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Volumn 30, Issue 8, 2010, Pages 2006-2016

OGFOD1, a novel modulator of eukaryotic translation initiation factor 2α phosphorylation and the cellular response to stress

Author keywords

[No Author keywords available]

Indexed keywords

ARSENIC TRIOXIDE; CAPRIN 1 PROTEIN; CELL PROTEIN; G3BP1 PROTEIN; INITIATION FACTOR 2; OGFOD1 PROTEIN; UNCLASSIFIED DRUG; USP10 PROTEIN; Y BOX BINDING PROTEIN 1;

EID: 77950686223     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.01350-09     Document Type: Article
Times cited : (62)

References (28)
  • 1
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: Post-transcriptional and epigenetic modulators of gene expression
    • Anderson, P., and N. Kedersha. 2009. RNA granules: post-transcriptional and epigenetic modulators of gene expression. Nat. Rev. Mol. Cell Biol. 10:430-436.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 2
    • 39949085583 scopus 로고    scopus 로고
    • Stress granules: The tao of RNA triage
    • Anderson, P., and N. Kedersha. 2008. Stress granules: the tao of RNA triage. Trends Biochem. Sci. 33:141-150.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 141-150
    • Anderson, P.1    Kedersha, N.2
  • 3
    • 55549130760 scopus 로고    scopus 로고
    • Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways
    • Arimoto, K., H. Fukuda, S. Imajoh-Ohmi, H. Saito, and M. Takekawa. 2008. Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways. Nat. Cell Biol. 10:1324-1332.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1324-1332
    • Arimoto, K.1    Fukuda, H.2    Imajoh-Ohmi, S.3    Saito, H.4    Takekawa, M.5
  • 5
    • 0033081226 scopus 로고    scopus 로고
    • Human DNA helicase VIII: A DNA and RNA helicase corresponding to the G3BP protein, an element of the Ras transduction pathway
    • DOI 10.1093/nar/27.3.817
    • Costa, M., A. Ochem, A. Staub, and A. Falaschi. 1999. Human DNA helicase VIII: a DNA and RNA helicase corresponding to the G3BP protein, an element of the ras transduction pathway. Nucleic Acids Res. 27:817-821. (Pubitemid 29209370)
    • (1999) Nucleic Acids Research , vol.27 , Issue.3 , pp. 817-821
    • Costa, M.1    Ochem, A.2    Staub, A.3    Falaschi, A.4
  • 8
    • 0035190991 scopus 로고    scopus 로고
    • Molecular mechanisms of gene expression regulation by the apoptosis-promoting protein TIA-1
    • DOI 10.1023/A:1012441824719
    • Forch, P., and J. Valcarcel. 2001. Molecular mechanisms of gene expression regulation by the apoptosis-promoting protein TIA-1. Apoptosis 6:463-468. (Pubitemid 33078757)
    • (2001) Apoptosis , vol.6 , Issue.6 , pp. 463-468
    • Forch, P.1    Valcarcel, J.2
  • 10
    • 17944362905 scopus 로고    scopus 로고
    • Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency
    • Han, A. P., C. Yu, L. Lu, Y. Fujiwara, C. Browne, G. Chin, M. Fleming, P. Leboulch, S. H. Orkin, and J. J. Chen. 2001. Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency. EMBO J. 20:6909-6918.
    • (2001) EMBO J. , vol.20 , pp. 6909-6918
    • Han, A.P.1    Yu, C.2    Lu, L.3    Fujiwara, Y.4    Browne, C.5    Chin, G.6    Fleming, M.7    Leboulch, P.8    Orkin, S.H.9    Chen, J.J.10
  • 11
    • 34249665243 scopus 로고    scopus 로고
    • Mechanism of translation initiation in the yeast Saccharomyces cerevisiae
    • M. B. Mathews, N. Sonenberg, and J. W. B. Hershey (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hinnebusch, A. G., T. E. Dever, and K. Asano. 2007. Mechanism of translation initiation in the yeast Saccharomyces cerevisiae, p. 225-268. In M. B. Mathews, N. Sonenberg, and J. W. B. Hershey (ed.), Translational control in biology and medicine. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2007) Translational Control in Biology and Medicine , pp. 225-268
