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Volumn 6, Issue , 2015, Pages

Temporal and spatial regulation of translation in the mammalian oocyte via the mTOR-eIF4F pathway

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 4F; LAMIN; MAMMALIAN TARGET OF RAPAMYCIN; CAPPED RNA; MESSENGER RNA; TARGET OF RAPAMYCIN KINASE;

EID: 84952984421     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7078     Document Type: Article
Times cited : (75)

References (83)
  • 1
    • 0029030104 scopus 로고
    • Translational regulation in development
    • Curtis, D., Lehmann, R. & Zamore, P. D. Translational regulation in development. Cell 81, 171-178 (1995).
    • (1995) Cell , vol.81 , pp. 171-178
    • Curtis, D.1    Lehmann, R.2    Zamore, P.D.3
  • 2
    • 0015526499 scopus 로고
    • Oogenetic origin of messenger RNA for embryonic synthesis of microtubule proteins
    • Raff, R. A., Colot, H. V., Selvig, S. E. & Gross, P. R. Oogenetic origin of messenger RNA for embryonic synthesis of microtubule proteins. Nature 235, 211-214 (1972).
    • (1972) Nature , vol.235 , pp. 211-214
    • Raff, R.A.1    Colot, H.V.2    Selvig, S.E.3    Gross, P.R.4
  • 3
    • 0018651727 scopus 로고
    • Origin and spatial distribution of maternal messenger RNA during oogenesis of an insect, Oncopeltus fasciatus
    • Capco, D. G. & Jeffery, W. R. Origin and spatial distribution of maternal messenger RNA during oogenesis of an insect, Oncopeltus fasciatus. J. Cell Sci. 39, 63-76 (1979).
    • (1979) J. Cell Sci. , vol.39 , pp. 63-76
    • Capco, D.G.1    Jeffery, W.R.2
  • 4
    • 14244260422 scopus 로고    scopus 로고
    • Major chromatin remodeling in the germinal vesicle (GV) of mammalian oocytes is dispensable for global transcriptional silencing but required for centromeric heterochromatin function
    • De La Fuente, R. et al. Major chromatin remodeling in the germinal vesicle (GV) of mammalian oocytes is dispensable for global transcriptional silencing but required for centromeric heterochromatin function. Dev. Biol. 275, 447-458 (2004).
    • (2004) Dev. Biol. , vol.275 , pp. 447-458
    • De La Fuente, R.1
  • 5
    • 0022163043 scopus 로고
    • Informational content of the echinoderm egg
    • Brandhorst, B. P. Informational content of the echinoderm egg. Dev. Biol. (NY) 1, 525-576 (1985).
    • (1985) Dev. Biol. (NY) , vol.1 , pp. 525-576
    • Brandhorst, B.P.1
  • 6
    • 0029081376 scopus 로고
    • Regulation of gene expression at the beginning of mammalian development
    • Nothias, J. Y., Majumder, S., Kaneko, K. J. & DePamphilis, M. L. Regulation of gene expression at the beginning of mammalian development. J. Biol. Chem. 270, 22077-22080 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 22077-22080
    • Nothias, J.Y.1    Majumder, S.2    Kaneko, K.J.3    DePamphilis, M.L.4
  • 7
    • 34547611878 scopus 로고    scopus 로고
    • Self-organization of MTOCs replaces centrosome function during acentrosomal spindle assembly in live mouse oocytes
    • Schuh, M. & Ellenberg, J. Self-organization of MTOCs replaces centrosome function during acentrosomal spindle assembly in live mouse oocytes. Cell 130, 484-498 (2007).
    • (2007) Cell , vol.130 , pp. 484-498
    • Schuh, M.1    Ellenberg, J.2
  • 8
  • 9
    • 13544277618 scopus 로고    scopus 로고
    • Putting RNAs in the right place at the right time: RNA localization in the frog oocyte
    • King, M. L., Messitt, T. J. & Mowry, K. L. Putting RNAs in the right place at the right time: RNA localization in the frog oocyte. Biol. Cell 97, 19-33 (2005).
    • (2005) Biol. Cell , vol.97 , pp. 19-33
    • King, M.L.1    Messitt, T.J.2    Mowry, K.L.3
  • 10
    • 70849088746 scopus 로고    scopus 로고
    • Subcellular mRNA localization in animal cells and why it matters
    • Holt, C. E. & Bullock, S. L. Subcellular mRNA localization in animal cells and why it matters. Science 326, 1212-1216 (2009).
