메뉴 건너뛰기




Volumn 265, Issue 2, 1999, Pages 754-762

Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2α kinase

Author keywords

cDNA cloning; Mouse liver; Protein kinase; Serum starvation; Translation initiation

Indexed keywords

AMINO ACID; AMINO ACID TRANSFER RNA LIGASE; COMPLEMENTARY DNA; INITIATION FACTOR 2; PROTEIN KINASE;

EID: 0001598487     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00780.x     Document Type: Article
Times cited : (226)

References (36)
  • 1
    • 0000002161 scopus 로고
    • Binding of Met-tRNA
    • (Trachsel, H., ed.), CRC Press Inc, Boca Raton, FL
    • 1. Jackson, R.J. (1991) Binding of Met-tRNA. In Translation in Eukaryotes (Trachsel, H., ed.), pp. 193-229. CRC Press Inc, Boca Raton, FL.
    • (1991) Translation in Eukaryotes , pp. 193-229
    • Jackson, R.J.1
  • 2
    • 0030267336 scopus 로고    scopus 로고
    • The eIF-2α kinases and the control of protein synthesis
    • 2. de Haro, C., Méndez, R. & Santoyo, J. (1996) The eIF-2α kinases and the control of protein synthesis. FASEB J. 10, 1378-1387.
    • (1996) FASEB J. , vol.10 , pp. 1378-1387
    • De Haro, C.1    Méndez, R.2    Santoyo, J.3
  • 3
    • 0001342909 scopus 로고    scopus 로고
    • Origins and targets of translational control
    • (Hershey, J.W.B., Mathews, M.B. & Sonenberg, N., eds), Cold Spring Harbor Laboratory Press, Plainview, NY
    • 3. Mathews, M.B., Sonenberg, N. & Hershey, J.W.B. (1996) Origins and targets of translational control. In Translational Control (Hershey, J.W.B., Mathews, M.B. & Sonenberg, N., eds), pp. 1-30. Cold Spring Harbor Laboratory Press, Plainview, NY.
    • (1996) Translational Control , pp. 1-30
    • Mathews, M.B.1    Sonenberg, N.2    Hershey, J.W.B.3
  • 4
    • 0030803256 scopus 로고    scopus 로고
    • Translational regulation of yeast GCN4: A window on factors that control initiator-tRNA binding to the ribosome
    • 4. Hinnebusch, A.G. (1997) Translational regulation of yeast GCN4: a window on factors that control initiator-tRNA binding to the ribosome. J. Biol. Chem. 272, 21661-21664.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21661-21664
    • Hinnebusch, A.G.1
  • 5
    • 0032519585 scopus 로고    scopus 로고
    • eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange
    • 5. Pavitt, G.D., Ramaiah, K.V.A., Kimball, S.R. & Hinnebusch, A.G. (1998) eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange. Genes Dev. 12, 514-526.
    • (1998) Genes Dev. , vol.12 , pp. 514-526
    • Pavitt, G.D.1    Ramaiah, K.V.A.2    Kimball, S.R.3    Hinnebusch, A.G.4
  • 6
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • 6. Hanks, S.K. & Hunter, T. (1995) The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 7
    • 0028935374 scopus 로고
    • Regulation of protein synthesis by heme-regulated eIF-2α kinase
    • 7. Chen, J.J. & London, I.M. (1995) Regulation of protein synthesis by heme-regulated eIF-2α kinase. Trends Biochem. Sci. 20, 105-108.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 105-108
    • Chen, J.J.1    London, I.M.2
  • 8
    • 0029007407 scopus 로고
    • PKR: A new name and new roles
    • 8. Proud, C.G. (1995) PKR: a new name and new roles. Trends Biochem. Sci. 20, 241-246.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 241-246
    • Proud, C.G.1
  • 9
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • 9. Harging, H.P., Zhang, Y. & Ron, D. (1999) Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397, 271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harging, H.P.1    Zhang, Y.2    Ron, D.3
  • 10
    • 0031755020 scopus 로고    scopus 로고
    • Identification and characterization of pancreatic eukaryotic initiation factor 2α-subunit kinase, PEK, involved in translational control
