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Volumn 5, Issue APRIL2016, 2016, Pages

Activation of GCN2 kinase by ribosome stalling links translation elongation with translation initiation

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ARGININE TRANSFER RNA; ATF4 PROTEIN, MOUSE; EIF2AK4 PROTEIN, MOUSE; GTPBP2 PROTEIN, MOUSE; GUANINE NUCLEOTIDE BINDING PROTEIN; INITIATION FACTOR 2; PROTEIN SERINE THREONINE KINASE;

EID: 84979583000     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.14295     Document Type: Article
Times cited : (134)

References (87)
  • 1
    • 84861843696 scopus 로고    scopus 로고
    • A mechanistic overview of translation initiation in eukaryotes
    • Aitken CE, Lorsch JR. 2012. A mechanistic overview of translation initiation in eukaryotes. Nature Structural & Molecular Biology 19: 568-576. doi: 10.1038/nsmb.2303.
    • (2012) Nature Structural & Molecular Biology , vol.19 , pp. 568-576
    • Aitken, C.E.1    Lorsch, J.R.2
  • 2
    • 84899656943 scopus 로고    scopus 로고
    • Diverse diseases from a ubiquitous process: The ribosomopathy paradox
    • Armistead J, Triggs-Raine B. 2014. Diverse diseases from a ubiquitous process: The ribosomopathy paradox. FEBS Letters 588: 1491-1500. doi: 10.1016/j.febslet.2014.03.024.
    • (2014) FEBS Letters , vol.588 , pp. 1491-1500
    • Armistead, J.1    Triggs-Raine, B.2
  • 3
    • 84866782195 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism
    • Baird TD, Wek RC. 2012. Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism. Advances in Nutrition 3: 307-321. doi: 10.3945/an.112.002113.
    • (2012) Advances in Nutrition , vol.3 , pp. 307-321
    • Baird, T.D.1    Wek, R.C.2
  • 4
    • 84907343347 scopus 로고    scopus 로고
    • Axonally synthesized ATF4 transmits a neurodegenerative signal across brain regions
    • Baleriola J, Walker CA, Jean YY, Crary JF, Troy CM, Nagy PL, Hengst U. 2014. Axonally synthesized ATF4 transmits a neurodegenerative signal across brain regions. Cell 158: 1159-1172. doi: 10.1016/j.cell.2014.07.001.
    • (2014) Cell , vol.158 , pp. 1159-1172
    • Baleriola, J.1    Walker, C.A.2    Jean, Y.Y.3    Crary, J.F.4    Troy, C.M.5    Nagy, P.L.6    Hengst, U.7
  • 5
    • 1542315525 scopus 로고    scopus 로고
    • Phosphorylation of translation initiation factor eif2α in the brain during pilocarpine-induced status epilepticus in mice
    • Carnevalli LS, Pereira CM, Longo BM, Jaqueta CB, Avedissian M, Mello LE, Castilho BA. 2004. Phosphorylation of translation initiation factor eif2α in the brain during pilocarpine-induced status epilepticus in mice. Neuroscience Letters 357: 191-194. doi: 10.1016/j.neulet.2003.12.093.
    • (2004) Neuroscience Letters , vol.357 , pp. 191-194
    • Carnevalli, L.S.1    Pereira, C.M.2    Longo, B.M.3    Jaqueta, C.B.4    Avedissian, M.5    Mello, L.E.6    Castilho, B.A.7
  • 8
    • 84899839442 scopus 로고    scopus 로고
    • Fragile X mental retardation protein regulates translation by binding directly to the ribosome
    • Chen E, Sharma MR, Shi X, Agrawal RK, Joseph S. 2014. Fragile X mental retardation protein regulates translation by binding directly to the ribosome. Molecular Cell 54: 407-417. doi: 10.1016/j.molcel.2014.03.023.