    • (2009) Science , vol.326 , pp. 1212-1216
    • Holt, C.E.1    Bullock, S.L.2
  • 11
    • 0031907522 scopus 로고    scopus 로고
    • Localization of mRNAs to the oocyte is common in Drosophila ovaries
    • Dubowy, J. & Macdonald, P. M. Localization of mRNAs to the oocyte is common in Drosophila ovaries. Mech. Dev. 70, 193-195 (2013).
    • (2013) Mech. Dev. , vol.70 , pp. 193-195
    • Dubowy, J.1    Macdonald, P.M.2
  • 12
    • 0022369196 scopus 로고
    • Inductive interactions in early amphibian development and their general nature
    • Nieuwkoop, P. D. Inductive interactions in early amphibian development and their general nature. J. Embryol. Exp. Morphol. 89, 333-347 (1985).
    • (1985) J. Embryol. Exp. Morphol. , vol.89 , pp. 333-347
    • Nieuwkoop, P.D.1
  • 13
    • 51449104730 scopus 로고    scopus 로고
    • A subcortical maternal complex essential for preimplantation mouse embryogenesis
    • Li, L., Baibakov, B. & Dean, J. A subcortical maternal complex essential for preimplantation mouse embryogenesis. Dev. Cell 15, 416-425 (2008).
    • (2008) Dev. Cell , vol.15 , pp. 416-425
    • Li, L.1    Baibakov, B.2    Dean, J.3
  • 14
    • 75749150366 scopus 로고    scopus 로고
    • P-body loss is concomitant with formation of a messenger RNA storage domain in mouse oocytes
    • Flemr, M., Ma, J., Schultz, R. M. & Svoboda, P. P-body loss is concomitant with formation of a messenger RNA storage domain in mouse oocytes. Biol. Reprod. 82, 1008-1017 (2010).
    • (2010) Biol. Reprod. , vol.82 , pp. 1008-1017
    • Flemr, M.1    Ma, J.2    Schultz, R.M.3    Svoboda, P.4
  • 15
    • 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. & 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, 4990-4997 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 16
    • 0029030440 scopus 로고
    • Phosphorylation of eukaryotic protein synthesis initiation factor 4E at Ser-209
    • Joshi, B. et al. Phosphorylation of eukaryotic protein synthesis initiation factor 4E at Ser-209. J. Biol. Chem. 270, 14597-14603 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 14597-14603
    • Joshi, B.1
  • 17
    • 0027969060 scopus 로고
    • Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form
    • Minich, W. B., Balasta, M. L., Goss, D. J. & Rhoads, R. E. Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: increased cap affinity of the phosphorylated form. Proc. Natl Acad. Sci. USA 91, 7668-7672 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7668-7672
    • Minich, W.B.1    Balasta, M.L.2    Goss, D.J.3    Rhoads, R.E.4
  • 18
    • 0036438924 scopus 로고    scopus 로고
    • Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation? Eur
    • Scheper, G. C. & Proud, C. G. Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation? Eur. J. Biochem. 269, 5350-5359 (2002).
    • (2002) J. Biochem. , vol.269 , pp. 5350-5359
    • Scheper, G.C.1    Proud, C.G.2
  • 19
    • 0033153166 scopus 로고    scopus 로고
    • Regulation of 4E-BP1 phosphorylation: A novel two-step mechanism
    • Gingras, A. C. et al. Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism. Genes Dev. 13, 1422-1437 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1422-1437
    • Gingras, A.C.1
  • 20
    • 84882291342 scopus 로고    scopus 로고
    • Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity
    • Feoktistova, K. et al. Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity. Proc. Natl Acad. Sci. USA 110, 13339-13344 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 13339-13344
    • Feoktistova, K.1
  • 21
    • 0026723117 scopus 로고
    • MRNAs containing extensive secondary structure in their 50 non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E
    • Koromilas, A. E., Lazaris-Karatzas, A. & Sonenberg, N. mRNAs containing extensive secondary structure in their 50 non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E. Embo. J. 11, 4153-4158 (1992).
    • (1992) Embo. J. , vol.11 , pp. 4153-4158
    • Koromilas, A.E.1    Lazaris-Karatzas, A.2    Sonenberg, N.3
  • 22
    • 7944235758 scopus 로고    scopus 로고
    • Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
    • Jacinto, E. et al. Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat. Cell Biol. 6, 1122-1128 (2004).