    • 10. Shi, Y., Vattem, K.M., Sood, R., An, J., Liang, J., Stramm, L. & Wek, R.C. (1998) Identification and characterization of pancreatic eukaryotic initiation factor 2α-subunit kinase, PEK, involved in translational control. Mol. Cell. Biol. 18, 7499-7509.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7499-7509
    • Shi, Y.1    Vattem, K.M.2    Sood, R.3    An, J.4    Liang, J.5    Stramm, L.6    Wek, R.C.7
  • 11
    • 0345313653 scopus 로고    scopus 로고
    • Characterization of a mutant pancreatic eIF-2α kinase, PEK, and co-localization with somatostatin in islet delta cells
    • 11. Shi, Y, An, J., Liang, J., Hayes, S.E., Sandusky, G.E., Stramm, L.E. & Yang, N.N. (1999) Characterization of a mutant pancreatic eIF-2α kinase, PEK, and co-localization with somatostatin in islet delta cells. J. Biol. Chem. 274, 5723-5730.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5723-5730
    • Shi, Y.1    An, J.2    Liang, J.3    Hayes, S.E.4    Sandusky, G.E.5    Stramm, L.E.6    Yang, N.N.7
  • 12
    • 0030911360 scopus 로고    scopus 로고
    • Cloning and characterization of cDNA encoding a protein synthesis initiation factor-2α (eIF-2α) kinase from Drosophila melanogaster: Homology to yeast GCN2 protein kinase
    • 12. Santoyo, J., Alcalde, J., Méndez, R., Pulido, D. & de Haro, C. (1997) Cloning and characterization of cDNA encoding a protein synthesis initiation factor-2α (eIF-2α) kinase from Drosophila melanogaster: homology to yeast GCN2 protein kinase. J. Biol. Chem. 272, 12544-12550.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12544-12550
    • Santoyo, J.1    Alcalde, J.2    Méndez, R.3    Pulido, D.4    De Haro, C.5
  • 13
    • 0032493732 scopus 로고    scopus 로고
    • cpc-3, the Neurospora crassa homologue of yeast GCN2, encodes a polypeptide with juxtaposed eIF2α kinase and histidyl-tRNA synthetase-related domains required for general amino acid control
    • 13. Sattlegger, E., Hinnebusch, A.C. & Barthelmess, I.B. (1998) cpc-3, the Neurospora crassa homologue of yeast GCN2, encodes a polypeptide with juxtaposed eIF2α kinase and histidyl-tRNA synthetase-related domains required for general amino acid control. J. Biol. Chem. 273, 20404-20416.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20404-20416
    • Sattlegger, E.1    Hinnebusch, A.C.2    Barthelmess, I.B.3
  • 14
    • 0002352428 scopus 로고    scopus 로고
    • Protein kinases that phosphorylate eIF2 and eIF2B, and their role in eukaryotic cell translational control
    • (Hershey, J.W., Mathews, M.B. & Sonenberg, N., eds), Cold Spring Harbor Laboratory Press, Plainview, NY
    • 14. Clemens, M.J. (1996) Protein kinases that phosphorylate eIF2 and eIF2B, and their role in eukaryotic cell translational control. In Translational Control (Hershey, J.W., Mathews, M.B. & Sonenberg, N., eds), pp. 139-172. Cold Spring Harbor Laboratory Press, Plainview, NY.
    • (1996) Translational Control , pp. 139-172
    • Clemens, M.J.1
  • 15
    • 0023665208 scopus 로고
    • Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis
    • 15. Scorsone, K.A., Panniers, R., Rowlands, A.G. & Henshaw, E.C. (1987) Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis. J. Biol. Chem. 262, 14538-14543.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14538-14543
    • Scorsone, K.A.1    Panniers, R.2    Rowlands, A.G.3    Henshaw, E.C.4
  • 16
    • 0023125673 scopus 로고
    • Regulation of polypeptide chain initiation in Chinese hamster ovary cells with a temperature-sensitive leucyl-tRNA synthetase
    • 16. Clemens, M.J., Galpine, A., Austin, S.A., Panniers, R., Henshaw, E.C., Duncan, R., Hershey, J.W.B. & Pollard, J.W. (1987) Regulation of polypeptide chain initiation in Chinese hamster ovary cells with a temperature-sensitive leucyl-tRNA synthetase. J. Biol. Chem. 262, 767-771.
