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Volumn 314, Issue 5, 2008, Pages 961-968

Inhibition of translation and modification of translation factors during apoptosis induced by the DNA-damaging agent MMS in sea urchin embryos

Author keywords

Apoptosis; DNA damaging agent; Protein synthesis; Sea urchin; Translation factors

Indexed keywords

INITIATION FACTOR 2; INITIATION FACTOR 4E BINDING PROTEIN 1; INITIATION FACTOR 4G; MESYLIC ACID METHYL ESTER;

EID: 39649116675     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2007.12.014     Document Type: Article
Times cited : (14)

References (44)
  • 1
    • 0000091608 scopus 로고    scopus 로고
    • Pathway and mechanism of initiation of protein synthesis
    • Sonenberg N., Hershey J.W., and Mathews M.B. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Hershey J.W., and Merrick W.C. Pathway and mechanism of initiation of protein synthesis. In: Sonenberg N., Hershey J.W., and Mathews M.B. (Eds). Translational control of gene expression (2000), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • (2000) Translational control of gene expression
    • Hershey, J.W.1    Merrick, W.C.2
  • 2
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins
    • Mader S., Lee H., Pause A., and Sonenberg N. The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins. Mol. Cell Biol. 15 (1995) 4990-4997
    • (1995) Mol. Cell Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 4
    • 0038095426 scopus 로고    scopus 로고
    • M-phase regulation of the recruitment of mRNAs onto polysomes using the CDK1/cyclin B inhibitor aminopurvalanol
    • Le Breton M., Belle R., Cormier P., Mulner-Lorillon O., and Morales J. M-phase regulation of the recruitment of mRNAs onto polysomes using the CDK1/cyclin B inhibitor aminopurvalanol. Biochem. Biophys. Res. Commun. 306 (2003) 880-886
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 880-886
    • Le Breton, M.1    Belle, R.2    Cormier, P.3    Mulner-Lorillon, O.4    Morales, J.5
  • 7
    • 33847408853 scopus 로고    scopus 로고
    • After fertilization of sea urchin eggs, eIF4G is post-translationally modified and associated with the cap-binding protein eIF4E
    • Oulhen N., Salaun P., Cosson B., Cormier P., and Morales J. After fertilization of sea urchin eggs, eIF4G is post-translationally modified and associated with the cap-binding protein eIF4E. J. Cell Sci. 120 (2007) 425-434
    • (2007) J. Cell Sci. , vol.120 , pp. 425-434
    • Oulhen, N.1    Salaun, P.2    Cosson, B.3    Cormier, P.4    Morales, J.5
  • 9
    • 0142027948 scopus 로고    scopus 로고
    • Ways of dying: multiple pathways to apoptosis
    • Adams J.M. Ways of dying: multiple pathways to apoptosis. Genes Dev. 17 (2003) 2481-2495
    • (2003) Genes Dev. , vol.17 , pp. 2481-2495
    • Adams, J.M.1
  • 10
    • 2342459790 scopus 로고    scopus 로고
    • DNA damage-induced apoptosis
    • Norbury C.J., and Zhivotovsky B. DNA damage-induced apoptosis. Oncogene 23 (2004) 2797-2808
    • (2004) Oncogene , vol.23 , pp. 2797-2808
    • Norbury, C.J.1    Zhivotovsky, B.2
  • 11
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • Holcik M., and Sonenberg N. Translational control in stress and apoptosis. Nat. Rev. Mol. Cell Biol 6 (2005) 318-327
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 12
    • 20144365870 scopus 로고    scopus 로고
    • Initiation factor modifications in the preapoptotic phase
    • Morley S.J., Coldwell M.J., and Clemens M.J. Initiation factor modifications in the preapoptotic phase. Cell Death Differ 12 (2005) 571-584
    • (2005) Cell Death Differ , vol.12 , pp. 571-584
    • Morley, S.J.1    Coldwell, M.J.2    Clemens, M.J.3
  • 13
    • 0037089549 scopus 로고    scopus 로고
    • Inhibition of protein synthesis in apoptosis: differential requirements by the tumor necrosis factor alpha family and a DNA-damaging agent for caspases and the double-stranded RNA-dependent protein kinase