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1122-1128
    • Jacinto, E.1
  • 23
    • 0035806992 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of the translational repressor eIF-4E binding protein-1 (4E-BP1)
    • Heesom, K. J., Gampel, A., Mellor, H. & Denton, R. M. Cell cycle-dependent phosphorylation of the translational repressor eIF-4E binding protein-1 (4E-BP1). Curr. Biol. 11, 1374-1379 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1374-1379
    • Heesom, K.J.1    Gampel, A.2    Mellor, H.3    Denton, R.M.4
  • 24
    • 84866747992 scopus 로고    scopus 로고
    • 4E-BP1 participates in maintaining spindle integrity and genomic stability via interacting with PLK1
    • Shang, Z. F. et al. 4E-BP1 participates in maintaining spindle integrity and genomic stability via interacting with PLK1. Cell Cycle 11, 3463-3471 (2012).
    • (2012) Cell Cycle , vol.11 , pp. 3463-3471
    • Shang, Z.F.1
  • 25
    • 0036240462 scopus 로고    scopus 로고
    • Regulation of translation during in vitro maturation of bovine oocytes: The role of MAP kinase, eIF4E (cap binding protein) phosphorylation, and eIF4E-BP1
    • Tomek, W. et al. Regulation of translation during in vitro maturation of bovine oocytes: the role of MAP kinase, eIF4E (cap binding protein) phosphorylation, and eIF4E-BP1. Biol. Reprod. 66, 1274-1282 (2002).
    • (2002) Biol. Reprod. , vol.66 , pp. 1274-1282
    • Tomek, W.1
  • 26
    • 28744451692 scopus 로고    scopus 로고
    • Suppression of translation during in vitro maturation of pig oocytes despite enhanced formation of cap-binding protein complex eIF4F and 4E-BP1 hyperphosphorylation
    • Ellederova, Z. et al. Suppression of translation during in vitro maturation of pig oocytes despite enhanced formation of cap-binding protein complex eIF4F and 4E-BP1 hyperphosphorylation. Mol. Reprod. Dev. 73, 68-76 (2006).
    • (2006) Mol. Reprod. Dev. , vol.73 , pp. 68-76
    • Ellederova, Z.1
  • 27
    • 84884971558 scopus 로고    scopus 로고
    • Association of maternal mRNA and phosphorylated EIF4EBP1 variants with the spindle in mouse oocytes: Localized translational control supporting female meiosis in mammals
    • Romasko, E. et al. Association of maternal mRNA and phosphorylated EIF4EBP1 variants with the spindle in mouse oocytes: localized translational control supporting female meiosis in mammals. Genetics 195, 349-355 (2013).
    • (2013) Genetics , vol.195 , pp. 349-355
    • Romasko, E.1
  • 28
    • 84860527756 scopus 로고    scopus 로고
    • A unifying model for mTORC1-mediated regulation of mRNA translation
    • Thoreen, C. C. et al. A unifying model for mTORC1-mediated regulation of mRNA translation. Nature 485, 109-113 (2012).
    • (2012) Nature , vol.485 , pp. 109-113
    • Thoreen, C.C.1
  • 29
    • 33846449110 scopus 로고    scopus 로고
    • Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G
    • Moerke, N. J. et al. Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G. Cell 128, 257-267 (2007).
    • (2007) Cell , vol.128 , pp. 257-267
    • Moerke, N.J.1
  • 30
    • 0015463870 scopus 로고
    • Incoporation of amino acids during maturation in vitro by the mouse oocyte: Effect of puromycin on protein synthesis
    • Stern, S., Rayyis, A. & Kennedy, J. F. Incoporation of amino acids during maturation in vitro by the mouse oocyte: effect of puromycin on protein synthesis. Biol. Reprod. 7, 341-346 (1972).
    • (1972) Biol. Reprod. , vol.7 , pp. 341-346
    • Stern, S.1    Rayyis, A.2    Kennedy, J.F.3
  • 31
    • 44349163999 scopus 로고    scopus 로고
    • De-phosphorylation of translation initiation factor 2a (eIF2a) enhances glucose tolerance and attenuates hepato-steatosis in mice
    • Oyadomari, S., Harding, H. P., Zhang, Y., Oyadomari, M. & Ron, D. De-phosphorylation of translation initiation factor 2a (eIF2a) enhances glucose tolerance and attenuates hepato-steatosis in mice. Cell. Metab. 7, 520-532 (2008).