    • (1987) J. Biol. Chem. , vol.262 , pp. 767-771
    • Clemens, M.J.1    Galpine, A.2    Austin, S.A.3    Panniers, R.4    Henshaw, E.C.5    Duncan, R.6    Hershey, J.W.B.7    Pollard, J.W.8
  • 17
    • 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
    • 17. Vázquez de Aldana, C.R., Marton, M.J. & Hinnebusch, A.G. (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.
    • (1995) EMBO J. , vol.14 , pp. 3184-3199
    • Vázquez De Aldana, C.R.1    Marton, M.J.2    Hinnebusch, A.G.3
  • 18
    • 1842287951 scopus 로고    scopus 로고
    • Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2α kinase GCN2
    • 18. Marton, M.J., Vazquez de Aldana, C.R., Qiu, H., Chakraburtty, K. & Hinnebusch, A.G. (1997) Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2α kinase GCN2. Mol. Cell. Biol. 17, 4474-4489.
    • (1997) Mol. Cell. Biol. , 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
  • 19
    • 0026725775 scopus 로고
    • Regulation of heme-controlled eukaryotic polypeptide chain initiation factor 2α-subunit kinase of reticulocyte lysates
    • 19. Méndez, R., Moreno, A. & de Haro, C. (1992) Regulation of heme-controlled eukaryotic polypeptide chain initiation factor 2α-subunit kinase of reticulocyte lysates. J. Biol. Chem. 267, 11500-11507.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11500-11507
    • Méndez, R.1    Moreno, A.2    De Haro, C.3
  • 20
    • 0033610887 scopus 로고    scopus 로고
    • Characterization of the hemin-sensitive eukaryotic initiation factor 2α kinase from mouse nonerythroid cells
    • 20. Berlanga, J.J., Herrero, S. & de Haro, C. (1998) Characterization of the hemin-sensitive eukaryotic initiation factor 2α kinase from mouse nonerythroid cells. J. Biol. Chem. 273, 32340-32346.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32340-32346
    • Berlanga, J.J.1    Herrero, S.2    De Haro, C.3
  • 23
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • 23. Pearson, W.R. & Lipman, D.J. (1988) Improved tools for biological sequence comparison. Proc. Natl Acad. Sci. USA 85, 2444-2448.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 24
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • 24. Thompson, J.D., Higgins, D.G. & Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 25
    • 0028108282 scopus 로고
    • Casein kinase II is implicated in the regulation of heme-controlled translational inhibitor of reticulocyte lysates
    • 25. Méndez, R. & de Haro, C. (1994) Casein kinase II is implicated in the regulation of heme-controlled translational inhibitor of reticulocyte lysates. J. Biol. Chem. 269, 6170-6176.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6170-6176
    • Méndez, R.1    De Haro, C.2
  • 26
    • 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
    • 26. Wek, R.C., Jackson, B.M. & Hinnebusch, A.G. (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. Proc. Natl Acad. Sci. USA 86, 4579-4583.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 4579-4583
    • Wek, R.C.1    Jackson, B.M.2    Hinnebusch, A.G.3
  • 27
    • 0023660877 scopus 로고
    • At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells
    • 27. Kozak, M. (1987) At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells. J. Mol. Biol. 196, 947-950.
    • (1987) J. Mol. Biol. , vol.196 , pp. 947-950
    • Kozak, M.1
  • 28
    • 0026495211 scopus 로고
    • Mutations activating the yeast eIF-2α kinase GCN2: Isolation of alleles altering the domain related to histidyl-tRNA synthetases