    • Hinnebusch, A.G.1    Dever, T.E.2    Asano, K.3
  • 12
    • 44349091967 scopus 로고    scopus 로고
    • Oxygen-regulated degradation of fission yeast SREBP by Ofd1, A prolyl hydroxylase family member
    • Hughes, B. T., and P. J. Espenshade. 2008. Oxygen-regulated degradation of fission yeast SREBP by Ofd1, a prolyl hydroxylase family member. EMBO J. 27:1491-1501.
    • (2008) EMBO J. , vol.27 , pp. 1491-1501
    • Hughes, B.T.1    Espenshade, P.J.2
  • 13
    • 0345599024 scopus 로고    scopus 로고
    • Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells
    • DOI 10.1083/jcb.200308075
    • Jousse, C., S. Oyadomari, I. Novoa, P. Lu, Y. Zhang, H. P. Harding, and D. Ron. 2003. Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells. J. Cell Biol. 163: 767-775. (Pubitemid 37517884)
    • (2003) Journal of Cell Biology , vol.163 , Issue.4 , pp. 767-775
    • Jousse, C.1    Oyadomari, S.2    Novoa, I.3    Lu, P.4    Zhang, Y.5    Harding, H.P.6    Ron, D.7
  • 14
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules
    • Kedersha, N. L., M. Gupta, W. Li, I. Miller, and P. Anderson. 1999. RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J. Cell Biol. 147:1431-1442.
    • (1999) J. Cell Biol. , vol.147 , pp. 1431-1442
    • Kedersha, N.L.1    Gupta, M.2    Li, W.3    Miller, I.4    Anderson, P.5
  • 15
    • 33745806590 scopus 로고    scopus 로고
    • Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae
    • Keeling, K. M., J. Salas-Marco, L. Z. Osherovich, and D. M. Bedwell. 2006. Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae. Mol. Cell. Biol. 26:5237-5248.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5237-5248
    • Keeling, K.M.1    Salas-Marco, J.2    Osherovich, L.Z.3    Bedwell, D.M.4
  • 16
    • 0033005366 scopus 로고    scopus 로고
    • Eukaryotic initiation factor eIF2
    • Kimball, S. R. 1999. Eukaryotic initiation factor eIF2. Int. J. Biochem. Cell Biol. 31:25-29.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 25-29
    • Kimball, S.R.1
  • 17
    • 0036837864 scopus 로고    scopus 로고
    • Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha
    • Koumenis, C., C. Naczki, M. Koritzinsky, S. Rastani, A. Diehl, N. Sonenberg, A. Koromilas, and B. G. Wouters. 2002. Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha. Mol. Cell. Biol. 22:7405-7416.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7405-7416
    • Koumenis, C.1    Naczki, C.2    Koritzinsky, M.3    Rastani, S.4    Diehl, A.5    Sonenberg, N.6    Koromilas, A.7    Wouters, B.G.8
  • 18
    • 0035166679 scopus 로고    scopus 로고
    • Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses
    • Lu, L., A. P. Han, and J. J. Chen. 2001. Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses. Mol. Cell. Biol. 21:7971-7980.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7971-7980
    • Lu, L.1    Han, A.P.2    Chen, J.J.3
  • 19
    • 0842285401 scopus 로고    scopus 로고
    • Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2
    • DOI 10.1038/sj.emboj.7600030
    • Lu, P. D., C. Jousse, S. J. Marciniak, Y. Zhang, I. Novoa, D. Scheuner, R. J. Kaufman, D. Ron, and H. P. Harding. 2004. Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2. EMBO J. 23: 169-179. (Pubitemid 38165757)
    • (2004) EMBO Journal , vol.23 , Issue.1 , pp. 169-179
    • Lu, P.D.1    Jousse, C.2    Marciniak, S.J.3    Zhang, Y.4    Novoa, I.5    Scheuner, D.6    Kaufman, R.J.7    Ron, D.8    Harding, H.P.9
  • 20
    • 20144378698 scopus 로고    scopus 로고
    • Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure
    • McEwen, E., N. Kedersha, B. Song, D. Scheuner, N. Gilks, A. Han, J. J. Chen, P. Anderson, and R. J. Kaufman. 2005. Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure. J. Biol. Chem. 280:16925-16933.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16925-16933