    • Jeffrey I.W., Bushell M., Tilleray V.J., Morley S., and Clemens M.J. Inhibition of protein synthesis in apoptosis: differential requirements by the tumor necrosis factor alpha family and a DNA-damaging agent for caspases and the double-stranded RNA-dependent protein kinase. Cancer Res 62 (2002) 2272-2280
    • (2002) Cancer Res , vol.62 , pp. 2272-2280
    • Jeffrey, I.W.1    Bushell, M.2    Tilleray, V.J.3    Morley, S.4    Clemens, M.J.5
  • 14
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap
    • Lazaris-Karatzas A., Montine K.S., and Sonenberg N. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap. Nature 345 (1990) 544-547
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 16
    • 0343167422 scopus 로고    scopus 로고
    • Rapid induction of apoptosis mediated by peptides that bind initiation factor eIF4E
    • Herbert T.P., Fahraeus R., Prescott A., Lane D.P., and Proud C.G. Rapid induction of apoptosis mediated by peptides that bind initiation factor eIF4E. Curr. Biol. 10 (2000) 793-796
    • (2000) Curr. Biol. , vol.10 , pp. 793-796
    • Herbert, T.P.1    Fahraeus, R.2    Prescott, A.3    Lane, D.P.4    Proud, C.G.5
  • 17
    • 0030443685 scopus 로고    scopus 로고
    • The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth
    • Rousseau D., Gingras A.C., Pause A., and Sonenberg N. The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth. Oncogene 13 (1996) 2415-2420
    • (1996) Oncogene , vol.13 , pp. 2415-2420
    • Rousseau, D.1    Gingras, A.C.2    Pause, A.3    Sonenberg, N.4
  • 18
    • 23944525416 scopus 로고    scopus 로고
    • 4E-BP functions as a metabolic brake used under stress conditions but not during normal growth
    • Teleman A.A., Chen Y.W., and Cohen S.M. 4E-BP functions as a metabolic brake used under stress conditions but not during normal growth. Genes Dev. 19 (2005) 1844-1848
    • (2005) Genes Dev. , vol.19 , pp. 1844-1848
    • Teleman, A.A.1    Chen, Y.W.2    Cohen, S.M.3
  • 19
    • 23944507152 scopus 로고    scopus 로고
    • Starvation and oxidative stress resistance in Drosophila are mediated through the eIF4E-binding protein, d4E-BP
    • Tettweiler G., Miron M., Jenkins M., Sonenberg N., and Lasko P.F. Starvation and oxidative stress resistance in Drosophila are mediated through the eIF4E-binding protein, d4E-BP. Genes Dev. 19 (2005) 1840-1843
    • (2005) Genes Dev. , vol.19 , pp. 1840-1843
    • Tettweiler, G.1    Miron, M.2    Jenkins, M.3    Sonenberg, N.4    Lasko, P.F.5
  • 20
    • 33748087093 scopus 로고    scopus 로고
    • Hypoxia and DNA-damaging agent bleomycin both increase the cellular level of the protein 4E-BP
    • Le Bouffant R., Cormier P., Mulner-Lorillon O., and Belle R. Hypoxia and DNA-damaging agent bleomycin both increase the cellular level of the protein 4E-BP. J. Cell Biochem. 99 (2006) 126-132
    • (2006) J. Cell Biochem. , vol.99 , pp. 126-132
    • Le Bouffant, R.1    Cormier, P.2    Mulner-Lorillon, O.3    Belle, R.4
  • 21
    • 0036709257 scopus 로고    scopus 로고
    • Physiological and induced apoptosis in sea urchin larvae undergoing metamorphosis
    • Roccheri M.C., Tipa C., Bonaventura R., and Matranga V. Physiological and induced apoptosis in sea urchin larvae undergoing metamorphosis. Int. J. Dev. Biol. 46 (2002) 801-806
    • (2002) Int. J. Dev. Biol. , vol.46 , pp. 801-806
    • Roccheri, M.C.1    Tipa, C.2    Bonaventura, R.3    Matranga, V.4
  • 22
    • 0035149528 scopus 로고    scopus 로고
    • Apoptosis in sea urchin oocytes, eggs, and early embryos
    • Voronina E., and Wessel G.M. Apoptosis in sea urchin oocytes, eggs, and early embryos. Mol. Reprod. Dev. 60 (2001) 553-561
    • (2001) Mol. Reprod. Dev. , vol.60 , pp. 553-561
    • Voronina, E.1    Wessel, G.M.2
  • 23
    • 33846910826 scopus 로고    scopus 로고
    • Apoptosis in early development of the sea urchin, Strongylocentrotus purpuratus
    • Vega Thurber R., and Epel D. Apoptosis in early development of the sea urchin, Strongylocentrotus purpuratus. Dev. Biol 303 (2007) 336-346
    • (2007) Dev. Biol , vol.303 , pp. 336-346
    • Vega Thurber, R.1    Epel, D.2
  • 24
    • 34447133623 scopus 로고    scopus 로고
