메뉴 건너뛰기




Volumn 44, Issue 2, 2014, Pages 139-146

GCN2-like eIF2α kinase manages the amino acid starvation response in Toxoplasma gondii

Author keywords

Apicomplexa; EIF2 kinase; Glutamine; Parasite; Stress; Translational control

Indexed keywords

COMPLEMENTARY DNA; GCN2 LIKE EIF2A KINASE C; GCN2 LIKE EIF2A KINASE D; GLUTAMINE; INITIATION FACTOR 2ALPHA; UNCLASSIFIED DRUG;

EID: 84892555028     PISSN: 00207519     EISSN: 18790135     Source Type: Journal    
DOI: 10.1016/j.ijpara.2013.08.005     Document Type: Article
Times cited : (26)

References (47)
  • 2
    • 84866782195 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism
    • Baird T.D., Wek R.C. Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism. Adv. Nutr. 2012, 3:307-321.
    • (2012) Adv. Nutr. , vol.3 , pp. 307-321
    • Baird, T.D.1    Wek, R.C.2
  • 4
    • 0001598487 scopus 로고    scopus 로고
    • Characterization of a mammalian homologu of the GCN2 eukaryotic initiation factor 2alpha kinase
    • Berlanga J.J., Santoyo J., De Haro C. Characterization of a mammalian homologu of the GCN2 eukaryotic initiation factor 2alpha kinase. Eur. J. Biochem. 1999, 265:754-762.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 754-762
    • Berlanga, J.J.1    Santoyo, J.2    De Haro, C.3
  • 6
    • 79955366731 scopus 로고    scopus 로고
    • EIF2{alpha} kinases control chalone production in Dictyostelium discoideum
    • Bowman R.L., Xiong Y., Kirsten J.H., Singleton C.K. EIF2{alpha} kinases control chalone production in Dictyostelium discoideum. Eukaryot. Cell 2011, 10:494-501.
    • (2011) Eukaryot. Cell , vol.10 , pp. 494-501
    • Bowman, R.L.1    Xiong, Y.2    Kirsten, J.H.3    Singleton, C.K.4
  • 7
    • 27144462250 scopus 로고    scopus 로고
    • Protozoan genomics for drug discovery
    • Chaudhary K., Roos D.S. Protozoan genomics for drug discovery. Nat. Biotechnol. 2005, 23:3.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 3
    • Chaudhary, K.1    Roos, D.S.2
  • 8
    • 33947584856 scopus 로고    scopus 로고
    • Regulation of protein synthesis by the heme-regulated eIF2alpha kinase: relevance to anemias
    • Chen J.J. Regulation of protein synthesis by the heme-regulated eIF2alpha kinase: relevance to anemias. Blood 2007, 109:2693-2699.
    • (2007) Blood , vol.109 , pp. 2693-2699
    • Chen, J.J.1
  • 9
    • 0029099953 scopus 로고
    • Regulation of glutaminase activity and glutamine metabolism
    • Curthoys N.P., Watford M. Regulation of glutaminase activity and glutamine metabolism. Ann. Rev. Nutr. 1995, 15:133-159.
    • (1995) Ann. Rev. Nutr. , vol.15 , pp. 133-159
    • Curthoys, N.P.1    Watford, M.2
  • 10
    • 0027136119 scopus 로고
    • Stable molecular transformation of Toxoplasma gondii: a selectable dihydrofolate reductase-thymidylate synthase marker based on drug-resistance mutations in malaria
    • Donald R.G., Roos D.S. Stable molecular transformation of Toxoplasma gondii: a selectable dihydrofolate reductase-thymidylate synthase marker based on drug-resistance mutations in malaria. Proc. Natl. Acad. Sci. USA 1993, 90:11703-11707.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11703-11707
    • Donald, R.G.1    Roos, D.S.2
  • 11
    • 84884353774 scopus 로고    scopus 로고
    • The eIF2alpha kinases: their structures and functions
    • Donnelly N., Gorman A.M., Gupta S., Samali A. The eIF2alpha kinases: their structures and functions. Cell. Mol. Life Sci. 2013, 70(19):3493-3511.
