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Volumn 86, Issue 6, 2010, Pages 1887-1894

Methylglyoxal activates Gcn2 to phosphorylate eIF2α independently of the TOR pathway in Saccharomyces cerevisiae

Author keywords

EIF2 ; Gcn2; Methylglyoxal; Rapamycin; S. cerevisiae; TORC1

Indexed keywords

INITIATION FACTORS; KINASE ACTIVITY; METHYLGLYOXAL; POTENT INHIBITOR; PROTEIN SYNTHESIS; RAPAMYCIN; S.CEREVISIAE; SACCHAROMYCES CEREVISIAE; TARGET OF RAPAMYCIN;

EID: 77952876250     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-009-2411-z     Document Type: Article
Times cited : (12)

References (35)
  • 1
    • 0033540030 scopus 로고    scopus 로고
    • The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors
    • 10.1038/45287 1:CAS:528:DC%2BD3cXjvVSh
    • T Beck MN Hall 1999 The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors Nature 402 689 692 10.1038/45287 1:CAS:528:DC%2BD3cXjvVSh
    • (1999) Nature , vol.402 , pp. 689-692
    • Beck, T.1    Hall, M.N.2
  • 2
    • 0034680772 scopus 로고    scopus 로고
    • Tripartite regulation of Gln3p by TOR, Ure2p, and phosphatases
    • 10.1074/jbc.M004235200 1:CAS:528:DC%2BD3cXosVSksbg%3D
    • PG Bertram JH Choi J Carvalho W Ai C Zeng TF Chan XF Zheng 2000 Tripartite regulation of Gln3p by TOR, Ure2p, and phosphatases J Biol Chem 275 35727 35733 10.1074/jbc.M004235200 1:CAS:528:DC%2BD3cXosVSksbg%3D
    • (2000) J Biol Chem , vol.275 , pp. 35727-35733
    • Bertram, P.G.1    Choi, J.H.2    Carvalho, J.3    Ai, W.4    Zeng, C.5    Chan, T.F.6    Zheng, X.F.7
  • 3
    • 0036148362 scopus 로고    scopus 로고
    • Convergence of TOR-nitrogen and Snf1-glucose signaling pathways onto Gln3
    • DOI 10.1128/MCB.22.4.1246-1252.2002
    • PG Bertram JH Choi J Carvalho TF Chan W Ai XF Zheng 2002 Convergence of TOR-nitrogen and Snf1-glucose signaling pathways onto Gln3 Mol Cell Biol 22 1246 1256 10.1128/MCB.22.4.1246-1252.2002 1:CAS:528:DC%2BD38XovVajsg%3D%3D (Pubitemid 34094859)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.4 , pp. 1246-1252
    • Bertram, P.G.1    Choi, J.H.2    Carvalho, J.3    Chan, T.-F.4    Ai, W.5    Zheng, X.F.S.6
  • 4
    • 33846012886 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-phosphate is required for translation initiation in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M601060200
    • E Cameroni C De Virgilio O Deloche 2006 Phosphatidylinositol 4-phosphate is required for translation initiation in Saccharomyces cerevisiae J Biol Chem 281 38139 38149 10.1074/jbc.M601060200 1:CAS:528:DC%2BD28Xht12nu7nL (Pubitemid 46043305)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.50 , pp. 38139-38149
    • Cameroni, E.1    De Virgilio, C.2    Deloche, O.3
  • 5
    • 0037382865 scopus 로고    scopus 로고
    • Translational control by TOR and TAP42 through dephosphorylation of eIF2α kinase GCN2
    • DOI 10.1101/gad.1069003
    • VA Cherkasova AG Hinnebusch 2003 Translational control by TOR and TAP42 through dephosphorylation of eIF2α kinase GCN2 Genes Dev 17 859 872 10.1101/gad.1069003 1:CAS:528:DC%2BD3sXislOltrw%3D (Pubitemid 36397374)
    • (2003) Genes and Development , vol.17 , Issue.7 , pp. 859-872
    • Cherkasova, V.A.1    Hinnebusch, A.G.2