    • (2014) Molecular Cell , vol.54 , pp. 407-417
    • Chen, E.1    Sharma, M.R.2    Shi, X.3    Agrawal, R.K.4    Joseph, S.5
  • 9
    • 84899475428 scopus 로고    scopus 로고
    • Translational control by heme-regulated eif2α kinase during erythropoiesis
    • Chen JJ. 2014. Translational control by heme-regulated eif2α kinase during erythropoiesis. Current Opinion in Hematology 21: 172-178. doi: 10.1097/MOH.0000000000000030.
    • (2014) Current Opinion in Hematology , vol.21 , pp. 172-178
    • Chen, J.J.1
  • 11
    • 84894646451 scopus 로고    scopus 로고
    • Translation elongation can control translation initiation on eukaryotic mRNAs
    • Chu D, Kazana E, Bellanger N, Singh T, Tuite MF, von der Haar T. 2014. Translation elongation can control translation initiation on eukaryotic mRNAs. The EMBO Journal 33: 21-34. doi: 10.1002/embj.201385651.
    • (2014) The EMBO Journal , vol.33 , pp. 21-34
    • Chu, D.1    Kazana, E.2    Bellanger, N.3    Singh, T.4    Tuite, M.F.5    von der Haar, T.6
  • 12
    • 24144445705 scopus 로고    scopus 로고
    • Improved statistical tests for differential gene expression by shrinking variance components estimates
    • Cui X, Hwang JT, Qiu J, Blades NJ, Churchill GA. 2005. Improved statistical tests for differential gene expression by shrinking variance components estimates. Biostatistics 6: 59-75. doi: 10.1093/biostatistics/kxh018.
    • (2005) Biostatistics , vol.6 , pp. 59-75
    • Cui, X.1    Hwang, J.T.2    Qiu, J.3    Blades, N.J.4    Churchill, G.A.5
  • 14
    • 84941549664 scopus 로고    scopus 로고
    • Ribosomopathies: How a common root can cause a tree of pathologies
    • Danilova N, Gazda HT. 2015. Ribosomopathies: How a common root can cause a tree of pathologies. Disease Models & Mechanisms 8: 1013-1026. doi: 10.1242/dmm.020529.
    • (2015) Disease Models & Mechanisms , vol.8 , pp. 1013-1026
    • Danilova, N.1    Gazda, H.T.2
  • 17
    • 84885398154 scopus 로고    scopus 로고
    • Deletion of the eif2α kinase GCN2 fails to rescue the memory decline associated with alzheimer’s disease
    • Devi L, Ohno M. 2013. Deletion of the eif2α kinase GCN2 fails to rescue the memory decline associated with alzheimer’s disease. PloS One 8:e77335. doi: 10.1371/journal.pone.0077335.
    • (2013) PloS One , vol.8 , pp. e77335
    • Devi, L.1    Ohno, M.2
  • 18
    • 84903814520 scopus 로고    scopus 로고
    • Perk mediates eif2α phosphorylation responsible for BACE1 elevation, CREB dysfunction and neurodegeneration in a mouse model of alzheimer’s disease
    • Devi L, Ohno M. 2014. Perk mediates eif2α phosphorylation responsible for BACE1 elevation, CREB dysfunction and neurodegeneration in a mouse model of alzheimer’s disease. Neurobiology of Aging 35: 2272-2281. doi: 10.1016/j.neurobiolaging.2014.04.031.
    • (2014) Neurobiology of Aging , vol.35 , pp. 2272-2281
    • Devi, L.1    Ohno, M.2
  • 19
    • 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. Molecular Cell 6: 269-279. doi: 10.1016/s1097-2765(00)00028-9.
    • (2000) Molecular Cell , vol.6 , pp. 269-279
    • Dong, J.1    Qiu, H.2    Garcia-Barrio, M.3    Anderson, J.4    Hinnebusch, A.G.5
  • 22
    • 84945260547 scopus 로고    scopus 로고
    • Dynamics of co-translational protein targeting
    • Elvekrog MM, Walter P. 2015. Dynamics of co-translational protein targeting. Current Opinion in Chemical Biology 29: 79-86. doi: 10.1016/j.cbpa.2015.09.016.