    • (2013) Cell. Mol. Life Sci. , vol.70 , Issue.19 , pp. 3493-3511
    • Donnelly, N.1    Gorman, A.M.2    Gupta, S.3    Samali, A.4
  • 12
    • 66149109088 scopus 로고    scopus 로고
    • PfeIK1, a eukaryotic initiation factor 2alpha kinase of the human malaria parasite Plasmodium falciparum, regulates stress-response to amino-acid starvation
    • Fennell C., Babbitt S., Russo I., Wilkes J., Ranford-Cartwright L., Goldberg D.E., Doerig C. PfeIK1, a eukaryotic initiation factor 2alpha kinase of the human malaria parasite Plasmodium falciparum, regulates stress-response to amino-acid starvation. Malar. J. 2009, 8:99.
    • (2009) Malar. J. , vol.8 , pp. 99
    • Fennell, C.1    Babbitt, S.2    Russo, I.3    Wilkes, J.4    Ranford-Cartwright, L.5    Goldberg, D.E.6    Doerig, C.7
  • 13
    • 0037148779 scopus 로고    scopus 로고
    • De novo pyrimidine biosynthesis is required for virulence of Toxoplasma gondii
    • Fox B.A., Bzik D.J. De novo pyrimidine biosynthesis is required for virulence of Toxoplasma gondii. Nature 2002, 415:926-929.
    • (2002) Nature , vol.415 , pp. 926-929
    • Fox, B.A.1    Bzik, D.J.2
  • 14
    • 77956646014 scopus 로고    scopus 로고
    • Avirulent uracil auxotrophs based on disruption of orotidine-5'-monophosphate decarboxylase elicit protective immunity to Toxoplasma gondii
    • Fox B.A., Bzik D.J. Avirulent uracil auxotrophs based on disruption of orotidine-5'-monophosphate decarboxylase elicit protective immunity to Toxoplasma gondii. Infect. Immun. 2010, 78:3744-3752.
    • (2010) Infect. Immun. , vol.78 , pp. 3744-3752
    • Fox, B.A.1    Bzik, D.J.2
  • 15
    • 1542375414 scopus 로고    scopus 로고
    • Toxoplasma gondii lacks the enzymes required for de novo arginine biosynthesis and arginine starvation triggers cyst formation
    • Fox B.A., Gigley J.P., Bzik D.J. Toxoplasma gondii lacks the enzymes required for de novo arginine biosynthesis and arginine starvation triggers cyst formation. Int. J. Parasitol. 2004, 34:323-331.
    • (2004) Int. J. Parasitol. , vol.34 , pp. 323-331
    • Fox, B.A.1    Gigley, J.P.2    Bzik, D.J.3
  • 16
    • 64749115995 scopus 로고    scopus 로고
    • Efficient gene replacements in Toxoplasma gondii strains deficient for nonhomologous end joining
    • Fox B.A., Ristuccia J.G., Gigley J.P., Bzik D.J. Efficient gene replacements in Toxoplasma gondii strains deficient for nonhomologous end joining. Eukaryot. Cell 2009, 8:520-529.
    • (2009) Eukaryot. Cell , vol.8 , pp. 520-529
    • Fox, B.A.1    Ristuccia, J.G.2    Gigley, J.P.3    Bzik, D.J.4
  • 17
    • 0034678890 scopus 로고    scopus 로고
    • Association of GCN1-GCN20 regulatory complex with the N-terminus of eIF2alpha kinase GCN2 is required for GCN2 activation
    • Garcia-Barrio M., Dong J., Ulfano S., Hinnebusch A.G. Association of GCN1-GCN20 regulatory complex with the N-terminus of eIF2alpha kinase GCN2 is required for GCN2 activation. EMBO J. 2000, 19:1887-1899.