  • 6
    • 0037020146 scopus 로고    scopus 로고
    • Cytoplasmic compartmentation of Gln3 during nitrogen catabolite repression and the mechanism of its nuclear localization during carbon starvation in Saccharomyces cerevisiae
    • 10.1074/jbc.M204879200 1:CAS:528:DC%2BD38XnsVejsL0%3D
    • KH Cox JJ Tate TG Cooper 2002 Cytoplasmic compartmentation of Gln3 during nitrogen catabolite repression and the mechanism of its nuclear localization during carbon starvation in Saccharomyces cerevisiae J Biol Chem 277 37559 37566 10.1074/jbc.M204879200 1:CAS:528:DC%2BD38XnsVejsL0%3D
    • (2002) J Biol Chem , vol.277 , pp. 37559-37566
    • Cox, K.H.1    Tate, J.J.2    Cooper, T.G.3
  • 7
    • 4444249882 scopus 로고    scopus 로고
    • NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent transcription in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M407372200
    • JL Crespo SB Helliwell C Wiederkehr P Demougin B Fowler M Primig MN Hall 2004 NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent transcription in Saccharomyces cerevisiae J Biol Chem 279 37512 37517 10.1074/jbc.M407372200 1:CAS:528:DC%2BD2cXntFSnsr4%3D (Pubitemid 39195463)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.36 , pp. 37512-37517
    • Crespo, J.L.1    Helliwell, S.B.2    Wiederkehr, C.3    Demougin, P.4    Fowler, B.5    Primig, M.6    Hall, M.N.7
  • 8
    • 0033635215 scopus 로고    scopus 로고
    • Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain
    • Dong J, Qiu H, Garcia-Barrio M, Anderson J, Hinnebusch AG (2000) Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain. Mol Cell 6:269-279
    • (2000) Mol Cell , vol.6 , pp. 269-279
    • Dong, J.1    Qiu, H.2    Garcia-Barrio, M.3    Anderson, J.4    Hinnebusch, A.G.5
  • 9
    • 0034678890 scopus 로고    scopus 로고
    • Association of GCN1-GCN20 regulatory complex with the N-terminus of eIF2α kinase GCN2 is required for GCN2 activation
    • 10.1093/emboj/19.8.1887 1:CAS:528:DC%2BD3cXivVKltrk%3D
    • M Garcia-Barrio J Dong S Ufano AG Hinnebusch 2000 Association of GCN1-GCN20 regulatory complex with the N-terminus of eIF2α kinase GCN2 is required for GCN2 activation EMBO J 19 1887 1899 10.1093/emboj/19.8.1887 1:CAS:528:DC%2BD3cXivVKltrk%3D
    • (2000) EMBO J , vol.19 , pp. 1887-1899
    • Garcia-Barrio, M.1    Dong, J.2    Ufano, S.3    Hinnebusch, A.G.4
  • 10
    • 27144510561 scopus 로고    scopus 로고
    • Translational regulation of GCN4 and the general amino acid control of yeast
    • DOI 10.1146/annurev.micro.59.031805.133833
    • AG Hinnebusch 2005 Translational regulation of GCN4 and the general amino acid control of yeast Annu Rev Microbiol 59 407 450 10.1146/annurev.micro.59. 031805.133833 1:CAS:528:DC%2BD2MXht1ShsL7N (Pubitemid 41507438)
    • (2005) Annual Review of Microbiology , vol.59 , pp. 407-450
    • Hinnebusch, A.G.1
  • 11
    • 0028853680 scopus 로고
    • Methylglyoxal and regulation of its metabolism in microorganisms
    • 10.1016/S0065-2911(08)60146-0 1:CAS:528:DyaK28Xht1Cmu78%3D
    • Y Inoue A Kimura 1995 Methylglyoxal and regulation of its metabolism in microorganisms Adv Microbiol Physiol 37 177 227 10.1016/S0065-2911(08)60146-0 1:CAS:528:DyaK28Xht1Cmu78%3D