    • Sea urchin embryo as a model for analysis of the signaling pathways linking DNA damage checkpoint, DNA repair and apoptosis
    • Le Bouffant R., Cormier P., Cueff A., Belle R., and Mulner-Lorillon O. Sea urchin embryo as a model for analysis of the signaling pathways linking DNA damage checkpoint, DNA repair and apoptosis. Cell Mol. Life Sci. 64 (2007) 1723-1734
    • (2007) Cell Mol. Life Sci. , vol.64 , pp. 1723-1734
    • Le Bouffant, R.1    Cormier, P.2    Cueff, A.3    Belle, R.4    Mulner-Lorillon, O.5
  • 26
    • 0242288828 scopus 로고    scopus 로고
    • Sea urchin elongation factor 1delta (EF1delta) and evidence for cell cycle-directed localization changes of a sub-fraction of the protein at M phase
    • Boulben S., Monnier A., Le Breton M., Morales J., Cormier P., Belle R., and Mulner-Lorillon O. Sea urchin elongation factor 1delta (EF1delta) and evidence for cell cycle-directed localization changes of a sub-fraction of the protein at M phase. Cell Mol. Life Sci 60 (2003) 2178-2188
    • (2003) Cell Mol. Life Sci , vol.60 , pp. 2178-2188
    • Boulben, S.1    Monnier, A.2    Le Breton, M.3    Morales, J.4    Cormier, P.5    Belle, R.6    Mulner-Lorillon, O.7
  • 27
    • 12344305214 scopus 로고    scopus 로고
    • eIF2 and the control of cell physiology
    • Proud C.G. eIF2 and the control of cell physiology. Semin Cell Dev. Biol. 16 (2005) 3-12
    • (2005) Semin Cell Dev. Biol. , vol.16 , pp. 3-12
    • Proud, C.G.1
  • 29
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • Hoeijmakers J.H. Genome maintenance mechanisms for preventing cancer. Nature 411 (2001) 366-374
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.1
  • 31
    • 85029425967 scopus 로고    scopus 로고
    • Le Bouffant, R., Mulner-Lorillon, O., Morales, J., Cormier, P., and Belle, R. Chromium(III) triggers the DNA-damaged checkpoint of the cell cycle and induces a functional increase of 4E-BP. Chem. Res. Toxicol. (in press).
    • Le Bouffant, R., Mulner-Lorillon, O., Morales, J., Cormier, P., and Belle, R. Chromium(III) triggers the DNA-damaged checkpoint of the cell cycle and induces a functional increase of 4E-BP. Chem. Res. Toxicol. (in press).
  • 32
    • 39649088786 scopus 로고    scopus 로고
    • Effects of protein phosphorylation on ubiquitination and stability of the translational inhibitor protein 4E-BP1
    • Elia A., Constantinou C., and Clemens M.J. Effects of protein phosphorylation on ubiquitination and stability of the translational inhibitor protein 4E-BP1. Oncogene (2007)
    • (2007) Oncogene
    • Elia, A.1    Constantinou, C.2    Clemens, M.J.3
  • 33
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., and Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419 (2002) 135-141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 34
    • 32544446451 scopus 로고    scopus 로고
    • Coping with stress: eIF2 kinases and translational control
    • Wek R.C., Jiang H.Y., and Anthony T.G. Coping with stress: eIF2 kinases and translational control. Biochem. Soc. Trans 34 (2006) 7-11
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 7-11
    • Wek, R.C.1    Jiang, H.Y.2    Anthony, T.G.3
  • 35
    • 33748753172 scopus 로고    scopus 로고
    • Nck in a complex containing the catalytic subunit of protein phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling and cell survival to endoplasmic reticulum stress
    • Latreille M., and Larose L. Nck in a complex containing the catalytic subunit of protein phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling and cell survival to endoplasmic reticulum stress. J. Biol. Chem 281 (2006) 26633-26644
    • (2006) J. Biol. Chem , vol.281 , pp. 26633-26644
    • Latreille, M.1    Larose, L.2
  • 36
    • 33751531587 scopus 로고    scopus 로고
    • Protein tyrosine and serine-threonine phosphatases in the sea urchin, Strongylocentrotus purpuratus: identification and potential functions
    • Byrum C.A., Walton K.D., Robertson A.J., Carbonneau S., Thomason R.T., Coffman J.A., and McClay D.R. Protein tyrosine and serine-threonine phosphatases in the sea urchin, Strongylocentrotus purpuratus: identification and potential functions. Dev. Biol 300 (2006) 194-218