    • (2000) EMBO J. , vol.19 , pp. 1887-1899
    • Garcia-Barrio, M.1    Dong, J.2    Ulfano, S.3    Hinnebusch, A.G.4
  • 18
    • 84858290288 scopus 로고    scopus 로고
    • Autophagy is a cell death mechanism in Toxoplasma gondii
    • Ghosh D., Walton J.L., Roepe P.D., Sinai A.P. Autophagy is a cell death mechanism in Toxoplasma gondii. Cell. Microbiol. 2012, 14(4):589-607.
    • (2012) Cell. Microbiol. , vol.14 , Issue.4 , pp. 589-607
    • Ghosh, D.1    Walton, J.L.2    Roepe, P.D.3    Sinai, A.P.4
  • 20
    • 27144510561 scopus 로고    scopus 로고
    • Translational regulation of GCN4 and the general amino acid control of yeast
    • Hinnebusch A.G. Translational regulation of GCN4 and the general amino acid control of yeast. Ann. Rev. Microbiol. 2005, 59:407-450.
    • (2005) Ann. Rev. Microbiol. , vol.59 , pp. 407-450
    • Hinnebusch, A.G.1
  • 21
    • 64749102772 scopus 로고    scopus 로고
    • Tagging of endogenous genes in a Toxoplasma gondii strain lacking Ku80
    • Huynh M.H., Carruthers V.B. Tagging of endogenous genes in a Toxoplasma gondii strain lacking Ku80. Eukaryot. Cell 2009, 8:530-539.
    • (2009) Eukaryot. Cell , vol.8 , pp. 530-539
    • Huynh, M.H.1    Carruthers, V.B.2
  • 22
    • 78049249377 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor-2{alpha} promotes the extracellular survival of obligate intracellular parasite Toxoplasma gondii
    • Joyce B.R., Queener S.F., Wek R.C., Sullivan W.J. Phosphorylation of eukaryotic initiation factor-2{alpha} promotes the extracellular survival of obligate intracellular parasite Toxoplasma gondii. Proc. Natl. Acad. Sci. USA 2010, 107:17200-17205.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17200-17205
    • Joyce, B.R.1    Queener, S.F.2    Wek, R.C.3    Sullivan, W.J.4
  • 23
    • 84879339845 scopus 로고    scopus 로고
    • The unfolded protein response in the protozoan parasite Toxoplasma gondii features translational and transcriptional control
    • Joyce B.R., Tampaki Z., Kim K., Wek R.C., Sullivan W.J. The unfolded protein response in the protozoan parasite Toxoplasma gondii features translational and transcriptional control. Eukaryot. Cell 2013, 12(7):979-989.
    • (2013) Eukaryot. Cell , vol.12 , Issue.7 , pp. 979-989
    • Joyce, B.R.1    Tampaki, Z.2    Kim, K.3    Wek, R.C.4    Sullivan, W.J.5
  • 24
    • 84875206408 scopus 로고    scopus 로고
    • Inhibitors of eIF2alpha dephosphorylation slow replication and stabilize latency in Toxoplasma gondii
    • Konrad C., Queener S.F., Wek R.C., Sullivan W.J. Inhibitors of eIF2alpha dephosphorylation slow replication and stabilize latency in Toxoplasma gondii. Antimicrob. Agents Chemother. 2013, 57(4):1815-1822.
    • (2013) Antimicrob. Agents Chemother. , vol.57 , Issue.4 , pp. 1815-1822
    • Konrad, C.1    Queener, S.F.2    Wek, R.C.3    Sullivan, W.J.4
  • 25
    • 80055104493 scopus 로고    scopus 로고
    • A GCN2-like eukaryotic initiation factor 2 kinase increases the viability of extracellular Toxoplasma gondii parasites
    • Konrad C., Wek R.C., Sullivan W.J. A GCN2-like eukaryotic initiation factor 2 kinase increases the viability of extracellular Toxoplasma gondii parasites. Eukaryot. Cell 2011, 10:1403-1412.