    • (1995) Adv Microbiol Physiol , vol.37 , pp. 177-227
    • Inoue, Y.1    Kimura, A.2
  • 12
    • 0034683568 scopus 로고    scopus 로고
    • Tor-mediated induction of autophagy via an Apg1 protein kinase complex
    • 10.1083/jcb.150.6.1507 1:CAS:528:DC%2BD3cXmslGlsr4%3D
    • Y Kamada T Funakoshi T Shintani K Nagano M Ohsumi Y Ohsumi 2000 Tor-mediated induction of autophagy via an Apg1 protein kinase complex J Cell Biol 150 1507 1513 10.1083/jcb.150.6.1507 1:CAS:528:DC%2BD3cXmslGlsr4%3D
    • (2000) J Cell Biol , vol.150 , pp. 1507-1513
    • Kamada, Y.1    Funakoshi, T.2    Shintani, T.3    Nagano, K.4    Ohsumi, M.5    Ohsumi, Y.6
  • 13
    • 0034625341 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae GATA sequences function as TATA elements during nitrogen catabolite repression and when Gln3p is excluded from the nucleus by overproduction of Ure2p
    • DOI 10.1074/jbc.M001648200
    • H Kathleen KH Cox R Rai M Distler JR Daugherty JA Coffman TG Cooper 2000 Saccharomyces cerevisiae GATA sequences function as TATA elements during nitrogen catabolite repression and when Gln3p is excluded from the nucleus by overproduction of Ure2p J Biol Chem 275 17611 17618 10.1074/jbc.M001648200 (Pubitemid 30430807)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.23 , pp. 17611-17618
    • Cox, K.1    Rai, R.2    Distler, M.3    Daugherty, J.R.4    Coffman, J.A.5    Cooper, T.G.6
  • 14
    • 0035907288 scopus 로고    scopus 로고
    • Budding yeast GCN1 binds the GI domain to activate the eIF2α kinase GCN2
    • 10.1074/jbc.M011793200 1:CAS:528:DC%2BD3MXjvFGhsrc%3D
    • H Kubota K Ota Y Sakaki T Ito 2001 Budding yeast GCN1 binds the GI domain to activate the eIF2α kinase GCN2 J Biol Chem 276 17591 17596 10.1074/jbc.M011793200 1:CAS:528:DC%2BD3MXjvFGhsrc%3D
    • (2001) J Biol Chem , vol.276 , pp. 17591-17596
    • Kubota, H.1    Ota, K.2    Sakaki, Y.3    Ito, T.4
  • 15
    • 0037743691 scopus 로고    scopus 로고
    • Rapamycin-induced translational derepression of GCN4 mRNA involves a novel mechanism for activation of the eIF2α kinase GCN2
    • DOI 10.1074/jbc.C300133200
    • H Kubota T Obata K Ota T Sasaki T Ito 2003 Rapamycin-induced translational derepression of GCN4 mRNA involves a novel mechanism for activation of the eIF2α kinase GCN2 J Biol Chem 278 20457 20460 10.1074/jbc.C300133200 1:CAS:528:DC%2BD3sXkt1Wjtb0%3D (Pubitemid 36806341)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.23 , pp. 20457-20460
    • Kubota, H.1    Obata, T.2    Ota, K.3    Sasaki, T.4    Ito, T.5
  • 16
    • 0036753494 scopus 로고    scopus 로고
    • Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control
    • DOI 10.1016/S1097-2765(02)00636-6
    • R Loewith E Jacinto S Wullschleger A Lorberg JL Crespo D Bonenfant W Oppliger P Jenoe MN Hall 2002 Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control Mol Cell 10 457 468 10.1016/S1097-2765(02)00636-6 1:CAS:528:DC%2BD38XnvFSlt74%3D (Pubitemid 35284167)
    • (2002) Molecular Cell , vol.10 , Issue.3 , pp. 457-468
    • Loewith, R.1    Jacinto, E.2    Wullschleger, S.3    Lorberg, A.4    Crespo, J.L.5    Bonenfant, D.6    Oppliger, W.7    Jenoe, P.8    Hall, M.N.9
  • 17
    • 4544374631 scopus 로고    scopus 로고