    • (2008) Cell. Metab. , vol.7 , pp. 520-532
    • Oyadomari, S.1    Harding, H.P.2    Zhang, Y.3    Oyadomari, M.4    Ron, D.5
  • 32
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras, A. C., Raught, B. & Sonenberg, N. Regulation of translation initiation by FRAP/mTOR. Genes Dev. 15, 807-826 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 807-826
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 33
    • 46349099804 scopus 로고    scopus 로고
    • Comprehensive detection of human terminal oligopyrimidine (TOP) gene and analysis of their characteristics
    • Yamashita, R. et al. Comprehensive detection of human terminal oligopyrimidine (TOP) gene and analysis of their characteristics. Nucleic Acids Res. 36, 3707-3715 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3707-3715
    • Yamashita, R.1
  • 34
    • 78650239404 scopus 로고    scopus 로고
    • Functions and regulation of the 70 kDa ribosomal S6 kinases
    • Fenton, T. R. & Gout, I. T. Functions and regulation of the 70 kDa ribosomal S6 kinases. Int. J. Biochem. Cell Biol. 43, 47-59 (2011).
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 47-59
    • Fenton, T.R.1    Gout, I.T.2
  • 35
    • 0031982683 scopus 로고    scopus 로고
    • A novel functional human eukaryotic translation initiation factor 4G
    • Gradi, A. et al. A novel functional human eukaryotic translation initiation factor 4G. Mol. Cell Biol. 18, 334-342 (1998).
    • (1998) Mol. Cell Biol. , vol.18 , pp. 334-342
    • Gradi, A.1
  • 36
    • 0034852292 scopus 로고    scopus 로고
    • IRES interaction with translation initiation factors: Functional characterization of novel RNA contacts with eIF3, eIF4B, and eIF4GII
    • López de Quinto, S., Lafuente, E. & Martnez-Salas, E. IRES interaction with translation initiation factors: functional characterization of novel RNA contacts with eIF3, eIF4B, and eIF4GII. RNA 7, 1213-1226 (2001).
    • (2001) RNA , vol.7 , pp. 1213-1226
    • López De Quinto, S.1    Lafuente, E.2    Martnez-Salas, E.3
  • 37
    • 77954095160 scopus 로고    scopus 로고
    • In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons
    • Dieterich, D. C. et al. In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons. Nat. Neurosci. 13, 897-905 (2010).
    • (2010) Nat. Neurosci. , vol.13 , pp. 897-905
    • Dieterich, D.C.1
  • 38
    • 34247140259 scopus 로고    scopus 로고
    • Changes in endoplasmic reticulum structure during mouse oocyte maturation are controlled by the cytoskeleton and cytoplasmic dynein
    • FitzHarris, G., Marangos, P. & Carroll, J. Changes in endoplasmic reticulum structure during mouse oocyte maturation are controlled by the cytoskeleton and cytoplasmic dynein. Dev. Biol. 305, 133-144 (2007).
    • (2007) Dev. Biol. , vol.305 , pp. 133-144
    • FitzHarris, G.1    Marangos, P.2    Carroll, J.3
  • 39
    • 84880659314 scopus 로고    scopus 로고
    • Biased inheritance of mitochondria during asymmetric cell division in the mouse oocyte
    • Dalton, C. M. & Carroll, J. Biased inheritance of mitochondria during asymmetric cell division in the mouse oocyte. J. Cell Sci. 126, 2955-2964 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 2955-2964
    • Dalton, C.M.1    Carroll, J.2
  • 40
    • 84881537115 scopus 로고    scopus 로고
    • REEP3/4 ensure endoplasmic reticulum clearance from metaphase chromatin and proper nuclear envelope architecture
    • Schlaitz, A.-L., Thompson, J., Wong, C. C. L., Yates, 3rd J. R. & Heald, R. REEP3/4 ensure endoplasmic reticulum clearance from metaphase chromatin and proper nuclear envelope architecture. Dev. Cell 26, 315-323 (2013).
    • (2013) Dev. Cell , vol.26 , pp. 315-323
    • Schlaitz, A.-L.1    Thompson, J.2    Wong, C.C.L.3    Yates, J.R.4    Heald, R.5
  • 41
    • 0033429554 scopus 로고    scopus 로고
    • Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and aminoacid deficiency on protein translation
    • Navé, B. T., Ouwens, M., Withers, D. J., Alessi, D. R. & Shepherd, P. R. Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and aminoacid deficiency on protein translation. Biochem. J. 344, 427-431 (1999).
    • (1999) Biochem. J. , vol.344 , pp. 427-431
    • Navé, B.T.1    Ouwens, M.2    Withers, D.J.3    Alessi, D.R.4    Shepherd, P.R.5
  • 42
    • 21844468767 scopus 로고    scopus 로고
    • Phosphorylation of mammalian target of rapamycin (mTOR) at Ser-2448 is mediated by p70S6 kinase
    • Chiang, G. G. & Abraham, R. T. Phosphorylation of mammalian target of rapamycin (mTOR) at Ser-2448 is mediated by p70S6 kinase. J. Biol. Chem. 280, 25485-25490 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 25485-25490
    • Chiang, G.G.1    Abraham, R.T.2
  • 43
    • 0033604521 scopus 로고    scopus 로고
    • Ribosomal S6 kinase signaling and the control of translation
    • Dufner, A. & Thomas, G. Ribosomal S6 kinase signaling and the control of translation. Exp. Cell Res. 253, 100-109 (1999).