    • (2011) Eukaryot. Cell , vol.10 , pp. 1403-1412
    • Konrad, C.1    Wek, R.C.2    Sullivan, W.J.3
  • 26
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: recent updates to the protein domain annotation resource
    • Letunic I., Doerks T., Bork P. SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res. 2012, 40:D302-D305.
    • (2012) Nucleic Acids Res. , vol.40
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 27
    • 0036926615 scopus 로고    scopus 로고
    • A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site
    • Stols Lucy, Gu Minyi, Dieckman Lynda, Raffen Rosemarie, Collart Frank R., Donnelly M.I. A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site. Protein Expr. Purif. 2002, 25:8.
    • (2002) Protein Expr. Purif. , vol.25 , pp. 8
    • Stols, L.1    Gu, M.2    Dieckman, L.3    Raffen, R.4    Collart, F.R.5    Donnelly, M.I.6
  • 28
    • 84869167609 scopus 로고    scopus 로고
    • Mitochondrial metabolism of glucose and glutamine is required for intracellular growth of Toxoplasma gondii
    • Macrae J.I., Sheiner L., Nahid A., Tonkin C., Striepen B., McConville M.J. Mitochondrial metabolism of glucose and glutamine is required for intracellular growth of Toxoplasma gondii. Cell Host Microbe 2012, 12:682-692.
    • (2012) Cell Host Microbe , vol.12 , pp. 682-692
    • Macrae, J.I.1    Sheiner, L.2    Nahid, A.3    Tonkin, C.4    Striepen, B.5    McConville, M.J.6
  • 29
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • Marciniak S.J., Ron D. Endoplasmic reticulum stress signaling in disease. Physiol. Rev. 2006, 86:1133-1149.
    • (2006) Physiol. Rev. , vol.86 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 33
    • 0031946361 scopus 로고    scopus 로고
    • Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain
    • Qiu H., Garcia-Barrio M.T., Hinnebusch A.G. Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain. Mol. Cell. Biol. 1998, 18:2697-2711.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2697-2711
    • Qiu, H.1    Garcia-Barrio, M.T.2    Hinnebusch, A.G.3
  • 34
    • 33845539293 scopus 로고    scopus 로고
    • Disruption of the ifkA and ifkB genes results in altered cell adhesion, morphological defects and a propensity to form pre-stalk O cells during development of Dictyostelium
    • Rai M., Xiong Y., Singleton C.K. Disruption of the ifkA and ifkB genes results in altered cell adhesion, morphological defects and a propensity to form pre-stalk O cells during development of Dictyostelium. Differentiation 2006, 74:583-595.
    • (2006) Differentiation , vol.74 , pp. 583-595
    • Rai, M.1    Xiong, Y.2    Singleton, C.K.3
  • 35
    • 44349125754 scopus 로고    scopus 로고
    • PERK and PKR: old kinases learn new tricks
    • Raven J.F., Koromilas A.E. PERK and PKR: old kinases learn new tricks. Cell Cycle 2008, 7:1146-1150.
    • (2008) Cell Cycle , vol.7 , pp. 1146-1150
    • Raven, J.F.1    Koromilas, A.E.2
  • 36
    • 0028709114 scopus 로고
    • Molecular tools for genetic dissection of the protozoan parasite Toxoplasma gondii
    • Roos D.S., Donald R.G., Morrissette N.S., Moulton A.L. Molecular tools for genetic dissection of the protozoan parasite Toxoplasma gondii. Methods Cell Biol. 1994, 45:27-63.
