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Volumn 350, Issue 2, 2011, Pages 476-483

Identification of a new isoform of eEF2 whose phosphorylation is required for completion of cell division in sea urchin embryos

Author keywords

Cell cycle; EEF2 isoforms; Phosphorylated eEF2; Protein translation; Sea urchin embryo

Indexed keywords

ELONGATION FACTOR 2; ISOPROTEIN;

EID: 79151475068     PISSN: 00121606     EISSN: 1095564X     Source Type: Journal    
DOI: 10.1016/j.ydbio.2010.12.015     Document Type: Article
Times cited : (9)

References (45)
  • 1
    • 0142219876 scopus 로고    scopus 로고
    • Identification and characterization of an inhibitor of eukaryotic elongation factor 2 kinase against human cancer cell lines
    • Arora S., Yang J.M., Kinzy T.G., Utsumi R., Okamoto T., Kitayama T., Ortiz P.A., Hait W.N. Identification and characterization of an inhibitor of eukaryotic elongation factor 2 kinase against human cancer cell lines. Cancer Res. 2003, 63:6894-6899.
    • (2003) Cancer Res. , vol.63 , pp. 6894-6899
    • Arora, S.1    Yang, J.M.2    Kinzy, T.G.3    Utsumi, R.4    Okamoto, T.5    Kitayama, T.6    Ortiz, P.A.7    Hait, W.N.8
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0018406891 scopus 로고
    • Elevation of protein synthesis is a complex response to fertilisation
    • Brandis J.W., Raff R.A. Elevation of protein synthesis is a complex response to fertilisation. Nature 1979, 278:467-469.
    • (1979) Nature , vol.278 , pp. 467-469
    • Brandis, J.W.1    Raff, R.A.2
  • 4
    • 0036438894 scopus 로고    scopus 로고
    • Regulation of peptide-chain elongation in mammalian cells
    • Browne G.J., Proud C.G. Regulation of peptide-chain elongation in mammalian cells. Eur. J. Biochem. 2002, 269:5360-5368.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5360-5368
    • Browne, G.J.1    Proud, C.G.2
  • 5
    • 0025358704 scopus 로고
    • Increased phosphorylation of elongation factor 2 during mitosis in transformed human amnion cells correlates with a decreased rate of protein synthesis
    • Celis J.E., Madsen P., Ryazanov A.G. Increased phosphorylation of elongation factor 2 during mitosis in transformed human amnion cells correlates with a decreased rate of protein synthesis. Proc. Natl Acad. Sci. USA 1990, 87:4231-4235.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4231-4235
    • Celis, J.E.1    Madsen, P.2    Ryazanov, A.G.3
  • 7
    • 36649031282 scopus 로고    scopus 로고
    • The eIF2alfa kinases
    • CSH Laboratory Press, New York, M.B. Mathews, N. Sonenberg, J.W.B. Hershey (Eds.)
    • Dever T.E., Dar A.C., Sicheri F. The eIF2alfa kinases. Translational control in biology and medicine 2007, 369-400. CSH Laboratory Press, New York. M.B. Mathews, N. Sonenberg, J.W.B. Hershey (Eds.).
    • (2007) Translational control in biology and medicine , pp. 369-400
    • Dever, T.E.1    Dar, A.C.2    Sicheri, F.3
  • 9
    • 0025099432 scopus 로고
    • The initiation of development at fertilization
    • Epel D. The initiation of development at fertilization. Cell Differ. Dev. 1990, 29:1-12.
    • (1990) Cell Differ. Dev. , vol.29 , pp. 1-12
    • Epel, D.1
  • 12
    • 34247163315 scopus 로고    scopus 로고
    • Regulation of translation elongation and the cotranslational protein targeting pathway
    • CSH Laboratory Press, New York, M.B. Mathews, N. Sonenberg, J.W.B. Hershey (Eds.)
    • Herbert T.P., Proud C.G. Regulation of translation elongation and the cotranslational protein targeting pathway. Translational control in biology and medicine 2007, 601-624. CSH Laboratory Press, New York. M.B. Mathews, N. Sonenberg, J.W.B. Hershey (Eds.).
    • (2007) Translational control in biology and medicine , pp. 601-624
    • Herbert, T.P.1    Proud, C.G.2
  • 13