    • (1999) Exp. Cell Res. , vol.253 , pp. 100-109
    • Dufner, A.1    Thomas, G.2
  • 44
    • 0004165313 scopus 로고    scopus 로고
    • (eds Sonenberg, N., Hershey, J. W. B. & Mathews, M. B.) Cold Spring Harbor Laboratory Press
    • Hornsten, O. & Meyuhas, E. in Translational Control of Gene Expression (eds Sonenberg, N., Hershey, J. W. B. & Mathews, M. B.) 671-693 (Cold Spring Harbor Laboratory Press, 2000).
    • (2000) Translational Control of Gene Expression , pp. 671-693
    • Hornsten, O.1    Meyuhas, E.2
  • 45
    • 34250755685 scopus 로고    scopus 로고
    • Epigenetic activation of a subset of mRNAs by eIF4E explains its effects on cell proliferation
    • Mamane, Y. et al. Epigenetic activation of a subset of mRNAs by eIF4E explains its effects on cell proliferation. PLoS ONE 2, e242 (2007).
    • (2007) PLoS ONE , vol.2 , pp. e242
    • Mamane, Y.1
  • 47
    • 0036333443 scopus 로고    scopus 로고
    • Rab11 polarization of the Drosophila oocyte: A novel link between membrane trafficking, microtubule organization, and oskar mRNA localization and translation
    • Dollar, G., Struckhoff, E., Michaud, J. & Cohen, R. S. Rab11 polarization of the Drosophila oocyte: a novel link between membrane trafficking, microtubule organization, and oskar mRNA localization and translation. Development 129, 517-526 (2002).
    • (2002) Development , vol.129 , pp. 517-526
    • Dollar, G.1    Struckhoff, E.2    Michaud, J.3    Cohen, R.S.4
  • 48
    • 0038345674 scopus 로고    scopus 로고
    • Bursts of high-frequency stimulation trigger rapid delivery of pre-existing alpha-CaMKII mRNA to synapses: A mechanism in dendritic protein synthesis during longterm potentiation in adult awake rats
    • Havik, B., Rokke, H., Bardsen, K., Davanger, S. & Bramham, C. R. Bursts of high-frequency stimulation trigger rapid delivery of pre-existing alpha-CaMKII mRNA to synapses: a mechanism in dendritic protein synthesis during longterm potentiation in adult awake rats. Eur. J. Neurosci. 17, 2679-2689 (2003).
    • (2003) Eur. J. Neurosci. , vol.17 , pp. 2679-2689
    • Havik, B.1    Rokke, H.2    Bardsen, K.3    Davanger, S.4    Bramham, C.R.5
  • 49
    • 69049087444 scopus 로고    scopus 로고
    • Localization, anchoring and translational control of oskar, gurken, bicoid and nanos mRNA during Drosophila oogenesis
    • Kugler, J. M. & Lasko, P. Localization, anchoring and translational control of oskar, gurken, bicoid and nanos mRNA during Drosophila oogenesis. Fly (Austin) 3, 15-28 (2009).
    • (2009) Fly (Austin) , vol.3 , pp. 15-28
    • Kugler, J.M.1    Lasko, P.2
  • 50
    • 79960040457 scopus 로고    scopus 로고
    • Tiny molecular beacons for in vivo mRNA detection
    • Bratu, D. P., Catrina, I. E. & Marras, S. A. E. Tiny molecular beacons for in vivo mRNA detection. Methods Mol. Biol. 714, 141-157 (2011).
    • (2011) Methods Mol. Biol. , vol.714 , pp. 141-157
    • Bratu, D.P.1    Catrina, I.E.2    Marras, S.A.E.3
  • 51
    • 33847185603 scopus 로고    scopus 로고
    • A screen for nuclear transcripts identifies two linked noncoding RNAs associated with SC35 splicing domains
    • Hutchinson, J. N. et al. A screen for nuclear transcripts identifies two linked noncoding RNAs associated with SC35 splicing domains. BMC Genomics 8, 39 (2007).
    • (2007) BMC Genomics , vol.8 , pp. 39
    • Hutchinson, J.N.1
  • 52
    • 36049047997 scopus 로고    scopus 로고
    • Splicing segregation: The minor spliceosome acts outside the nucleus and controls cell proliferation
    • König, H., Matter, N., Bader, R., Thiele, W. & Müller, F. Splicing segregation: the minor spliceosome acts outside the nucleus and controls cell proliferation. Cell 131, 718-729 (2007).