    • (2015) Current Opinion in Chemical Biology , vol.29 , pp. 79-86
    • Elvekrog, M.M.1    Walter, P.2
  • 25
    • 84901393610 scopus 로고    scopus 로고
    • Crystal structures of GCN2 protein kinase c-terminal domains suggest regulatory differences in yeast and mammals
    • He H, Singh I, Wek SA, Dey S, Baird TD, Wek RC, Georgiadis MM. 2014. Crystal structures of GCN2 protein kinase c-terminal domains suggest regulatory differences in yeast and mammals. The Journal of Biological Chemistry 289: 15023-15034. doi: 10.1074/jbc.M114.560789.
    • (2014) The Journal of Biological Chemistry , vol.289 , pp. 15023-15034
    • He, H.1    Singh, I.2    Wek, S.A.3    Dey, S.4    Baird, T.D.5    Wek, R.C.6    Georgiadis, M.M.7
  • 26
    • 84902193122 scopus 로고    scopus 로고
    • The scanning mechanism of eukaryotic translation initiation
    • Hinnebusch AG. 2014. The scanning mechanism of eukaryotic translation initiation. Annual Review of Biochemistry 83: 779-812. doi: 10.1146/annurev-biochem-060713-035802.
    • (2014) Annual Review of Biochemistry , vol.83 , pp. 779-812
    • Hinnebusch, A.G.1
  • 28
    • 70450257666 scopus 로고    scopus 로고
    • A bifunctional intronic element regulates the expression of the arginine/lysine transporter cat-1 via mechanisms involving the purine-rich element binding protein A (pur alpha)
    • Huang CC, Chiribau CB, Majumder M, Chiang CM, Wek RC, Kelm RJ, Khalili K, Snider MD, Hatzoglou M. 2009. A bifunctional intronic element regulates the expression of the arginine/lysine transporter cat-1 via mechanisms involving the purine-rich element binding protein A (pur alpha). The Journal of Biological Chemistry 284: 32312-32320. doi: 10.1074/jbc.M109.024471.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 32312-32320
    • Huang, C.C.1    Chiribau, C.B.2    Majumder, M.3    Chiang, C.M.4    Wek, R.C.5    Kelm, R.J.6    Khalili, K.7    Snider, M.D.8    Hatzoglou, M.9
  • 29
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da W, Sherman BT, Lempicki RA. 2009. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nature Protocols 4: 44-57. doi: 10.1038/nprot.2008.211.
    • (2009) Nature Protocols , vol.4 , pp. 44-57
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 30
    • 84877801536 scopus 로고    scopus 로고
    • Quality control systems for aberrant mrnas induced by aberrant translation elongation and termination
    • Inada T. 2013. Quality control systems for aberrant mrnas induced by aberrant translation elongation and termination. Biochimica Et Biophysica Acta 1829: 634-642. doi: 10.1016/j.bbagrm.2013.02.004.
    • (2013) Biochimica Et Biophysica Acta , vol.1829 , pp. 634-642
    • Inada, T.1
  • 32
    • 84878912996 scopus 로고    scopus 로고
    • Arrest peptides: Cis-acting modulators of translation
    • Ito K, Chiba S. 2013. Arrest peptides: Cis-acting modulators of translation. Annual Review of Biochemistry 82: 171-202. doi: 10.1146/annurev-biochem-080211-105026.