    • Activity of the Yap1 transcription factor in Saccharomyces cerevisiae is modulated by methylglyoxal, a metabolite derived from glycolysis
    • DOI 10.1128/MCB.24.19.8753-8764.2004
    • K Maeta S Izawa S Okazaki S Kuge Y Inoue 2004 Activity of the Yap1 transcription factor in Saccharomyces cerevisiae is modulated by methylglyoxal, a metabolite derived from glycolysis Mol Cell Biol 24 8753 8764 10.1128/MCB.24.19.8753-8764.2004 1:CAS:528:DC%2BD2cXnvVakur4%3D (Pubitemid 39245093)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.19 , pp. 8753-8764
    • Maeta, K.1    Izawa, S.2    Okazaki, S.3    Kuge, S.4    Inoue, Y.5
  • 18
    • 12844281130 scopus 로고    scopus 로고
    • Methylglyoxal, a metabolite derived from glycolysis, functions as a signal initiator of the high osmolarity glycerol-mitogen-activated protein kinase cascade and calcineurin/Crz1-mediated pathway in Saccharomyces cerevisiae
    • 1:CAS:528:DC%2BD2cXhtFGgu7rK
    • K Maeta S Izawa Y Inoue 2005 Methylglyoxal, a metabolite derived from glycolysis, functions as a signal initiator of the high osmolarity glycerol-mitogen-activated protein kinase cascade and calcineurin/Crz1-mediated pathway in Saccharomyces cerevisiae J Biol Chem 280 253 280 1:CAS:528: DC%2BD2cXhtFGgu7rK
    • (2005) J Biol Chem , vol.280 , pp. 253-280
    • Maeta, K.1    Izawa, S.2    Inoue, Y.3
  • 19
    • 0027175499 scopus 로고
    • GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, is required for phosphorylation of eukaryotic translation initiation factor 2 by protein kinase GCN2
    • 1:CAS:528:DyaK3sXlslOhtrY%3D
    • MJ Marton D Crouch AG Hinnebusch 1993 GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, is required for phosphorylation of eukaryotic translation initiation factor 2 by protein kinase GCN2 Mol Cell Biol 13 3541 3556 1:CAS:528:DyaK3sXlslOhtrY%3D
    • (1993) Mol Cell Biol , vol.13 , pp. 3541-3556
    • Marton, M.J.1    Crouch, D.2    Hinnebusch, A.G.3
  • 20
    • 0035965277 scopus 로고    scopus 로고
    • Regulation of Snf1 Kinase. Activation requires phosphorylation of threonine 210 by an upstream kinase as well as a distinct step mediated by the Snf4 subunit
    • DOI 10.1074/jbc.M104418200
    • RR McCartney MC Schmidt 2001 Regulation of Snf1 kinase. Activation requires phosphorylation of threonine 210 by an upstream kinase as well as a distinct step mediated by the Snf4 subunit J Biol Chem 276 36460 36466 10.1074/jbc.M104418200 1:CAS:528:DC%2BD3MXnt1yrtrY%3D (Pubitemid 37384256)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.39 , pp. 36460-36466
    • McCartney, R.R.1    Schmidt, M.C.2
  • 21
    • 0032512636 scopus 로고    scopus 로고
    • Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast
    • DOI 10.1074/jbc.273.7.3963
    • T Noda Y Ohsumi 1998 Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast J Biol Chem 273 3963 3966 10.1074/jbc.273.7.3963 1:CAS:528:DyaK1cXht1ahsr8%3D (Pubitemid 28103257)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.7 , pp. 3963-3966
    • Noda, T.1    Ohsumi, Y.2
  • 22
    • 0029036915 scopus 로고
    • Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae
    • 10.1006/bbrc.1995.1636 1:CAS:528:DyaK2MXlsF2mtr4%3D
