbert, T.P.8    Bevington, A.9
  • 26
    • 34147141941 scopus 로고    scopus 로고
    • A MAP4 kinase related to Ste20 is a nutrient-sensitive regulator of mTOR signalling
    • Findlay GM, Yan L, Procter J, Mieulet V, Lamb RF. A MAP4 kinase related to Ste20 is a nutrient-sensitive regulator of mTOR signalling. Biochem J 403: 13-20, 2007.
    • (2007) Biochem J , vol.403 , pp. 13-20
    • Findlay, G.M.1    Yan, L.2    Procter, J.3    Mieulet, V.4    Lamb, R.F.5
  • 29
    • 77953543377 scopus 로고    scopus 로고
    • The Beclin 1-VPS34 complex-at the crossroads of autophagy and beyond
    • Funderburk SF, Wang QJ, Yue Z. The Beclin 1-VPS34 complex-at the crossroads of autophagy and beyond. Trends Cell Biol 20: 355-362, 2010.
    • (2010) Trends Cell Biol , vol.20 , pp. 355-362
    • Funderburk, S.F.1    Wang, Q.J.2    Yue, Z.3
  • 30
    • 21044440310 scopus 로고    scopus 로고
    • PAT-related amino acid transporters regulate growth via a novel mechanism that does not require bulk transport of amino acids
    • Goberdhan DCI, Meredith D, Boyd CAR, Wilson C. PAT-related amino acid transporters regulate growth via a novel mechanism that does not require bulk transport of amino acids. Development 132: 2365-2375, 2005.
    • (2005) Development , vol.132 , pp. 2365-2375
    • Goberdhan, D.C.I.1    Meredith, D.2    Boyd, C.A.R.3    Wilson, C.4
  • 31
    • 79959445342 scopus 로고    scopus 로고
    • The actions of exogenous leucine on mTOR signalling and amino acid transporters in human myotubes
    • Gran P, Cameron-Smith D. The actions of exogenous leucine on mTOR signalling and amino acid transporters in human myotubes. BMC Physiol 11: 10, 2011.
    • (2011) BMC Physiol , vol.11 , pp. 10
    • Gran, P.1    Cameron-Smith, D.2
  • 34
    • 77955360284 scopus 로고    scopus 로고
    • A Limited role for PI(3,4,5)P regulation in controlling skeletal muscle mass in response to resistance exercise
    • Hamilton DL, Philp A, MacKenzie MG, Baar K. A Limited role for PI(3,4,5)P regulation in controlling skeletal muscle mass in response to resistance exercise. PLos One 5: e11624, 2010.
    • (2010) PLos One , vol.5
    • Hamilton, D.L.1    Philp, A.2    McKenzie, M.G.3    Baar, K.4
  • 35
    • 0032486268 scopus 로고    scopus 로고
    • Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism
    • Hara K, Yonezawa K, Weng QP, Kozlowski MT, Belham C, Avruch J. Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism. J Biol Chem 273: 14484-14494, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 14484-14494
    • Hara, K.1    Yonezawa, K.2    Weng, Q.P.3    Kozlowski, M.T.4    Belham, C.5    Avruch, J.6
  • 36
    • 34548036471 scopus 로고    scopus 로고
    • Plasticity of human skeletal muscle: Gene expression to in vivo function
    • Harridge SDR. Plasticity of human skeletal muscle: gene expression to in vivo function. Exp Physiol 92: 783-797, 2007.
    • (2007) Exp Physiol , vol.92 , pp. 783-797
    • Harridge, S.D.R.1
  • 37
  • 40
    • 14644417747 scopus 로고    scopus 로고
    • Ceramide down-regulates System A amino acid transport and protein synthesis in rat skeletal muscle cells
    • Hyde R, Hajduch E, Powell DJ, Taylor PM, Hundal HS. Ceramide down-regulates System A amino acid transport and protein synthesis in rat skeletal muscle cells. FASEB J 19: 461-463, 2005.
    • (2005) FASEB J , vol.19 , pp. 461-463
    • Hyde, R.1    Hajduch, E.2    Powell, D.J.3    Taylor, P.M.4    Hundal, H.S.5
  • 41
    • 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. Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Dev 17: 1829-1834, 2003.