    • (2013) Annual Review of Biochemistry , vol.82 , pp. 171-202
    • Ito, K.1    Chiba, S.2
  • 34
    • 17144389838 scopus 로고    scopus 로고
    • Phosphorylation of the alpha-subunit of the eukaryotic initiation factor-2 (eif2α) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition
    • Jiang HY, Wek RC. 2005. Phosphorylation of the alpha-subunit of the eukaryotic initiation factor-2 (eif2α) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition. The Journal of Biological Chemistry 280: 14189-14202. doi: 10.1074/jbc.M413660200.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 14189-14202
    • Jiang, H.Y.1    Wek, R.C.2
  • 35
    • 84866783355 scopus 로고    scopus 로고
    • The transcription factor network associated with the amino acid response in mammalian cells
    • Kilberg MS, Balasubramanian M, Fu L, Shan J. 2012. The transcription factor network associated with the amino acid response in mammalian cells. Advances in Nutrition 3: 295-306. doi: 10.3945/an.112.001891.
    • (2012) Advances in Nutrition , vol.3 , pp. 295-306
    • Kilberg, M.S.1    Balasubramanian, M.2    Fu, L.3    Shan, J.4
  • 39
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi Y, Segal M, Normington K, Gething MJ, Sambrook J. 1988. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332: 462-464. doi: 10.1038/332462a0.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 42
    • 84873467908 scopus 로고    scopus 로고
    • Cotranslational response to proteotoxic stress by elongation pausing of ribosomes
    • Liu B, Han Y, Qian SB. 2013. Cotranslational response to proteotoxic stress by elongation pausing of ribosomes. Molecular Cell 49: 453-463. doi: 10.1016/j.molcel.2012.12.001.
    • (2013) Molecular Cell , vol.49 , pp. 453-463
    • Liu, B.1    Han, Y.2    Qian, S.B.3
  • 43
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-delta delta C(T)) method
    • Livak KJ, Schmittgen TD. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-delta delta C(T)) method. Methods 25: 402-408. doi: 10.1006/meth.2001.1262.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 44
    • 84924629414 scopus 로고    scopus 로고
    • Moderated estimation of fold change and dispersion for rna-seq data with deseq2
    • Love MI, Huber W, Anders S. 2014. Moderated estimation of fold change and dispersion for rna-seq data with deseq2. Genome Biology 15. doi: 10.1186/s13059-014-0550-8.
    • (2014) Genome Biology , pp. 15
    • Love, M.I.1    Huber, W.2    Anders, S.3
  • 45
    • 5444264022 scopus 로고    scopus 로고
    • Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response
    • Lu PD, Harding HP, Ron D. 2004. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. The Journal of Cell Biology 167: 27-33. doi: 10.1083/jcb.200408003.
    • (2004) The Journal of Cell Biology , vol.167 , pp. 27-33
    • Lu, P.D.1    Harding, H.P.2    Ron, D.3
  • 46
    • 54249096045 scopus 로고    scopus 로고
    • Electrostatics in the ribosomal tunnel modulate chain elongation rates
    • Lu J, Deutsch C. 2008. Electrostatics in the ribosomal tunnel modulate chain elongation rates. Journal of Molecular Biology 384: 73-86. doi: 10.1016/j.jmb.2008.08.089.
    • (2008) Journal of Molecular Biology , vol.384 , pp. 73-86
    • Lu, J.1    Deutsch, C.2
  • 47
  • 49
    • 1842287951 scopus 로고    scopus 로고
    • Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eif2α kinase GCN2
    • Marton MJ, Vazquez de Aldana CR, Qiu H, Chakraburtty K, Hinnebusch AG. 1997. Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eif2α kinase GCN2. Molecular and Cellular Biology 17: 4474-4489. doi: 10.1128/MCB.17.8.4474.
    • (1997) Molecular and Cellular Biology , vol.17 , pp. 4474-4489
    • Marton, M.J.1    Vazquez de Aldana, C.R.2    Qiu, H.3    Chakraburtty, K.4    Hinnebusch, A.G.5
  • 51
    • 0017842405 scopus 로고
    • Codon-specific interaction of uncharged transfer-RNA with eukaryotic ribosomes
    • Murchie MJ, Leader DP. 1978. Codon-specific interaction of uncharged transfer-RNA with eukaryotic ribosomes. Biochimica Et Biophysica Acta 520: 233-236. doi: 10.1016/0005-2787(78)90024-2.