    • (2007) Cell , vol.131 , pp. 718-729
    • König, H.1    Matter, N.2    Bader, R.3    Thiele, W.4    Müller, F.5
  • 53
    • 0026740963 scopus 로고
    • U2 small nuclear RNA localization and expression during bovine preimplantation development
    • Watson, A. J., Wiemer, K. E., Arcellana-Panlilio, M. & Schultz, G. A. U2 small nuclear RNA localization and expression during bovine preimplantation development. Mol. Reprod. Dev. 31, 231-240 (1992).
    • (1992) Mol. Reprod. Dev. , vol.31 , pp. 231-240
    • Watson, A.J.1    Wiemer, K.E.2    Arcellana-Panlilio, M.3    Schultz, G.A.4
  • 54
    • 0023915764 scopus 로고
    • Regulation of meiotic metaphase by a cytoplasmic maturation-promoting factor during mouse oocyte maturation
    • Hashimoto, N. & Kishimoto, T. Regulation of meiotic metaphase by a cytoplasmic maturation-promoting factor during mouse oocyte maturation. Dev. Biol. 126, 242-252 (1988).
    • (1988) Dev. Biol. , vol.126 , pp. 242-252
    • Hashimoto, N.1    Kishimoto, T.2
  • 55
    • 13444259647 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by eIF4E inhibitory proteins
    • Richter, J. D. & Sonenberg, N. Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature 433, 477-480 (2005).
    • (2005) Nature , vol.433 , pp. 477-480
    • Richter, J.D.1    Sonenberg, N.2
  • 56
    • 2442466927 scopus 로고    scopus 로고
    • Cap-dependent and cap-independent translation in eukaryotic systems
    • Merrick, W. C. Cap-dependent and cap-independent translation in eukaryotic systems. Gene 332, 1-11 (2004).
    • (2004) Gene , vol.332 , pp. 1-11
    • Merrick, W.C.1
  • 57
    • 0034665634 scopus 로고    scopus 로고
    • Bub3 gene disruption in mice reveals essential mitotic spindle checkpoint function during early embryogenesis
    • Kalitsis, P., Earle, E., Fowler, K. J. & Choo, K. H. Bub3 gene disruption in mice reveals essential mitotic spindle checkpoint function during early embryogenesis. Genes Dev. 14, 2277-2282 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 2277-2282
    • Kalitsis, P.1    Earle, E.2    Fowler, K.J.3    Choo, K.H.4
  • 58
    • 44649130105 scopus 로고    scopus 로고
    • P53-Driven apoptosis limits centrosome amplification and genomic instability downstream of NPM1 phosphorylation
    • Cuomo, M. E. et al. p53-Driven apoptosis limits centrosome amplification and genomic instability downstream of NPM1 phosphorylation. Nat. Cell Biol. 10, 723-730 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 723-730
    • Cuomo, M.E.1
  • 59
    • 70449433050 scopus 로고    scopus 로고
    • Bub3 is a spindle assembly checkpoint protein regulating chromosome segregation during mouse oocyte meiosis
    • Li, M. et al. Bub3 is a spindle assembly checkpoint protein regulating chromosome segregation during mouse oocyte meiosis. PLoS ONE 4, e7701 (2009).
    • (2009) PLoS ONE , vol.4 , pp. e7701
    • Li, M.1
  • 60
    • 84897473699 scopus 로고    scopus 로고
    • Cell division: Control of the chromosomal passenger complex in time and space
    • Van der Horst, A. & Lens, S. M. A. Cell division: control of the chromosomal passenger complex in time and space. Chromosoma 123, 25-42 (2013).
    • (2013) Chromosoma , vol.123 , pp. 25-42
    • Van Der Horst, A.1    Lens, S.M.A.2
  • 62
    • 84865339153 scopus 로고    scopus 로고
    • Lack of response to unaligned chromosomes in mammalian female gametes
    • Sebestova, J., Danylevska, A., Novakova, L., Kubelka, M. & Anger, M. Lack of response to unaligned chromosomes in mammalian female gametes. Cell Cycle 11, 3011-3018 (2012).