    • 0018377032 scopus 로고
    • Efficiency of protein synthesis after fertilisation of sea urchin eggs
    • Hille M.B., Albers A.A. Efficiency of protein synthesis after fertilisation of sea urchin eggs. Nature 1979, 278:469-471.
    • (1979) Nature , vol.278 , pp. 469-471
    • Hille, M.B.1    Albers, A.A.2
  • 14
    • 0015134638 scopus 로고
    • Measurements of messenger RNA entering polysomes upon fertilization of sea urchin eggs
    • Humphreys T. Measurements of messenger RNA entering polysomes upon fertilization of sea urchin eggs. Dev. Biol. 1971, 26:201-208.
    • (1971) Dev. Biol. , vol.26 , pp. 201-208
    • Humphreys, T.1
  • 15
    • 0034573770 scopus 로고    scopus 로고
    • Changes in the activities of protein phosphatase type 1 and type 2A in sea urchin embryos during early development
    • Kawamoto M., Fujiwara A., Kuno S., Yasumasu I. Changes in the activities of protein phosphatase type 1 and type 2A in sea urchin embryos during early development. Zygote 2000, 8(Suppl 1):S68-S69.
    • (2000) Zygote , vol.8 , Issue.SUPPL 1
    • Kawamoto, M.1    Fujiwara, A.2    Kuno, S.3    Yasumasu, I.4
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 39649116675 scopus 로고    scopus 로고
    • Inhibition of translation and modification of translation factors during apoptosis induced by the DNA-damaging agent MMS in sea urchin embryos
    • Le Bouffant R., Boulben S., Cormier P., Mulner-Lorillon O., Belle R., Morales J. Inhibition of translation and modification of translation factors during apoptosis induced by the DNA-damaging agent MMS in sea urchin embryos. Exp. Cell Res. 2008, 314:961-968.
    • (2008) Exp. Cell Res. , vol.314 , pp. 961-968
    • Le Bouffant, R.1    Boulben, S.2    Cormier, P.3    Mulner-Lorillon, O.4    Belle, R.5    Morales, J.6
  • 19
    • 36348996412 scopus 로고    scopus 로고
    • Origins and principles of translational control
    • CSH Laboratory Press, New York, M.B. Mathews, N. Sonenberg, J.W.B. Hershey (Eds.)
    • Mathews M.B., Sonenberg N., Hershey J.W.B. Origins and principles of translational control. Translational control in biology and medicine 2007, 369-400. CSH Laboratory Press, New York. M.B. Mathews, N. Sonenberg, J.W.B. Hershey (Eds.).
    • (2007) Translational control in biology and medicine , pp. 369-400
    • Mathews, M.B.1    Sonenberg, N.2    Hershey, J.W.B.3
  • 20
    • 0002024553 scopus 로고    scopus 로고
    • The protein biosynthesis elongation cycle
    • CSHL Press, New York, N. Sonenberg, J. Hershey, M. Mathews (Eds.)
    • Merrick W.C., Nyborg J. The protein biosynthesis elongation cycle. Translational control of gene expression 2000, 89-125. CSHL Press, New York. N. Sonenberg, J. Hershey, M. Mathews (Eds.).
    • (2000) Translational control of gene expression , pp. 89-125
    • Merrick, W.C.1    Nyborg, J.2
  • 21
    • 0035431399 scopus 로고    scopus 로고
    • Protein translation during early cell divisions of sea urchin embryos regulated at the level of polypeptide chain elongation and highly sensitive to natural polyamines
    • Monnier A., Morales J., Cormier P., Boulben S., Belle R., Mulner-Lorillon O. Protein translation during early cell divisions of sea urchin embryos regulated at the level of polypeptide chain elongation and highly sensitive to natural polyamines. Zygote 2001, 9:229-236.
    • (2001) Zygote , vol.9 , pp. 229-236
    • Monnier, A.1    Morales, J.2    Cormier, P.3    Boulben, S.4    Belle, R.5    Mulner-Lorillon, O.6
  • 24
    • 0023522187 scopus 로고
    • Identification of the major Mr 100, 000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2
    • Nairn A.C., Palfrey H.C. Identification of the major Mr 100, 000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2. J. Biol. Chem. 1987, 262:17299-17303.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17299-17303
