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Volumn 11, Issue 4, 2004, Pages 365-372

Synaptic plasticity and translation initiation

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 2; MESSENGER RNA; NEUROTROPHIN RECEPTOR;

EID: 4043055356     PISSN: 10720502     EISSN: None     Source Type: Journal    
DOI: 10.1101/lm.79004     Document Type: Review
Times cited : (95)

References (94)
  • 1
    • 0034990497 scopus 로고    scopus 로고
    • Dynamic visualization of local protein synthesis in hippocampal neurons
    • Aakalu, G., Smith, W.B., Nguyen, N., Jiang, C., and Schuman, E.M. 2001. Dynamic visualization of local protein synthesis in hippocampal neurons. Neuron 30: 489-502.
    • (2001) Neuron , vol.30 , pp. 489-502
    • Aakalu, G.1    Smith, W.B.2    Nguyen, N.3    Jiang, C.4    Schuman, E.M.5
  • 2
    • 2542542866 scopus 로고    scopus 로고
    • Selective modulation of some forms of Schaffer collateral-CA1 synaptic plasticity in mice with a disruption of the CPEB-1 gene
    • Alarcon, J.M., Hodgman, R., Theis, M., Huang, Y.-S., Kandel, E.R., and Richter, J.D. 2004. Selective modulation of some forms of Schaffer collateral-CA1 synaptic plasticity in mice with a disruption of the CPEB-1 gene. Learn. Mem. 11: 318-327.
    • (2004) Learn. Mem. , vol.11 , pp. 318-327
    • Alarcon, J.M.1    Hodgman, R.2    Theis, M.3    Huang, Y.-S.4    Kandel, E.R.5    Richter, J.D.6
  • 3
    • 0037456560 scopus 로고    scopus 로고
    • Sunrise at the synapse: The FMRP mRNP shaping the synaptic interface
    • Antar, L.N. and Bassell, G.J. 2003. Sunrise at the synapse: The FMRP mRNP shaping the synaptic interface. Neuron 37: 555-558.
    • (2003) Neuron , vol.37 , pp. 555-558
    • Antar, L.N.1    Bassell, G.J.2
  • 4
    • 0242586074 scopus 로고    scopus 로고
    • Localization of translational components at the ultramicroscopic level at postsynaptic sites of the rat brain
    • Asaki, C., Usuda, N., Nakazawa, A., Kametani, K., and Suzuki, T. 2003. Localization of translational components at the ultramicroscopic level at postsynaptic sites of the rat brain. Brain Res. 972: 168-176.
    • (2003) Brain Res. , vol.972 , pp. 168-176
    • Asaki, C.1    Usuda, N.2    Nakazawa, A.3    Kametani, K.4    Suzuki, T.5
  • 5
    • 0027377580 scopus 로고
    • FMR1 protein: Conserved RNP family domains and selective RNA binding
    • Ashley Jr., C.T., Wilkinson, K.D., Reines, D., and Warren, S.T. 1993. FMR1 protein: Conserved RNP family domains and selective RNA binding. Science 262: 563-566.
    • (1993) Science , vol.262 , pp. 563-566
    • Ashley Jr., C.T.1    Wilkinson, K.D.2    Reines, D.3    Warren, S.T.4
  • 7
    • 4043117394 scopus 로고    scopus 로고
    • NMDA receptor activation results in PKA- and ERK-dependent Mnk1 activation and increased eIF4E phosphorylation in hippocampal area CA1
    • in press
    • Banko, J.L., Hou, L., and Klann, E. 2004. NMDA receptor activation results in PKA- and ERK-dependent Mnk1 activation and increased eIF4E phosphorylation in hippocampal area CA1. J. Neurochem. (in press).
    • (2004) J. Neurochem.
    • Banko, J.L.1    Hou, L.2    Klann, E.3
  • 8
    • 0035829729 scopus 로고    scopus 로고
    • Phosphorylation and local presynaptic protein synthesis in calcium- and calcineurin-dependent induction of crayfish long-term facilitation
    • Beaumont, V., Zhong, N., Fletcher, R., Froemke, R.C., and Zucker, R.S. 2001. Phosphorylation and local presynaptic protein synthesis in calcium- and calcineurin-dependent induction of crayfish long-term facilitation. Neuron 32: 489-501.
    • (2001) Neuron , vol.32 , pp. 489-501
    • Beaumont, V.1    Zhong, N.2    Fletcher, R.3    Froemke, R.C.4    Zucker, R.S.5
  • 9
    • 0030066934 scopus 로고    scopus 로고
    • Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits cap-dependent initiation of translation