    • McEwen, E.1    Kedersha, N.2    Song, B.3    Scheuner, D.4    Gilks, N.5    Han, A.6    Chen, J.J.7    Anderson, P.8    Kaufman, R.J.9
  • 21
    • 34247111608 scopus 로고    scopus 로고
    • eIF2α phosphorylation in cellular stress responses and disease
    • M. B. Mathews, N. Sonenberg, and J. W. B. Hershey (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Ron, D., and H. P. Harding. 2007. eIF2α phosphorylation in cellular stress responses and disease, p. 345-368. In M. B. Mathews, N. Sonenberg, and J. W. B. Hershey (ed.), Translational control in biology and medicine. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2007) Translational Control in Biology and Medicine , pp. 345-368
    • Ron, D.1    Harding, H.P.2
  • 22
    • 0023753058 scopus 로고
    • Physiological stresses inhibit guanine-nucleotide-exchange factor in Ehrlich cells
    • Rowlands, A. G., K. S. Montine, E. C. Henshaw, and R. Panniers. 1988. Physiological stresses inhibit guanine-nucleotide-exchange factor in Ehrlich cells. Eur. J. Biochem. 175:93-99.
    • (1988) Eur. J. Biochem. , vol.175 , pp. 93-99
    • Rowlands, A.G.1    Montine, K.S.2    Henshaw, E.C.3    Panniers, R.4
  • 23
    • 0023665208 scopus 로고
    • Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis
    • Scorsone, K. A., R. Panniers, A. G. Rowlands, and E. C. Henshaw. 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
  • 24
    • 33947210861 scopus 로고    scopus 로고
    • Distinct structural features of caprin-1 mediate its interaction with G3BP-1 and its induction of phosphorylation of eukaryotic translation initiation factor 2alpha, entry to cytoplasmic stress granules, and selective interaction with a subset of mRNAs
    • Solomon, S., Y. Xu, B. Wang, M. D. David, P. Schubert, D. Kennedy, and J. W. Schrader. 2007. Distinct structural features of caprin-1 mediate its interaction with G3BP-1 and its induction of phosphorylation of eukaryotic translation initiation factor 2alpha, entry to cytoplasmic stress granules, and selective interaction with a subset of mRNAs. Mol. Cell. Biol. 27:2324-2342.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 2324-2342
    • Solomon, S.1    Xu, Y.2    Wang, B.3    David, M.D.4    Schubert, P.5    Kennedy, D.6    Schrader, J.W.7
  • 26
    • 0031891869 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase
    • Srivastava, S. P., K. U. Kumar, and R. J. Kaufman. 1998. Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase. J. Biol. Chem. 273:2416-2423.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2416-2423
    • Srivastava, S.P.1    Kumar, K.U.2    Kaufman, R.J.3
  • 27
    • 0034775591 scopus 로고    scopus 로고
    • RasGAP-associated endoribonuclease G3Bp: Selective RNA degradation and phosphorylation-dependent localization
    • Tourriere, H., I. E. Gallouzi, K. Chebli, J. P. Capony, J. Mouaikel, P. van der Geer, and J. Tazi. 2001. RasGAP-associated endoribonuclease G3Bp: selective RNA degradation and phosphorylation-dependent localization. Mol. Cell. Biol. 21:7747-7760.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7747-7760
    • Tourriere, H.1    Gallouzi, I.E.2    Chebli, K.3    Capony, J.P.4    Mouaikel, J.5    Van Der Geer, P.6    Tazi, J.7
  • 28
    • 0036787003 scopus 로고    scopus 로고
    • Components of an interdependent unit within the SSU processome regulate and mediate its activity
    • Wehner, K. A., J. E. Gallagher, and S. J. Baserga. 2002. Components of an interdependent unit within the SSU processome regulate and mediate its activity. Mol. Cell. Biol. 22:7258-7267.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7258-7267
    • Wehner, K.A.1    Gallagher, J.E.2    Baserga, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.