    • T Noda A Matsuura Y Wada Y Ohsumi 1995 Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae Biochem Biophys Res Commun 210 126 132 10.1006/bbrc.1995.1636 1:CAS:528:DyaK2MXlsF2mtr4%3D
    • (1995) Biochem Biophys Res Commun , vol.210 , pp. 126-132
    • Noda, T.1    Matsuura, A.2    Wada, Y.3    Ohsumi, Y.4
  • 23
    • 53449084103 scopus 로고    scopus 로고
    • Role of Gcn4 for adaptation to methylglyoxal in Saccharomyces cerevisiae: Methylglyoxal attenuates protein synthesis through phosphorylation of eIF2α
    • 10.1016/j.bbrc.2008.09.063 1:CAS:528:DC%2BD1cXht1KlsrfN
    • W Nomura K Maeta K Kita S Izawa Y Inoue 2008 Role of Gcn4 for adaptation to methylglyoxal in Saccharomyces cerevisiae: Methylglyoxal attenuates protein synthesis through phosphorylation of eIF2α Biochem Biophys Res Commun 376 738 742 10.1016/j.bbrc.2008.09.063 1:CAS:528:DC%2BD1cXht1KlsrfN
    • (2008) Biochem Biophys Res Commun , vol.376 , pp. 738-742
    • Nomura, W.1    Maeta, K.2    Kita, K.3    Izawa, S.4    Inoue, Y.5
  • 24
    • 0037093333 scopus 로고    scopus 로고
    • Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2
    • DOI 10.1101/gad.979402
    • H Qiu C Hu J Dong AG Hinnebusch 2002 Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2 Genes Dev 16 1271 1280 10.1101/gad.979402 1:CAS:528:DC%2BD38XktFSmsb4%3D (Pubitemid 34553107)
    • (2002) Genes and Development , vol.16 , Issue.10 , pp. 1271-1280
    • Qiu, H.1    Hu, C.2    Dong, J.3    Hinnebusch, A.G.4
  • 26
  • 27
    • 0032403058 scopus 로고    scopus 로고
    • The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease
    • 10.1093/emboj/17.23.6924 1:CAS:528:DyaK1MXivFalsQ%3D%3D
    • A Schmidt T Beck A Koller J Kunz MN Hall 1998 The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease EMBO J 17 6924 6931 10.1093/emboj/17.23.6924 1:CAS:528:DyaK1MXivFalsQ%3D%3D
    • (1998) EMBO J , vol.17 , pp. 6924-6931
    • Schmidt, A.1    Beck, T.2    Koller, A.3    Kunz, J.4    Hall, M.N.5
  • 28
    • 0028561918 scopus 로고
    • Interaction between FKBP12-rapamycin and TOR involves a conserved serine residue
    • 1:CAS:528:DyaK2cXmvFahtb0%3D
    • R Stan MM McLaughlin R Cafferkey RK Johnson M Rosenberg GP Livi 1994 Interaction between FKBP12-rapamycin and TOR involves a conserved serine residue J Biol Chem 269 32027 32030 1:CAS:528:DyaK2cXmvFahtb0%3D
    • (1994) J Biol Chem , vol.269 , pp. 32027-32030
    • Stan, R.1    McLaughlin, M.M.2    Cafferkey, R.3    Johnson, R.K.4    Rosenberg, M.5    Livi, G.P.6
  • 29
    • 33646918686 scopus 로고    scopus 로고
    • Methylglyoxal as a signal initiator for activation of the stress-activated protein kinase cascade in the fission yeast Schizosaccharomyces pombe
    • DOI 10.1074/jbc.M511037200
    • Y Takatsume S Izawa Y Inoue 2006 Methylglyoxal as a signal initiator for activation of the stress-activated protein kinase cascade in the fission yeast Schizosaccharomyces pombe J Biol Chem 281 9086 9092 10.1074/jbc.M511037200 1:CAS:528:DC%2BD28XjtVSktb0%3D (Pubitemid 43864621)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9086-9092
    • Takatsume, Y.1    Izawa, S.2    Inoue, Y.3
  • 30
    • 34547121478 scopus 로고    scopus 로고