    • Nairn, A.C.1    Palfrey, H.C.2
  • 25
    • 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., Morales J. After fertilization of sea urchin eggs, eIF4G is post-translationally modified and associated with the cap-binding protein eIF4E. J. Cell Sci. 2007, 120:425-434.
    • (2007) J. Cell Sci. , vol.120 , pp. 425-434
    • Oulhen, N.1    Salaun, P.2    Cosson, B.3    Cormier, P.4    Morales, J.5
  • 26
    • 73449095458 scopus 로고    scopus 로고
    • EIF4E-binding proteins are differentially modified after ammonia versus intracellular calcium activation of sea urchin unfertilized eggs
    • Oulhen N., Mulner-Lorillon O., Cormier P. eIF4E-binding proteins are differentially modified after ammonia versus intracellular calcium activation of sea urchin unfertilized eggs. Mol. Reprod. Dev. 2010, 77:83-91.
    • (2010) Mol. Reprod. Dev. , vol.77 , pp. 83-91
    • Oulhen, N.1    Mulner-Lorillon, O.2    Cormier, P.3
  • 27
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin D.J., Hojrup P., Bleasby A.J. Rapid identification of proteins by peptide-mass fingerprinting. Curr. Biol. 1993, 3:327-332.
    • (1993) Curr. Biol. , vol.3 , pp. 327-332
    • Pappin, D.J.1    Hojrup, P.2    Bleasby, A.J.3
  • 28
    • 34548059203 scopus 로고    scopus 로고
    • Flipping the switch: how a sperm activates the egg at fertilization
    • Parrington J., Davis L.C., Galione A., Wessel G. Flipping the switch: how a sperm activates the egg at fertilization. Dev. Dyn. 2007, 236:2027-2038.
    • (2007) Dev. Dyn. , vol.236 , pp. 2027-2038
    • Parrington, J.1    Davis, L.C.2    Galione, A.3    Wessel, G.4
  • 29
    • 34247118887 scopus 로고    scopus 로고
    • Signalling to translation: how signal transduction pathways control the protein synthetic machinery
    • Proud C.G. Signalling to translation: how signal transduction pathways control the protein synthetic machinery. Biochem. J. 2007, 403:217-234.
    • (2007) Biochem. J. , vol.403 , pp. 217-234
    • Proud, C.G.1
  • 30
  • 31
    • 0024454195 scopus 로고
    • The tumour promoter okadaic acid inhibits reticulocyte-lysate protein synthesis by increasing the net phosphorylation of elongation factor 2
    • Redpath N.T., Proud C.G. The tumour promoter okadaic acid inhibits reticulocyte-lysate protein synthesis by increasing the net phosphorylation of elongation factor 2. Biochem. J. 1989, 262:69-75.
    • (1989) Biochem. J. , vol.262 , pp. 69-75
    • Redpath, N.T.1    Proud, C.G.2
  • 32
    • 0025224185 scopus 로고
    • Phosphorylation of elongation factor 2: a key mechanism regulating gene expression in vertebrates
    • Ryazanov A.G., Spirin A.S. Phosphorylation of elongation factor 2: a key mechanism regulating gene expression in vertebrates. New Biol. 1990, 2:843-850.
    • (1990) New Biol. , vol.2 , pp. 843-850
    • Ryazanov, A.G.1    Spirin, A.S.2
  • 33
    • 0025733261 scopus 로고
    • Regulation of protein synthesis at the elongation stage. New insights into the control of gene expression in eukaryotes
    • Ryazanov A.G., Rudkin B.B., Spirin A.S. Regulation of protein synthesis at the elongation stage. New insights into the control of gene expression in eukaryotes. FEBS Lett. 1991, 285:170-175.
    • (1991) FEBS Lett. , vol.285 , pp. 170-175
    • Ryazanov, A.G.1    Rudkin, B.B.2    Spirin, A.S.3
  • 35
    • 2442618913 scopus 로고    scopus 로고
    • Signal transduction pathways that contribute to CDK1/cyclin B activation during the first mitotic division in sea urchin embryos
    • Salaun P., Le Breton M., Morales J., Belle R., Boulben S., Mulner-Lorillon O., Cormier P. Signal transduction pathways that contribute to CDK1/cyclin B activation during the first mitotic division in sea urchin embryos. Exp. Cell Res. 2004, 296:347-357.