    • (2012) Cell Cycle , vol.11 , pp. 3011-3018
    • Sebestova, J.1    Danylevska, A.2    Novakova, L.3    Kubelka, M.4    Anger, M.5
  • 63
    • 0020408545 scopus 로고
    • The phosphorylation of ribosomal protein S6 in rat tissues following cycloheximide injection, in diabetes, and after denervation of diaphragm. A simple immunological determination of the extent of S6 phosphorylation on protein blots
    • Nielsen, P. J., Manchester, K. L., Towbin, H., Gordon, J. & Thomas, G. The phosphorylation of ribosomal protein S6 in rat tissues following cycloheximide injection, in diabetes, and after denervation of diaphragm. A simple immunological determination of the extent of S6 phosphorylation on protein blots. J. Biol. Chem. 257, 12316-12321 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 12316-12321
    • Nielsen, P.J.1    Manchester, K.L.2    Towbin, H.3    Gordon, J.4    Thomas, G.5
  • 64
    • 0020123932 scopus 로고
    • Rapid alterations in initiation rate and recruitment of inactive RNA are temporally correlated with S6 phosphorylation
    • Duncan, R. & McConkey, E. H. Rapid alterations in initiation rate and recruitment of inactive RNA are temporally correlated with S6 phosphorylation. Eur. J. Biochem. 123, 539-544 (1982).
    • (1982) Eur. J. Biochem. , vol.123 , pp. 539-544
    • Duncan, R.1    McConkey, E.H.2
  • 65
    • 0030915898 scopus 로고    scopus 로고
    • Rapamycin suppresses 50TOP mRNA translation through inhibition of p70s6k
    • Jefferies, H. B. et al. Rapamycin suppresses 50TOP mRNA translation through inhibition of p70s6k. EMBO J. 16, 3693-3704 (1997).
    • (1997) EMBO J. , vol.16 , pp. 3693-3704
    • Jefferies, H.B.1
  • 66
    • 0032568269 scopus 로고    scopus 로고
    • Translation control: Connecting mitogens and the ribosome
    • Peterson, R. T. & Schreiber, S. L. Translation control: connecting mitogens and the ribosome. Curr. Biol. 8, 248-250 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 248-250
    • Peterson, R.T.1    Schreiber, S.L.2
  • 67
    • 0037844887 scopus 로고    scopus 로고
    • Mitotic regulation of ribosomal S6 kinase 1 involves Ser/Thr, Pro phosphorylation of consensus and non-consensus sites by Cdc2
    • Shah, O. J., Ghosh, S. & Hunter, T. Mitotic regulation of ribosomal S6 kinase 1 involves Ser/Thr, Pro phosphorylation of consensus and non-consensus sites by Cdc2. J. Biol. Chem. 278, 16433-16442 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 16433-16442
    • Shah, O.J.1    Ghosh, S.2    Hunter, T.3
  • 68
    • 84880709668 scopus 로고    scopus 로고
    • MTORC1 phosphorylation sites encode their sensitivity to starvation and rapamycin
    • Kang, S. A. et al. mTORC1 phosphorylation sites encode their sensitivity to starvation and rapamycin. Science 341, 1236566 (2013).
    • (2013) Science , vol.341 , pp. 1236566
    • Kang, S.A.1
  • 69
    • 77954618863 scopus 로고    scopus 로고
    • Redistribution of mitochondria leads to bursts of ATP production during spontaneous mouse oocyte maturation
    • Yu, Y., Dumollard, R., Rossbach, A., Lai, F. A. & Swann, K. Redistribution of mitochondria leads to bursts of ATP production during spontaneous mouse oocyte maturation. J. Cell. Physiol. 224, 672-680 (2010).
    • (2010) J. Cell. Physiol. , vol.224 , pp. 672-680
    • Yu, Y.1    Dumollard, R.2    Rossbach, A.3    Lai, F.A.4    Swann, K.5
  • 70
    • 84874964540 scopus 로고    scopus 로고
    • Sequential actin-based pushing forces drive meiosis i chromosome migration and symmetry breaking in oocytes
    • Yi, K. et al. Sequential actin-based pushing forces drive meiosis I chromosome migration and symmetry breaking in oocytes. J. Cell Biol. 200, 567-576 (2013).
    • (2013) J. Cell Biol. , vol.200 , pp. 567-576
    • Yi, K.1
  • 71
    • 56149087648 scopus 로고    scopus 로고
    • Nucleophosmin is required for chromosome congression, proper mitotic spindle formation, and kinetochore-microtubule attachment in HeLa cells
    • Amin, M. A., Matsunaga, S., Uchiyama, S. & Fukui, K. Nucleophosmin is required for chromosome congression, proper mitotic spindle formation, and kinetochore-microtubule attachment in HeLa cells. FEBS Lett. 582, 3839-3844 (2008).