    • (1978) Biochimica Et Biophysica Acta , vol.520 , pp. 233-236
    • Murchie, M.J.1    Leader, D.P.2
  • 52
    • 2542489215 scopus 로고    scopus 로고
    • Dimerization is required for activation of eIF2 kinase Gcn2 in response to diverse environmental stress conditions
    • Narasimhan J, Staschke KA, Wek RC. 2004. Dimerization is required for activation of eIF2 kinase Gcn2 in response to diverse environmental stress conditions. The Journal of Biological Chemistry 279: 22820-22832. doi: 10.1074/jbc.M402228200.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 22820-22832
    • Narasimhan, J.1    Staschke, K.A.2    Wek, R.C.3
  • 53
    • 84931576485 scopus 로고    scopus 로고
    • Optimization of codon translation rates via trna modifications maintains proteome integrity
    • Nedialkova DD, Leidel SA. 2015. Optimization of codon translation rates via trna modifications maintains proteome integrity. Cell 161: 1606-1618. doi: 10.1016/j.cell.2015.05.022.
    • (2015) Cell , vol.161 , pp. 1606-1618
    • Nedialkova, D.D.1    Leidel, S.A.2
  • 56
    • 84930682682 scopus 로고    scopus 로고
    • Widespread co-translational RNA decay reveals ribosome dynamics
    • Pelechano V, Wei W, Steinmetz LM. 2015. Widespread co-translational RNA decay reveals ribosome dynamics. Cell 161: 1400-1412. doi: 10.1016/j.cell.2015.05.008.
    • (2015) Cell , vol.161 , pp. 1400-1412
    • Pelechano, V.1    Wei, W.2    Steinmetz, L.M.3
  • 58
    • 0034073380 scopus 로고    scopus 로고
    • Defects in tRNA processing and nuclear export induce GCN4 translation independently of phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2
    • Qiu H, Hu C, Anderson J, Björk GR, Sarkar S, Hopper AK, Hinnebusch AG. 2000. Defects in tRNA processing and nuclear export induce GCN4 translation independently of phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2. Molecular and Cellular Biology 20: 2505-2516. doi: 10.1128/MCB.20.7.2505-2516.2000.
    • (2000) Molecular and Cellular Biology , vol.20 , pp. 2505-2516
    • Qiu, H.1    Hu, C.2    Anderson, J.3    Björk, G.R.4    Sarkar, S.5    Hopper, A.K.6    Hinnebusch, A.G.7
  • 59
    • 84937436324 scopus 로고    scopus 로고
    • Codon bias as a means to fine-tune gene expression
    • Quax TE, Claassens NJ, Söll D, van der Oost J. 2015. Codon bias as a means to fine-tune gene expression. Molecular Cell 59: 149-161. doi: 10.1016/j.molcel.2015.05.035.
    • (2015) Molecular Cell , vol.59 , pp. 149-161
    • Quax, T.E.1    Claassens, N.J.2    Söll, D.3    van der Oost, J.4
  • 60
    • 84945181747 scopus 로고    scopus 로고
    • PERK inhibition prevents tau-mediated neurodegeneration in a mouse model of frontotemporal dementia
    • Radford H, Moreno JA, Verity N, Halliday M, Mallucci GR. 2015. PERK inhibition prevents tau-mediated neurodegeneration in a mouse model of frontotemporal dementia. Acta Neuropathologica 130: 633-642. doi: 10.1007/s00401-015-1487-z.