    • (2003) Genes Dev , vol.17 , pp. 1829-1834
    • Inoki, K.1    Li, Y.2    Xu, T.3    Guan, K.L.4
  • 42
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki K, Zhu T, Guan KL. TSC2 mediates cellular energy response to control cell growth and survival. Cell 115: 577-590, 2003.
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 44
    • 70449623354 scopus 로고    scopus 로고
    • IL-6 stimulates system A amino acid transporter activity in trophoblast cells through STAT3 and increased expression of SNAT2
    • Jones HN, Jansson T, Powell TL. IL-6 stimulates system A amino acid transporter activity in trophoblast cells through STAT3 and increased expression of SNAT2. Am J Physiol Cell Physiol 297: C1228-C1235, 2009.
    • (2009) Am J Physiol Cell Physiol , vol.297
    • Jones, H.N.1    Jansson, T.2    Powell, T.L.3
  • 45
    • 44149127993 scopus 로고    scopus 로고
    • The class III PI(3)K Vps34 promotes autophagy and endocytosis but not TOR signaling in Drosophila
    • Juhász G, Hill JH, Yan Y, Sass M, Baehrecke EH, Backer JM, Neufeld TP. The class III PI(3)K Vps34 promotes autophagy and endocytosis but not TOR signaling in Drosophila. J Cell Biol 181: 655-666, 2008.
    • (2008) J Cell Biol , vol.181 , pp. 655-666
    • Juhász, G.1    Hill, J.H.2    Yan, Y.3    Sass, M.4    Baehrecke, E.H.5    Backer, J.M.6    Neufeld, T.P.7
  • 47
    • 80053430528 scopus 로고    scopus 로고
    • ULK1 inhibits the kinase activity of mTORC1 and cell proliferation
    • Jung CH, Seo M, Otto NM, Do KH. ULK1 inhibits the kinase activity of mTORC1 and cell proliferation. Autophagy 7: 1212-1221, 2011.
    • (2011) Autophagy , vol.7 , pp. 1212-1221
    • Jung, C.H.1    Seo, M.2    Otto, N.M.3    Do, K.H.4
  • 51
    • 41249094257 scopus 로고    scopus 로고
    • Rapid turnover of the mTOR Complex 1 (mTORC1) repressor REDD1 and activation of mTORC1 signaling following inhibition of protein synthesis
    • Kimball SR, Do AND, Kutzler L, Cavener DR, Jefferson LS. Rapid turnover of the mTOR Complex 1 (mTORC1) repressor REDD1 and activation of mTORC1 signaling following inhibition of protein synthesis. J Biol Chem 283: 3465-3475, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 3465-3475
    • Kimball, S.R.1    Do, A.N.D.2    Kutzler, L.3    Cavener, D.R.4    Jefferson, L.S.5
  • 52
    • 0346996344 scopus 로고    scopus 로고
    • Regulation of global and specific mRNA translation by oral administration of branched-chain amino acids
    • Kimball SR, Jefferson LS. Regulation of global and specific mRNA translation by oral administration of branched-chain amino acids. Biochem Biophys Res Commun 313: 423-427, 2004.
    • (2004) Biochem Biophys Res Commun , vol.313 , pp. 423-427
    • Kimball, S.R.1    Jefferson, L.S.2
  • 53
    • 77956740779 scopus 로고    scopus 로고
    • Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals
    • Kogan K, Spear ED, Kaiser CA, Fass D. Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals. J Mol Biol 402: 388-398, 2010.
    • (2010) J Mol Biol , vol.402 , pp. 388-398
    • Kogan, K.1    Spear, E.D.2    Kaiser, C.A.3    Fass, D.4
  • 56
    • 77954671228 scopus 로고    scopus 로고
    • Role of N-end rule ubiquitin ligases UBR1 and UBR2 in regulating the leucine-mTOR signaling pathway
    • Kume K, Iizumi Y, Shimada M, Ito Y, Kishi T, Yamaguchi Y, Handa H. Role of N-end rule ubiquitin ligases UBR1 and UBR2 in regulating the leucine-mTOR signaling pathway. Genes to Cells 15: 339-349, 2010.