    • 28. Ramirez, M., Wek, R.C., Vazquez de Aldana, C.R., Jackson, B.M., Freeman, B. & Hinnebusch, A.G. (1992) Mutations activating the yeast eIF-2α kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases. Mol. Cell. Biol. 12, 5801-5815.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5801-5815
    • Ramirez, M.1    Wek, R.C.2    Vazquez De Aldana, C.R.3    Jackson, B.M.4    Freeman, B.5    Hinnebusch, A.G.6
  • 29
    • 0022260969 scopus 로고
    • Regulation of initiation factors during translational repression caused by serum depletion. Covalent modification
    • 29. Duncan, R. & Hershey, J.W.B. (1985) Regulation of initiation factors during translational repression caused by serum depletion. Covalent modification. J. Biol. Chem. 260, 5493-5497.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5493-5497
    • Duncan, R.1    Hershey, J.W.B.2
  • 30
    • 0028171125 scopus 로고
    • eIF-2 kinases: Regulators of general and gene-specific translation initiation
    • 30. Wek, R.C. (1994) eIF-2 kinases: regulators of general and gene-specific translation initiation. Trends Biochem. Sci. 19, 491-496.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 491-496
    • Wek, R.C.1
  • 31
    • 0030788568 scopus 로고    scopus 로고
    • The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase
    • 31. Arnez, J.G., Augustine, J.G. & Franklyn, C.S. (1997) The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase. Proc. Natl Acad. Sci. USA 94, 7144-7149.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7144-7149
    • Arnez, J.G.1    Augustine, J.G.2    Franklyn, C.S.3
  • 32
    • 0029785485 scopus 로고    scopus 로고
    • Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2
    • 32. Zhu, S., Sobolev, A.Y. & Wek, R.C. (1996) Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2. J. Biol. Chem. 271, 24989-24994.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24989-24994
    • Zhu, S.1    Sobolev, A.Y.2    Wek, R.C.3
  • 33
    • 0031899816 scopus 로고    scopus 로고
    • Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2α kinases PKR and GCN2
    • 33. Romano, P.R., García-Barrio, M.T., Zhang, X., Wang, Q., Taylor, D.R., Zhang, F., Herring, C., Mathews, M.B., Qin, J. & Hinnebusch, A.G. (1998) Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2α kinases PKR and GCN2. Mol. Cell. Biol. 18, 2282-2297.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2282-2297
    • Romano, P.R.1    García-Barrio, M.T.2    Zhang, X.3    Wang, Q.4    Taylor, D.R.5    Zhang, F.6    Herring, C.7    Mathews, M.B.8    Qin, J.9    Hinnebusch, A.G.10
  • 34
    • 0026465921 scopus 로고
    • Protein phosphorylation in translational control
    • 34. Proud, C.G. (1992) Protein phosphorylation in translational control. Curr. Top. Cell. Regul. 32, 243-369.
    • (1992) Curr. Top. Cell. Regul. , vol.32 , pp. 243-369
    • Proud, C.G.1
  • 35
    • 0032528917 scopus 로고    scopus 로고
    • Amino acid availability regulates p70, S6 kinase and multiple translation factors
    • 35. Wang, X., Campbell, L.E., Miller, C.M. & Proud, C.G. (1998) Amino acid availability regulates p70, S6 kinase and multiple translation factors. Biochem. J. 334, 261-267.
    • (1998) Biochem. J. , vol.334 , pp. 261-267
    • Wang, X.1    Campbell, L.E.2    Miller, C.M.3    Proud, C.G.4
  • 36
    • 0032553411 scopus 로고    scopus 로고
    • Implication of eIF2B rather than eIF4E in the regulation of global protein synthesis by amino acids in L6 myoblast
    • 36. Kimball, S.R., Horetsky, R.L. & Jefferson, L.S. (1998) Implication of eIF2B rather than eIF4E in the regulation of global protein synthesis by amino acids in L6 myoblast. J. Biol. Chem. 273, 30945-30953.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30945-30953
    • Kimball, S.R.1    Horetsky, R.L.2    Jefferson, L.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.