    • (2015) Acta Neuropathologica , vol.130 , pp. 633-642
    • Radford, H.1    Moreno, J.A.2    Verity, N.3    Halliday, M.4    Mallucci, G.R.5
  • 61
    • 0025801817 scopus 로고
    • Ribosome association of GCN2 protein kinase, a translational activator of the GCN4 gene of Saccharomyces cerevisiae
    • Ramirez M, Wek RC, Hinnebusch AG. 1991. Ribosome association of GCN2 protein kinase, a translational activator of the GCN4 gene of Saccharomyces cerevisiae. Molecular and Cellular Biology 11: 3027-3036. doi: 10.1128/MCB.11.6.3027.
    • (1991) Molecular and Cellular Biology , vol.11 , pp. 3027-3036
    • Ramirez, M.1    Wek, R.C.2    Hinnebusch, A.G.3
  • 62
    • 84943742690 scopus 로고    scopus 로고
    • Pausing on polyribosomes: Make way for elongation in translational control
    • Richter JD, Coller J. 2015. Pausing on polyribosomes: Make way for elongation in translational control. Cell 163: 292-300. doi: 10.1016/j.cell.2015.09.041.
    • (2015) Cell , vol.163 , pp. 292-300
    • Richter, J.D.1    Coller, J.2
  • 63
    • 84870732594 scopus 로고    scopus 로고
    • Protein-folding homeostasis in the endoplasmic reticulum and nutritional regulation
    • Ron D, Harding HP. 2012. Protein-folding homeostasis in the endoplasmic reticulum and nutritional regulation. Cold Spring Harbor Perspectives in Biology 4:a013177. doi: 10.1101/cshperspect.a013177.
    • (2012) Cold Spring Harbor Perspectives in Biology , vol.4 , pp. a013177
    • Ron, D.1    Harding, H.P.2
  • 64
    • 84903784093 scopus 로고    scopus 로고
    • Genetic inhibition of phosphorylation of the translation initiation factor eif2α does not block ab-dependent elevation of BACE1 and APP levels or reduce amyloid pathology in a mouse model of alzheimer’s disease
    • Sadleir KR, Eimer WA, Kaufman RJ, Osten P, Vassar R. 2014. Genetic inhibition of phosphorylation of the translation initiation factor eif2α does not block ab-dependent elevation of BACE1 and APP levels or reduce amyloid pathology in a mouse model of alzheimer’s disease. PloS One 9:e101643. doi: 10.1371/journal.pone.0101643.
    • (2014) PloS One , vol.9 , pp. e101643
    • Sadleir, K.R.1    Eimer, W.A.2    Kaufman, R.J.3    Osten, P.4    Vassar, R.5
  • 66
    • 84879345901 scopus 로고    scopus 로고
    • Rate-limiting steps in yeast protein translation
    • Shah P, Ding Y, Niemczyk M, Kudla G, Plotkin JB. 2013. Rate-limiting steps in yeast protein translation. Cell 153: 1589-1601. doi: 10.1016/j.cell.2013.05.049.
    • (2013) Cell , vol.153 , pp. 1589-1601
    • Shah, P.1    Ding, Y.2    Niemczyk, M.3    Kudla, G.4    Plotkin, J.B.5
  • 67
    • 84873442839 scopus 로고    scopus 로고
    • Widespread regulation of translation by elongation pausing in heat shock
    • Shalgi R, Hurt JA, Krykbaeva I, Taipale M, Lindquist S, Burge CB. 2013. Widespread regulation of translation by elongation pausing in heat shock. Molecular Cell 49: 439-452. doi: 10.1016/j.molcel.2012.11.028.
    • (2013) Molecular Cell , vol.49 , pp. 439-452
    • Shalgi, R.1    Hurt, J.A.2    Krykbaeva, I.3    Taipale, M.4    Lindquist, S.5    Burge, C.B.6
  • 68
    • 84888136766 scopus 로고    scopus 로고
    • Less is more: Improving proteostasis by translation slow down
    • Sherman MY, Qian SB. 2013. Less is more: Improving proteostasis by translation slow down. Trends in Biochemical Sciences 38: 585-591. doi: 10.1016/j.tibs.2013.09.003.