    • (2010) Genes to Cells , vol.15 , pp. 339-349
    • Kume, K.1    Iizumi, Y.2    Shimada, M.3    Ito, Y.4    Kishi, T.5    Yamaguchi, Y.6    Handa, H.7
  • 57
    • 50149086076 scopus 로고    scopus 로고
    • TUSC4/ NPRL2, a novel PDK1-interacting protein, inhibits PDK1 tyrosine phosphorylation and its downstream signaling
    • Kurata A, Katayama R, Watanabe T, Tsuruo T, Fujita N. TUSC4/ NPRL2, a novel PDK1-interacting protein, inhibits PDK1 tyrosine phosphorylation and its downstream signaling. Cancer Sci 99: 1827-1834, 2008.
    • (2008) Cancer Sci , vol.99 , pp. 1827-1834
    • Kurata, A.1    Katayama, R.2    Watanabe, T.3    Tsuruo, T.4    Fujita, N.5
  • 58
    • 70350418625 scopus 로고    scopus 로고
    • mTOR signaling at a glance
    • Laplante M, Sabatini DM. mTOR signaling at a glance. J Cell Sci 122: 3589-3594, 2009.
    • (2009) J Cell Sci , vol.122 , pp. 3589-3594
    • Laplante, M.1    Sabatini, D.M.2
  • 59
    • 77649251207 scopus 로고    scopus 로고
    • mTORC1 activates SREBP-1c and uncouples lipogenesis from gluconeogenesis
    • Laplante M, Sabatini DM. mTORC1 activates SREBP-1c and uncouples lipogenesis from gluconeogenesis. Proc Natl Acad Sci USA 107: 3281-3282, 2010.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3281-3282
    • Laplante, M.1    Sabatini, D.M.2
  • 60
    • 31544440119 scopus 로고    scopus 로고
    • Potential importance of leucine in treatment of obesity and the metabolic syndrome
    • Layman DK, Walker DA. Potential importance of leucine in treatment of obesity and the metabolic syndrome. J Nutr 136: 319S-323S, 2006.
    • (2006) J Nutr , vol.136
    • Layman, D.K.1    Walker, D.A.2
  • 61
    • 78149476877 scopus 로고    scopus 로고
    • The association of AMPK with ULK1 regulates autophagy
    • Lee JW, Park S, Takahashi Y, Wang HG. The association of AMPK with ULK1 regulates autophagy. PLos One 5: e15394, 2010.
    • (2010) PLos One , vol.5
    • Lee, J.W.1    Park, S.2    Takahashi, Y.3    Wang, H.G.4
  • 62
    • 34047154536 scopus 로고    scopus 로고
    • ATG1, an autophagy regulator, inhibits cell growth by negatively regulating S6 kinase
    • Lee SB, Kim S, Lee J, Park J, Lee G, Kim Y, Kim JM, Chung J. ATG1, an autophagy regulator, inhibits cell growth by negatively regulating S6 kinase. EMBO Rep 8: 360-365, 2007.
    • (2007) EMBO Rep , vol.8 , pp. 360-365
    • Lee, S.B.1    Kim, S.2    Lee, J.3    Park, J.4    Lee, G.5    Kim, Y.6    Kim, J.M.7    Chung, J.8
  • 64
    • 3042701853 scopus 로고    scopus 로고
    • Platelet-derived growth factor stimulates LAT1 gene expression in vascular smooth muscle: Role in cell growth
    • Liu X, Reyna S, Ensenat D, Peyton K, Wang H, Schafer A, Durante W. Platelet-derived growth factor stimulates LAT1 gene expression in vascular smooth muscle: role in cell growth. FASEB J 18: 768-770, 2004.
    • (2004) FASEB J , vol.18 , pp. 768-770
    • Liu, X.1    Reyna, S.2    Ensenat, D.3    Peyton, K.4    Wang, H.5    Schafer, A.6    Durante, W.7
  • 65
    • 41949101770 scopus 로고    scopus 로고
    • SKAR links Pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs
    • Ma XM, Yoon SO, Richardson CJ, Jülich K, Blenis J. SKAR links Pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs. Cell 133: 303-313, 2008.