    • (2006) Dev. Biol , vol.300 , pp. 194-218
    • Byrum, C.A.1    Walton, K.D.2    Robertson, A.J.3    Carbonneau, S.4    Thomason, R.T.5    Coffman, J.A.6    McClay, D.R.7
  • 37
    • 0026350892 scopus 로고
    • Increase in eukaryotic initiation factor 2B activity following fertilization reflects changes in redox potential
    • Akkaraju G.R., Hansen L.J., and Jagus R. Increase in eukaryotic initiation factor 2B activity following fertilization reflects changes in redox potential. J. Biol. Chem 266 (1991) 24451-24459
    • (1991) J. Biol. Chem , vol.266 , pp. 24451-24459
    • Akkaraju, G.R.1    Hansen, L.J.2    Jagus, R.3
  • 38
    • 0025001738 scopus 로고
    • Purification and characterization of sea urchin initiation factor 2. The requirement of guanine nucleotide exchange factor for the release of eukaryotic polypeptide chain initiation factor 2-bound GDP
    • Dholakia J.N., Xu Z., Hille M.B., and Wahba A.J. Purification and characterization of sea urchin initiation factor 2. The requirement of guanine nucleotide exchange factor for the release of eukaryotic polypeptide chain initiation factor 2-bound GDP. J. Biol. Chem 265 (1990) 19319-19323
    • (1990) J. Biol. Chem , vol.265 , pp. 19319-19323
    • Dholakia, J.N.1    Xu, Z.2    Hille, M.B.3    Wahba, A.J.4
  • 39
    • 0033016770 scopus 로고    scopus 로고
    • Caspase-3 is necessary and sufficient for cleavage of protein synthesis eukaryotic initiation factor 4G during apoptosis
    • Bushell M., McKendrick L., Janicke R.U., Clemens M.J., and Morley S.J. Caspase-3 is necessary and sufficient for cleavage of protein synthesis eukaryotic initiation factor 4G during apoptosis. FEBS Lett 451 (1999) 332-336
    • (1999) FEBS Lett , vol.451 , pp. 332-336
    • Bushell, M.1    McKendrick, L.2    Janicke, R.U.3    Clemens, M.J.4    Morley, S.J.5
  • 41
    • 0035902916 scopus 로고    scopus 로고
    • Proteasome inhibitors and immunosuppressive drugs promote the cleavage of eIF4GI and eIF4GII by caspase-8-independent mechanisms in Jurkat T cell lines
    • Morley S.J., and Pain V.M. Proteasome inhibitors and immunosuppressive drugs promote the cleavage of eIF4GI and eIF4GII by caspase-8-independent mechanisms in Jurkat T cell lines. FEBS Lett 503 (2001) 206-212
    • (2001) FEBS Lett , vol.503 , pp. 206-212
    • Morley, S.J.1    Pain, V.M.2
  • 42
    • 1442326151 scopus 로고    scopus 로고
    • Degradation of poly(A)-binding protein in apoptotic cells and linkage to translation regulation
    • Marissen W.E., Triyoso D., Younan P., and Lloyd R.E. Degradation of poly(A)-binding protein in apoptotic cells and linkage to translation regulation. Apoptosis 9 (2004) 67-75
    • (2004) Apoptosis , vol.9 , pp. 67-75
    • Marissen, W.E.1    Triyoso, D.2    Younan, P.3    Lloyd, R.E.4
  • 43
    • 34648857572 scopus 로고    scopus 로고
    • Translation regulation after taxol treatment in NIH3T3 cells involves the elongation factor (eEF)2
    • Pineiro D., Gonzalez V.M., Hernandez-Jimenez M., Salinas M., and Martin M.E. Translation regulation after taxol treatment in NIH3T3 cells involves the elongation factor (eEF)2. Exp. Cell Res 313 (2007) 3694-3706
    • (2007) Exp. Cell Res , vol.313 , pp. 3694-3706
    • Pineiro, D.1    Gonzalez, V.M.2    Hernandez-Jimenez, M.3    Salinas, M.4    Martin, M.E.5
  • 44
    • 34249886604 scopus 로고    scopus 로고
    • Translational control of development
    • Mathews M.B., Sonenberg N., and Hershey J.W. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Thompson B., Wickens M., and Kimble J. Translational control of development. In: Mathews M.B., Sonenberg N., and Hershey J.W. (Eds). In "Translational control in Biology and Medicine" (2007), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • (2007) In "Translational control in Biology and Medicine"
    • Thompson, B.1    Wickens, M.2    Kimble, J.3


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