    • Stress-responsive Gln3 localization in Saccharomyces cerevisiae is separable from and can overwhelm nitrogen source regulation
    • DOI 10.1074/jbc.M609550200
    • JJ Tate TG Cooper 2007 Stress-responsive Gln3 localization in Saccharomyces cerevisiae is separable from and can overwhelm nitrogen source regulation J Biol Chem 282 18467 18480 10.1074/jbc.M609550200 1:CAS:528:DC%2BD2sXmsVOks7k%3D (Pubitemid 47100261)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.25 , pp. 18467-18480
    • Tate, J.J.1    Cooper, T.G.2
  • 31
    • 33846007281 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Sit4 phosphatase is active irrespective of the nitrogen source provided, and Gln3 phosphorylation levels become nitrogen source-responsive in a sit4-deleted strain
    • DOI 10.1074/jbc.M606973200
    • JJ Tate A Feller E Dubois TG Cooper 2006 Saccharomyces cerevisiae Sit4 phosphatase is active irrespective of the nitrogen source provided, and Gln3 phosphorylation levels become nitrogen source-responsive in a sit4-deleted strain J Biol Chem 281 37980 37992 10.1074/jbc.M606973200 1:CAS:528: DC%2BD28Xht1Kit7zP (Pubitemid 46042102)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.49 , pp. 37980-37992
    • Tate, J.J.1    Feller, A.2    Dubois, E.3    Cooper, T.G.4
  • 32
    • 0029001571 scopus 로고
    • GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex that mediates activation of the eIF-2α kinase GCN2 in amino acid-starved cells
    • 1:CAS:528:DyaK2MXntVekurg%3D
    • CR Vazquez de Aldana MJ Marton AG Hinnebusch 1995 GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex that mediates activation of the eIF-2α kinase GCN2 in amino acid-starved cells EMBO J 14 3184 3199 1:CAS:528:DyaK2MXntVekurg%3D
    • (1995) EMBO J , vol.14 , pp. 3184-3199
    • Vazquez De Aldana, C.R.1    Marton, M.J.2    Hinnebusch, A.G.3
  • 33
    • 0029006391 scopus 로고
    • The histidyl-tRNA synthetase-related sequence in the eIF-2α protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids
    • 1:CAS:528:DyaK2MXntVGiur0%3D
    • SA Wek S Zhu RC Wek 1995 The histidyl-tRNA synthetase-related sequence in the eIF-2α protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids Mol Cell Biol 15 4497 4506 1:CAS:528:DyaK2MXntVGiur0%3D
    • (1995) Mol Cell Biol , vol.15 , pp. 4497-4506
    • Wek, S.A.1    Zhu, S.2    Wek, R.C.3
  • 34
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • DOI 10.1016/j.cell.2006.01.016, PII S0092867406001085
    • S Wullschleger R Loewith MN Hall 2006 TOR signaling in growth and metabolism Cell 124 471 484 10.1016/j.cell.2006.01.016 1:CAS:528: DC%2BD28Xhslaqs74%3D (Pubitemid 43199434)
    • (2006) Cell , vol.124 , Issue.3 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 35
    • 0034028905 scopus 로고    scopus 로고
    • Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase
    • DOI 10.1128/MCB.20.8.2706-2717.2000
    • R Yang SA Wek RC Wek 2000 Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase Mol Cell Biol 20 2706 2717 10.1128/MCB.20.8.2706-2717.2000 1:CAS:528:DC%2BD3cXit1ymu78%3D (Pubitemid 30183489)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.8 , pp. 2706-2717
    • Yang, R.1    Wek, S.A.2    Wek, R.C.3


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