    • (2008) Cell , vol.133 , pp. 303-313
    • Ma, X.M.1    Yoon, S.O.2    Richardson, C.J.3    Jülich, K.4    Blenis, J.5
  • 66
    • 58049216316 scopus 로고    scopus 로고
    • RalA functions as an indispensable signal mediator for the nutrient-sensing system
    • Maehama T, Tanaka M, Nishina H, Murakami M, Kanaho Y, Hanada K. RalA functions as an indispensable signal mediator for the nutrient-sensing system. J Biol Chem 283: 35053-35059, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 35053-35059
    • Maehama, T.1    Tanaka, M.2    Nishina, H.3    Murakami, M.4    Kanaho, Y.5    Hanada, K.6
  • 67
    • 77956697347 scopus 로고    scopus 로고
    • Chapter 2. Cell signaling in protein synthesis: Ribosome biogenesis and translation initiation and elongation
    • In:, edited by John WBH. New York: Academic
    • Mahoney SJ, Dempsey JM, Blenis J. Chapter 2. Cell signaling in protein synthesis: ribosome biogenesis and translation initiation and elongation. In: Progress in Molecular Biology and Translational Science, edited by John WBH. New York: Academic, 2009, p. 53-107.
    • (2009) Progress in Molecular Biology and Translational Science , pp. 53-107
    • Mahoney, S.J.1    Dempsey, J.M.2    Blenis, J.3
  • 69
  • 70
    • 0036141543 scopus 로고    scopus 로고
    • Rapid suppression of protein degradation in skeletal muscle after oral feeding of leucine in rats
    • Nagasawa T, Kido T, Yoshizawa F, Ito Y, Nishizawa N. Rapid suppression of protein degradation in skeletal muscle after oral feeding of leucine in rats. J Nutr Biochem 13: 121-127, 2002.
    • (2002) J Nutr Biochem , vol.13 , pp. 121-127
    • Nagasawa, T.1    Kido, T.2    Yoshizawa, F.3    Ito, Y.4    Nishizawa, N.5
  • 71
    • 24644499561 scopus 로고    scopus 로고
    • Leucine suppresses myofibrillar proteolysis by down-regulating ubiquitin-proteasome pathway in chick skeletal muscles
    • Nakashima K, Ishida A, Yamazaki M, Abe H. Leucine suppresses myofibrillar proteolysis by down-regulating ubiquitin-proteasome pathway in chick skeletal muscles. Biochem Biophys Res Commun 336: 660-666, 2005.
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 660-666
    • Nakashima, K.1    Ishida, A.2    Yamazaki, M.3    Abe, H.4
  • 72
    • 67651235863 scopus 로고    scopus 로고
    • A genome-wide screen for regulators of TORC1 in response to amino acid starvation reveals a conserved Npr2/3 complex
    • Neklesa TK, Davis RW. A genome-wide screen for regulators of TORC1 in response to amino acid starvation reveals a conserved Npr2/3 complex. PLoS Genet 5: e1000515, 2009.
    • (2009) PLoS Genet , vol.5
    • Neklesa, T.K.1    Davis, R.W.2
  • 76
    • 33847743064 scopus 로고    scopus 로고
    • hvps34, an ancient player, enters a growing game: MTOR Complex1/S6K1 signaling
    • Nobukuni T, Kozma SC, Thomas G. hvps34, an ancient player, enters a growing game: mTOR Complex1/S6K1 signaling. Curr Opin Cell Biol 19: 135-141, 2007.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 135-141
    • Nobukuni, T.1    Kozma, S.C.2    Thomas, G.3
  • 77
    • 34247568898 scopus 로고    scopus 로고
    • The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis
    • Peplowska K, Markgraf DF, Ostrowicz CW, Bange G, Ungermann C. The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis. Dev Cell 12: 739-750, 2007.
    • (2007) Dev Cell , vol.12 , pp. 739-750
    • Peplowska, K.1    Markgraf, D.F.2    Ostrowicz, C.W.3    Bange, G.4    Ungermann, C.5
  • 78
    • 28444434793 scopus 로고    scopus 로고
    • eIF3: A connector of S6K1 to the translation preinitiation complex
    • Peterson TR, Sabatini DM. eIF3: a connector of S6K1 to the translation preinitiation complex. Mol Cell 20: 655-657, 2005.