    • (2008) FEBS Lett. , vol.582 , pp. 3839-3844
    • Amin, M.A.1    Matsunaga, S.2    Uchiyama, S.3    Fukui, K.4
  • 72
    • 55949106979 scopus 로고    scopus 로고
    • Deconstructing Survivin: Comprehensive genetic analysis of Survivin function by conditional knockout in a vertebrate cell line
    • Yue, Z. et al. Deconstructing Survivin: comprehensive genetic analysis of Survivin function by conditional knockout in a vertebrate cell line. J. Cell Biol. 183, 279-296 (2008).
    • (2008) J. Cell Biol. , vol.183 , pp. 279-296
    • Yue, Z.1
  • 73
    • 0028650299 scopus 로고
    • Intron-less RNA injected into the nucleus of Xenopus oocytes accesses a regulated translation control pathway
    • Braddock, M. et al. Intron-less RNA injected into the nucleus of Xenopus oocytes accesses a regulated translation control pathway. Nucleic Acids Res. 22, 5255-5264 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5255-5264
    • Braddock, M.1
  • 74
    • 0036721534 scopus 로고    scopus 로고
    • Germinal vesicle material is essential for nucleus remodeling after nuclear transfer
    • Gao, S. et al. Germinal vesicle material is essential for nucleus remodeling after nuclear transfer. Biol. Reprod. 67, 928-934 (2002).
    • (2002) Biol. Reprod. , vol.67 , pp. 928-934
    • Gao, S.1
  • 75
    • 19344363154 scopus 로고    scopus 로고
    • Oocyte nucleus controls progression through meiotic maturation
    • Polanski, Z., Hoffmann, S. & Tsurumi, C. Oocyte nucleus controls progression through meiotic maturation. Dev. Biol. 281, 184-195 (2005).
    • (2005) Dev. Biol. , vol.281 , pp. 184-195
    • Polanski, Z.1    Hoffmann, S.2    Tsurumi, C.3
  • 76
    • 84883244324 scopus 로고    scopus 로고
    • Molecular causes of aneuploidy in mammalian eggs
    • Jones, K. T. & Lane, S. I. R. Molecular causes of aneuploidy in mammalian eggs. Development 140, 3719-3730 (2013).
    • (2013) Development , vol.140 , pp. 3719-3730
    • Jones, K.T.1    Lane, S.I.R.2
  • 77
    • 77954095160 scopus 로고    scopus 로고
    • In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons
    • Dieterich, D. C. et al. In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons. Nat. Neurosci. 13, 897-905 (2010).
    • (2010) Nat. Neurosci. , vol.13 , pp. 897-905
    • Dieterich, D.C.1
  • 78
    • 0036765389 scopus 로고    scopus 로고
    • Simultaneous analysis of chromosomes and chromosome associated proteins in mammalian oocytes and embryos
    • Hodges, C. A. & Hunt, P. A. Simultaneous analysis of chromosomes and chromosome associated proteins in mammalian oocytes and embryos. Chromosoma 111, 165-169 (2002).
    • (2002) Chromosoma , vol.111 , pp. 165-169
    • Hodges, C.A.1    Hunt, P.A.2
  • 79
    • 56449096676 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation initiation in the early stage porcine parthenotes
    • Susor, A. et al. Regulation of cap-dependent translation initiation in the early stage porcine parthenotes. Mol. Reprod. Dev. 75, 1716-1725 (2008).
    • (2008) Mol. Reprod. Dev. , vol.75 , pp. 1716-1725
    • Susor, A.1
  • 80
    • 84873428466 scopus 로고    scopus 로고
    • Mechanistic basis of infertility of mouse intersubspecific hybrids
    • Bhattacharyya, T. et al. Mechanistic basis of infertility of mouse intersubspecific hybrids. Proc. Natl Acad. Sci. USA 110, E468-E477 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E468-E477
    • Bhattacharyya, T.1
  • 81
    • 84860527756 scopus 로고    scopus 로고
    • A unifying model for mTORC1-mediated regulation of mRNA translation
    • Thoreen, C. C. et al. A unifying model for mTORC1-mediated regulation of mRNA translation. Nature 485, 109-113 (2012).
    • (2012) Nature , vol.485 , pp. 109-113
    • Thoreen, C.C.1
  • 82
    • 84876318702 scopus 로고    scopus 로고
    • Translational repression and eIF4A2 activity are critical for microRNA mediated gene regulation
    • Meijer, H. A. et al. Translational repression and eIF4A2 activity are critical for microRNA mediated gene regulation. Science 340, 82-85 (2013).
    • (2013) Science , vol.340 , pp. 82-85
    • Meijer, H.A.1


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