    • (2013) Trends in Biochemical Sciences , vol.38 , pp. 585-591
    • Sherman, M.Y.1    Qian, S.B.2
  • 69
    • 78651148617 scopus 로고
    • Loss of nucleotide and amino acid pool components from yeast cells following exposure to ultraviolet and photoreactivating radiations
    • Siegel SJ, Swenson PA. 1964. Loss of nucleotide and amino acid pool components from yeast cells following exposure to ultraviolet and photoreactivating radiations. Journal of Cellular Physiology 63: 253-260. doi: 10.1002/jcp.1030630216.
    • (1964) Journal of Cellular Physiology , vol.63 , pp. 253-260
    • Siegel, S.J.1    Swenson, P.A.2
  • 71
    • 84873287971 scopus 로고    scopus 로고
    • Atf4 protects against neuronal death in cellular parkinson’s disease models by maintaining levels of parkin
    • Sun X, Liu J, Crary JF, Malagelada C, Sulzer D, Greene LA, Levy OA. 2013. Atf4 protects against neuronal death in cellular parkinson’s disease models by maintaining levels of parkin. The Journal of Neuroscience 33: 2398-2407. doi: 10.1523/JNEUROSCI.2292-12.2013.
    • (2013) The Journal of Neuroscience , vol.33 , pp. 2398-2407
    • Sun, X.1    Liu, J.2    Crary, J.F.3    Malagelada, C.4    Sulzer, D.5    Greene, L.A.6    Levy, O.A.7
  • 72
    • 84868148725 scopus 로고    scopus 로고
    • Failure of amino acid homeostasis causes cell death following proteasome inhibition
    • Suraweera A, Münch C, Hanssum A, Bertolotti A. 2012. Failure of amino acid homeostasis causes cell death following proteasome inhibition. Molecular Cell 48: 242-253. doi: 10.1016/j.molcel.2012.08.003.
    • (2012) Molecular Cell , vol.48 , pp. 242-253
    • Suraweera, A.1    Münch, C.2    Hanssum, A.3    Bertolotti, A.4
  • 73
    • 84879757298 scopus 로고    scopus 로고
    • The perfect host: A mouse host embryo facilitating more efficient germ line transmission of genetically modified embryonic stem cells
    • Taft RA, Low BE, Byers SL, Murray SA, Kutny P, Wiles MV. 2013. The perfect host: A mouse host embryo facilitating more efficient germ line transmission of genetically modified embryonic stem cells. PloS One 8: e67826. doi: 10.1371/journal.pone.0067826.
    • (2013) PloS One , vol.8 , pp. e67826
    • Taft, R.A.1    Low, B.E.2    Byers, S.L.3    Murray, S.A.4    Kutny, P.5    Wiles, M.V.6
  • 76
    • 0024381444 scopus 로고
    • Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availability
    • Wek RC, Jackson BM, Hinnebusch AG. 1989. Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availability. Proceedings of the National Academy of Sciences of the United States of America 86: 4579-4583. doi: 10.1073/pnas.86.12.4579.
    • (1989) Proceedings of the National Academy of Sciences of the United States of America , vol.86 , pp. 4579-4583
    • Wek, R.C.1    Jackson, B.M.2    Hinnebusch, A.G.3
  • 77
    • 0029006391 scopus 로고
    • The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids
    • Wek SA, Zhu S, Wek RC. 1995. The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids. Molecular and Cellular Biology 15: 4497-4506. doi: 10.1128/MCB.15.8.4497.