    • (2005) Mol Cell , vol.20 , pp. 655-657
    • Peterson, T.R.1    Sabatini, D.M.2
  • 79
    • 0034283186 scopus 로고    scopus 로고
    • L-leucine availability regulates phosphatidylinositol 3-kinase, p70 S6 kinase and glycogen synthase kinase-3 activity in L6 muscle cells: Evidence for the involvement of the mammalian target of rapamycin (mTOR) pathway in the L-leucine-induced up-regulation of system A amino acid transport
    • Peyrollier K, Hajduch E, Blair AS, Hyde R, Hundal HS. L-leucine availability regulates phosphatidylinositol 3-kinase, p70 S6 kinase and glycogen synthase kinase-3 activity in L6 muscle cells: evidence for the involvement of the mammalian target of rapamycin (mTOR) pathway in the L-leucine-induced up-regulation of system A amino acid transport. Biochem J 350: 361-368, 2000.
    • (2000) Biochem J , vol.350 , pp. 361-368
    • Peyrollier, K.1    Hajduch, E.2    Blair, A.S.3    Hyde, R.4    Hundal, H.S.5
  • 81
    • 0347627139 scopus 로고    scopus 로고
    • mTOR-mediated regulation of translation factors by amino acids
    • Proud C. mTOR-mediated regulation of translation factors by amino acids. Biochem Biophys Res Commun 313: 429-436, 2004.
    • (2004) Biochem Biophys Res Commun , vol.313 , pp. 429-436
    • Proud, C.1
  • 82
    • 13444259647 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by eIF4E inhibitory proteins
    • Richter JD, Sonenberg N. Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature 433: 477-480, 2005.
    • (2005) Nature , vol.433 , pp. 477-480
    • Richter, J.D.1    Sonenberg, N.2
  • 83
    • 33746876019 scopus 로고    scopus 로고
    • Leucine supplementation improves muscle protein synthesis in elderly men independently of hyperaminoacidaemia
    • Rieu I, Balage M, Sornet C, Giraudet C, Pujos E, Grizard J, Mosoni L, Dardevet D. Leucine supplementation improves muscle protein synthesis in elderly men independently of hyperaminoacidaemia. J Physiol 575: 305-315, 2006.
    • (2006) J Physiol , vol.575 , pp. 305-315
    • Rieu, I.1    Balage, M.2    Sornet, C.3    Giraudet, C.4    Pujos, E.5    Grizard, J.6    Mosoni, L.7    Dardevet, D.8
  • 84
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink J, Ghigo E, Kalaidzidis Y, Zerial M. Rab conversion as a mechanism of progression from early to late endosomes. Cell 122: 735-749, 2005.
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 85
    • 58349106216 scopus 로고    scopus 로고
    • Regulation of placental amino acid transporter activity by mammalian target of rapamycin
    • Roos S, Kanai Y, Prasad PD, Powell TL, Jansson T. Regulation of placental amino acid transporter activity by mammalian target of rapamycin. Am J Physiol Cell Physiol 296: C142-C150, 2009.
    • (2009) Am J Physiol Cell Physiol , vol.296
    • Roos, S.1    Kanai, Y.2    Prasad, P.D.3    Powell, T.L.4    Jansson, T.5
  • 86
    • 18244362311 scopus 로고    scopus 로고
    • Novel role of the small GTPase Rheb: Its implication in endocytic pathway independent of the activation of mammalian target of rapamycin
    • Saito K, Araki Y, Kontani K, Nishina H, Katada T. Novel role of the small GTPase Rheb: its implication in endocytic pathway independent of the activation of mammalian target of rapamycin. J Biochem 137: 423-430, 2005.
    • (2005) J Biochem , vol.137 , pp. 423-430
    • Saito, K.1    Araki, Y.2    Kontani, K.3    Nishina, H.4    Katada, T.5
  • 87
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • Sancak Y, Bar-Peled L, Zoncu R, Markhard AL, Nada S, Sabatini DM. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141: 290-303, 2010.