    • (1994) Methods Cell Biol. , vol.45 , pp. 27-63
    • Roos, D.S.1    Donald, R.G.2    Morrissette, N.S.3    Moulton, A.L.4
  • 38
    • 84857751667 scopus 로고    scopus 로고
    • EIF2alpha kinases regulate development through the BzpR transcription factor in Dictyostelium discoideum
    • Singleton C.K., Xiong Y., Kirsten J.H., Pendleton K.P. EIF2alpha kinases regulate development through the BzpR transcription factor in Dictyostelium discoideum. PLoS ONE 2012, 7:e32500.
    • (2012) PLoS ONE , vol.7
    • Singleton, C.K.1    Xiong, Y.2    Kirsten, J.H.3    Pendleton, K.P.4
  • 39
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N., Hinnebusch A.G. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 2009, 136:731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 40
    • 0033962298 scopus 로고    scopus 로고
    • A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alpha
    • Sood R., Porter A.C., Olsen D.A., Cavener D.R., Wek R.C. A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alpha. Genetics 2000, 154:787-801.
    • (2000) Genetics , vol.154 , pp. 787-801
    • Sood, R.1    Porter, A.C.2    Olsen, D.A.3    Cavener, D.R.4    Wek, R.C.5
  • 41
    • 2942714921 scopus 로고    scopus 로고
    • Parasite-specific eIF2 (eukaryotic initiation factor-2) kinase required for stress-induced translation control
    • Sullivan W.J., Narasimhan J., Bhatti M.M., Wek R.C. Parasite-specific eIF2 (eukaryotic initiation factor-2) kinase required for stress-induced translation control. Biochem. J. 2004, 380:523-531.
    • (2004) Biochem. J. , vol.380 , pp. 523-531
    • Sullivan, W.J.1    Narasimhan, J.2    Bhatti, M.M.3    Wek, R.C.4
  • 42
    • 84859350581 scopus 로고    scopus 로고
    • Mechanisms of Toxoplasma gondii persistence and latency
    • Sullivan W.J., Jeffers V. Mechanisms of Toxoplasma gondii persistence and latency. FEMS Microbiol. Rev. 2012, 36:717-733.
    • (2012) FEMS Microbiol. Rev. , vol.36 , pp. 717-733
    • Sullivan, W.J.1    Jeffers, V.2
  • 43
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter P., Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011, 334:1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 44
    • 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 R.C., Jackson B.M., Hinnebusch A.G. 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 1989, 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
  • 45
    • 0029006391 scopus 로고
    • The histidyl-tRNA synthetase-related sequence in eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids
    • Wek S.A., Zhu S., Wek R.C. The histidyl-tRNA synthetase-related sequence in eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids. Mol. Cell. Biol. 1995, 15:4497-4506.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4497-4506
    • Wek, S.A.1    Zhu, S.2    Wek, R.C.3
  • 46
    • 11244283763 scopus 로고    scopus 로고
    • Differential activation of eIF2 kinases in response to cellular stresses in Schizosaccharomyces pombe
    • Zhan K., Narasimhan J., Wek R.C. Differential activation of eIF2 kinases in response to cellular stresses in Schizosaccharomyces pombe. Genetics 2004, 168:1867-1875.
    • (2004) Genetics , vol.168 , pp. 1867-1875
    • Zhan, K.1    Narasimhan, J.2    Wek, R.C.3
  • 47
    • 0042352484 scopus 로고    scopus 로고
    • Molecular cloning of an Arabidopsis homologue of GCN2, a protein kinase involved in co-ordinated response to amino acid starvation
    • Zhang Y., Dickinson J.R., Paul M.J., Halford N.G. Molecular cloning of an Arabidopsis homologue of GCN2, a protein kinase involved in co-ordinated response to amino acid starvation. Planta 2003, 217:668-675.
    • (2003) Planta , vol.217 , pp. 668-675
    • Zhang, Y.1    Dickinson, J.R.2    Paul, M.J.3    Halford, N.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.