    • (2004) Exp. Cell Res. , vol.296 , pp. 347-357
    • Salaun, P.1    Le Breton, M.2    Morales, J.3    Belle, R.4    Boulben, S.5    Mulner-Lorillon, O.6    Cormier, P.7
  • 36
    • 17844395474 scopus 로고    scopus 로고
    • Embryonic-stage-dependent changes in the level of eIF4E-binding proteins during early development of sea urchin embryos
    • Salaun P., Boulben S., Mulner-Lorillon O., Belle R., Sonenberg N., Morales J., Cormier P. Embryonic-stage-dependent changes in the level of eIF4E-binding proteins during early development of sea urchin embryos. J. Cell Sci. 2005, 118:1385-1394.
    • (2005) J. Cell Sci. , vol.118 , pp. 1385-1394
    • Salaun, P.1    Boulben, S.2    Mulner-Lorillon, O.3    Belle, R.4    Sonenberg, N.5    Morales, J.6    Cormier, P.7
  • 37
    • 42049083539 scopus 로고    scopus 로고
    • Regulation of mRNA translation during cellular division
    • Sivan G., Elroy-Stein O. Regulation of mRNA translation during cellular division. Cell Cycle 2008, 7:741-744.
    • (2008) Cell Cycle , vol.7 , pp. 741-744
    • Sivan, G.1    Elroy-Stein, O.2
  • 38
    • 34748870653 scopus 로고    scopus 로고
    • Ribosomal slowdown mediates translational arrest during cellular division
    • Sivan G., Kedersha N., Elroy-Stein O. Ribosomal slowdown mediates translational arrest during cellular division. Mol. Cell. Biol. 2007, 27:6639-6646.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6639-6646
    • Sivan, G.1    Kedersha, N.2    Elroy-Stein, O.3
  • 39
    • 41949107421 scopus 로고    scopus 로고
    • Cdc2-cyclin B regulates eEF2 kinase activity in a cell cycle- and amino acid-dependent manner
    • Smith E.M., Proud C.G. cdc2-cyclin B regulates eEF2 kinase activity in a cell cycle- and amino acid-dependent manner. EMBO J. 2008, 27:1005-1016.
    • (2008) EMBO J. , vol.27 , pp. 1005-1016
    • Smith, E.M.1    Proud, C.G.2
  • 40
    • 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
  • 41
    • 34547683444 scopus 로고    scopus 로고
    • Postsynaptic decoding of neural activity: eEF2 as a biochemical sensor coupling miniature synaptic transmission to local protein synthesis
    • Sutton M.A., Taylor A.M., Ito H.T., Pham A., Schuman E.M. Postsynaptic decoding of neural activity: eEF2 as a biochemical sensor coupling miniature synaptic transmission to local protein synthesis. Neuron 2007, 55:648-661.
    • (2007) Neuron , vol.55 , pp. 648-661
    • Sutton, M.A.1    Taylor, A.M.2    Ito, H.T.3    Pham, A.4    Schuman, E.M.5
  • 42
    • 0022450047 scopus 로고
    • Translational control of gene expression in a normal fibroblast. Characterization of a subclass of mRNAs with unusual kinetic properties
    • Walden W.E., Thach R.E. Translational control of gene expression in a normal fibroblast. Characterization of a subclass of mRNAs with unusual kinetic properties. Biochemistry 1986, 25:2033-2041.
    • (1986) Biochemistry , vol.25 , pp. 2033-2041
    • Walden, W.E.1    Thach, R.E.2
  • 44
    • 38349133609 scopus 로고    scopus 로고
    • '... The end of the beginning': cdk1 thresholds and exit from mitosis
    • Wolf F., Sigl R., Geley S. '... The end of the beginning': cdk1 thresholds and exit from mitosis. Cell Cycle 2007, 6:1408-1411.
    • (2007) Cell Cycle , vol.6 , pp. 1408-1411
    • Wolf, F.1    Sigl, R.2    Geley, S.3
  • 45
    • 0027375364 scopus 로고
    • Peptide mass maps: a highly informative approach to protein identification
    • Yates J.R., Speicher S., Griffin P.R., Hunkapiller T. Peptide mass maps: a highly informative approach to protein identification. Anal. Biochem. 1993, 214:397-408.
    • (1993) Anal. Biochem. , vol.214 , pp. 397-408
    • Yates, J.R.1    Speicher, S.2    Griffin, P.R.3    Hunkapiller, T.4


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