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3    Markhard, A.L.4    Nada, S.5    Sabatini, D.M.6
  • 89
    • 67649823420 scopus 로고    scopus 로고
    • Specific activation of mTORC1 by Rheb G-protein in vitro involves enhanced recruitment of its substrate protein
    • Sato T, Nakashima A, Guo L, Tamanoi F. Specific activation of mTORC1 by Rheb G-protein in vitro involves enhanced recruitment of its substrate protein. J Biol Chem 284: 12783-12791, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 12783-12791
    • Sato, T.1    Nakashima, A.2    Guo, L.3    Tamanoi, F.4
  • 90
    • 0038643484 scopus 로고    scopus 로고
    • Rheb promotes cell growth as a component of the insulin/TOR signalling network
    • Saucedo LJ, Gao X, Chiarelli DA, Li L, Pan D, Edgar BA. Rheb promotes cell growth as a component of the insulin/TOR signalling network. Nat Cell Biol 5: 566-571, 2003.
    • (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
  • 91
    • 79953211917 scopus 로고    scopus 로고
    • Nutrient starvation elicits an acute autophagic response mediated by Ulk1 dephosphorylation and its subsequent dissociation from AMPK
    • Shang L, Chen S, Du F, Li S, Zhao L, Wang X. Nutrient starvation elicits an acute autophagic response mediated by Ulk1 dephosphorylation and its subsequent dissociation from AMPK. Proc Nat Acad Sci USA 108: 4788-4793, 2011.
    • (2011) Proc Nat Acad Sci USA , vol.108 , pp. 4788-4793
    • Shang, L.1    Chen, S.2    Du, F.3    Li, S.4    Zhao, L.5    Wang, X.6
  • 92
    • 79961118336 scopus 로고    scopus 로고
    • AMPK and mTOR coordinate the regulation of Ulk1 and mammalian autophagy initiation
    • Shang L, Wang X. AMPK and mTOR coordinate the regulation of Ulk1 and mammalian autophagy initiation. Autophagy 7: 924-926, 2011.
    • (2011) Autophagy , vol.7 , pp. 924-926
    • Shang, L.1    Wang, X.2
  • 93
    • 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. 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: 18717-18727, 2005.
    • (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
  • 94
    • 0026564916 scopus 로고
    • Review: How amino acids get into cells: Mechanisms, models, menus, and mediators
    • Souba WW, Pacitti AJ. Review: How amino acids get into cells: mechanisms, models, menus, and mediators. J Parenter Enteral Nutr 16: 569-578, 1992.
    • (1992) J Parenter Enteral Nutr , vol.16 , pp. 569-578
    • Souba, W.W.1    Pacitti, A.J.2
  • 95
    • 37749027195 scopus 로고    scopus 로고
    • A functional insulin-like growth factor receptor is not necessary for load-induced skeletal muscle hypertrophy
    • Spangenburg EE, Le Roith D, Ward CW, Bodine SC. A functional insulin-like growth factor receptor is not necessary for load-induced skeletal muscle hypertrophy. J Physiol 586: 283-291, 2008.
    • (2008) J Physiol , vol.586 , pp. 283-291
    • Spangenburg, E.E.1    le Roith, D.2    Ward, C.W.3    Bodine, S.C.4
  • 96
    • 77950523750 scopus 로고    scopus 로고
    • Npr2, yeast homolog of the human tumor suppressor NPRL2, is a target of Grr1 required for adaptation to growth on diverse nitrogen sources
    • Spielewoy N, Guaderrama M, Wohlschlegel JA, Ashe M, Yates JR, III, Wittenberg C. Npr2, yeast homolog of the human tumor suppressor NPRL2, is a target of Grr1 required for adaptation to growth on diverse nitrogen sources. Eukaryotic Cell 9: 592-601, 2010.