    • (1995) Molecular and Cellular Biology , vol.15 , pp. 4497-4506
    • Wek, S.A.1    Zhu, S.2    Wek, R.C.3
  • 79
    • 0242291496 scopus 로고    scopus 로고
    • MAANOVA: A Software Package for the Analysis of Spotted cDNA. Microarray Experiments. In: Parmigiani G, Garett ES, Irizarry RA, Zeger SL (Eds)
    • New York, NY: Springer New York
    • Wu H, Kerr MK, Cui X, Churchill GA. 2003. MAANOVA: A Software Package for the Analysis of Spotted cDNA. Microarray Experiments. In: Parmigiani G, Garett ES, Irizarry RA, Zeger SL (Eds). The Analysis of Gene Expression Data. New York, NY: Springer New York. p313-341. doi: 10.1007/0-387-21679-0_14.
    • (2003) The Analysis of Gene Expression Data , pp. 313-341
    • Wu, H.1    Kerr, M.K.2    Cui, X.3    Churchill, G.A.4
  • 80
    • 0034028905 scopus 로고    scopus 로고
    • Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase
    • Yang R, Wek SA, Wek RC. 2000. Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase. Molecular and Cellular Biology 20: 2706-2717. doi: 10.1128/MCB.20.8.2706-2717.2000.
    • (2000) Molecular and Cellular Biology , vol.20 , pp. 2706-2717
    • Yang, R.1    Wek, S.A.2    Wek, R.C.3
  • 82
    • 85050579899 scopus 로고    scopus 로고
    • Ribosomopathies: Global process, tissue specific defects
    • Yelick PC, Trainor PA. 2015. Ribosomopathies: Global process, tissue specific defects. Rare Diseases 3: e1025185. doi: 10.1080/21675511.2015.1025185.
    • (2015) Rare Diseases , vol.3 , pp. e1025185
    • Yelick, P.C.1    Trainor, P.A.2
  • 83
    • 0035966269 scopus 로고    scopus 로고
    • Xbp1 mRNA is induced by ATF6 and spliced by IRE1. in response to ER stress to produce a highly active transcription factor
    • Yoshida H, Matsui T, Yamamoto A, Okada T, Mori K. 2001. Xbp1 mRNA is induced by ATF6 and spliced by IRE1. in response to ER stress to produce a highly active transcription factor. Cell 107: 881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 84
    • 33745844503 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in health and disease
    • Zhao L, Ackerman SL. 2006. Endoplasmic reticulum stress in health and disease.. Current Opinion in Cell Biology 18: 444-452. doi: 10.1016/j.ceb.2006.06.005.
    • (2006) Current Opinion in Cell Biology , vol.18 , pp. 444-452
    • Zhao, L.1    Ackerman, S.L.2
  • 85
    • 84937795234 scopus 로고    scopus 로고
    • Transfer RNAs mediate the rapid adaptation of escherichia coli to oxidative stress
    • Zhong J, Xiao C, Gu W, Du G, Sun X, He QY, Zhang G. 2015. Transfer RNAs mediate the rapid adaptation of escherichia coli to oxidative stress. PLoS Genetics 11:e1005302. doi: 10.1371/journal.pgen.1005302.
    • (2015) PLoS Genetics , vol.11 , pp. e1005302
    • Zhong, J.1    Xiao, C.2    Gu, W.3    Du, G.4    Sun, X.5    He, Q.Y.6    Zhang, G.7
  • 86
    • 0029785485 scopus 로고    scopus 로고
    • Histidyl-trna synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eif-2
    • Zhu S, Sobolev AY, Wek RC. 1996. Histidyl-trna synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eif-2. The Journal of Biological Chemistry 271: 24989-24994.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 24989-24994
    • Zhu, S.1    Sobolev, A.Y.2    Wek, R.C.3
  • 87
    • 0031916835 scopus 로고    scopus 로고
    • Ribosome-binding domain of eukaryotic initiation factor-2 kinase GCN2 facilitates translation control
    • Zhu S, Wek RC. 1998. Ribosome-binding domain of eukaryotic initiation factor-2 kinase GCN2 facilitates translation control. The Journal of Biological Chemistry 273: 1808-1814.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 1808-1814
    • Zhu, S.1    Wek, R.C.2


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