    • (2010) Eukaryotic Cell , vol.9 , pp. 592-601
    • Spielewoy, N.1    Guaderrama, M.2    Wohlschlegel, J.A.3    Ashe, M.4    Yates III, J.R.5    Wittenberg, C.6
  • 99
    • 79953211540 scopus 로고    scopus 로고
    • Amino acids activate mammalian target of rapamycin Complex 2 (mTORC2) via PI3K/Akt signaling
    • Tato I, Bartrons R, Ventura F, Rosa JL. Amino acids activate mammalian target of rapamycin Complex 2 (mTORC2) via PI3K/Akt signaling. J Biol Chem 286: 6128-6142, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 6128-6142
    • Tato, I.1    Bartrons, R.2    Ventura, F.3    Rosa, J.L.4
  • 100
    • 0141733228 scopus 로고    scopus 로고
    • Inactivation of the tuberous sclerosis complex-1 and-2 gene products occurs by phosphoinositide 3-kinase/ Akt-dependent and-independent phosphorylation of tuberin
    • Tee AR, Anjum R, Blenis J. Inactivation of the tuberous sclerosis complex-1 and-2 gene products occurs by phosphoinositide 3-kinase/ Akt-dependent and-independent phosphorylation of tuberin. J Biol Chem 278: 37288-37296, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 37288-37296
    • Tee, A.R.1    Anjum, R.2    Blenis, J.3
  • 101
    • 12344262762 scopus 로고    scopus 로고
    • mTOR, translational control and human disease
    • Tee AR, Blenis J. mTOR, translational control and human disease. Sem Cell Dev Biol 16: 29-37, 2005.
    • (2005) Sem Cell Dev Biol , vol.16 , pp. 29-37
    • Tee, A.R.1    Blenis, J.2
  • 102
    • 0037108750 scopus 로고    scopus 로고
    • Tuberous sclerosis complex-1 and-2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling
    • Tee AR, Fingar DC, Manning BD, Kwiatkowski DJ, Cantley LC, Blenis J. Tuberous sclerosis complex-1 and-2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling. Proc Natl Acad Sci USA 99: 13571-13576, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.99 , pp. 13571-13576
    • Tee, A.R.1    Fingar, D.C.2    Manning, B.D.3    Kwiatkowski, D.J.4    Cantley, L.C.5    Blenis, J.6
  • 103
    • 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. Tuberous sclerosis complex gene products, tuberin and hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr Biol 13: 1259-1268, 2003.
    • (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
  • 107
    • 0035881470 scopus 로고    scopus 로고
    • Regulation of elongation factor 2 kinase by p90 RSK1 and p70 S6 kinase
    • Wang X, Li W, Williams M, Terada N, Alessi DR, Proud CG. Regulation of elongation factor 2 kinase by p90 RSK1 and p70 S6 kinase. EMBO J 20: 4370-4379, 2001.
    • (2001) EMBO J , vol.20 , pp. 4370-4379
    • Wang, X.1    Li, W.2    Williams, M.3    Terada, N.4    Alessi, D.R.5    Proud, C.G.6
  • 108
    • 33749431713 scopus 로고    scopus 로고
    • The mTOR pathway in the control of protein synthesis
    • Wang X, Proud CG. The mTOR pathway in the control of protein synthesis. Physiology (Bethesda, Md) 21: 362-369, 2006.
    • (2006) Physiology (Bethesda, Md) , vol.21 , pp. 362-369
    • Wang, X.1    Proud, C.G.2
  • 112
    • 0033968596 scopus 로고    scopus 로고
    • Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR
    • Yokogami K, Wakisaka S, Avruch J, Reeves SA. Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR. Curr Biol 10: 47-50, 2000.
    • (2000) Curr Biol , vol.10 , pp. 47-50
    • Yokogami, K.1    Wakisaka, S.2    Avruch, J.3    Reeves, S.A.4
  • 114
    • 34249680883 scopus 로고    scopus 로고
    • Increasing dietary leucine intake reduces diet-induced obesity and improves glucose and cholesterol metabolism in mice via multimechanisms
    • Zhang Y, Guo K, LeBlanc RE, Loh D, Schwartz GJ, Yu YH. Increasing dietary leucine intake reduces diet-induced obesity and improves glucose and cholesterol metabolism in mice via multimechanisms. Diabetes 56: 1647-1654, 2007.
    • (2007) Diabetes , vol.56 , pp. 1647-1654
    • Zhang, Y.1    Guo, K.2    le Blanc, R.E.3    Loh, D.4    Schwartz, G.J.5    Yu, Y.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.