    • Beretta, L., Gingras, A.C., Svitkin, Y.V., Hall, M.N., and Sonenberg, N. 1996. Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits cap-dependent initiation of translation. EMBO J. 15: 658-664.
    • (1996) EMBO J. , vol.15 , pp. 658-664
    • Beretta, L.1    Gingras, A.C.2    Svitkin, Y.V.3    Hall, M.N.4    Sonenberg, N.5
  • 11
    • 0032546976 scopus 로고    scopus 로고
    • Purified recombinant FMRP exhibits selective RNA binding as an intrinsic property of the fragile X mental retardation protein
    • Brown, V., Small, K., Lakkis, L., Yeng, Y., Gunter, C., Wilkinson, K.D., and Warren, S.T. 1998. Purified recombinant FMRP exhibits selective RNA binding as an intrinsic property of the fragile X mental retardation protein. J. Biol. Chem. 273: 15521-15527.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15521-15527
    • Brown, V.1    Small, K.2    Lakkis, L.3    Yeng, Y.4    Gunter, C.5    Wilkinson, K.D.6    Warren, S.T.7
  • 12
    • 18044379515 scopus 로고    scopus 로고
    • Microarray identification of FMRP-associated brain mRNAs and altered mRNA translational profiles in fragile X syndrome
    • Brown, V., Jin, P., Ceman, S., Darnell, J.C., O'Donnell, W.T., Tenebaum, S.A., Jin, X., Feng, Y., Wilkinson, K.D., Keene, J.D., et al. 2001. Microarray identification of FMRP-associated brain mRNAs and altered mRNA translational profiles in fragile X syndrome. Cell 107: 477-487.
    • (2001) Cell , vol.107 , pp. 477-487
    • Brown, V.1    Jin, P.2    Ceman, S.3    Darnell, J.C.4    O'Donnell, W.T.5    Tenebaum, S.A.6    Jin, X.7    Feng, Y.8    Wilkinson, K.D.9    Keene, J.D.10
  • 13
    • 0344630216 scopus 로고    scopus 로고
    • Time-restricted role for dendritic activation of the mTOR-p70S6K pathway in the induction of late-phase long-term potentiation in the CA1
    • Cammalleri, M., Lütjens, R., Berton, F., King, A.R., Simpson, C., Francesconi, W., and Sanna, P.P. 2003. Time-restricted role for dendritic activation of the mTOR-p70S6K pathway in the induction of late-phase long-term potentiation in the CA1. Proc. Natl. Acad. Sci. 100: 14368-14373.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 14368-14373
    • Cammalleri, M.1    Lütjens, R.2    Berton, F.3    King, A.R.4    Simpson, C.5    Francesconi, W.6    Sanna, P.P.7
  • 14
    • 0037099704 scopus 로고    scopus 로고
    • Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A) binding protein controls cyclin B1 mRNA translation and oocyte maturation
    • Cao, Q. and Richter, J.D. 2002. Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A) binding protein controls cyclin B1 mRNA translation and oocyte maturation. EMBO J. 21: 3852-3862.
    • (2002) EMBO J. , vol.21 , pp. 3852-3862
    • Cao, Q.1    Richter, J.D.2
  • 15
    • 0025003542 scopus 로고
    • Functional properties of phosphorylated elongation factor 2
    • Carlberg, U., Nilsson, A., and Nygard, O. 1990. Functional properties of phosphorylated elongation factor 2. Eur. J. Biochem. 191: 639-645.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 639-645
    • Carlberg, U.1    Nilsson, A.2    Nygard, O.3
  • 16
    • 0032692620 scopus 로고    scopus 로고
    • A transient, neuron-wide form of CREB-mediated long-term facilitation can be stabilized at specific synapses by local protein synthesis
    • Casadio, A., Martin, K.C., Giustetto, M., Zhu, H., Chen, M., Bartsch, D., Bailey, C.H., and Kandel, E.R. 1999. A transient, neuron-wide form of CREB-mediated long-term facilitation can be stabilized at specific synapses by local protein synthesis. Cell 99: 221-237.
    • (1999) Cell , vol.99 , pp. 221-237
    • Casadio, A.1    Martin, K.C.2    Giustetto, M.3    Zhu, H.4    Chen, M.5    Bartsch, D.6    Bailey, C.H.7    Kandel, E.R.8
  • 17
    • 12244291012 scopus 로고    scopus 로고
    • Adenylyl cyclase-dependent form of chemical long-term potentiation triggers translational regulation at the elongation step
    • Chotiner, J.K., Khorasani, H., Nairn, A.C., O'Dell, T.J., and Watson, J.B. 2003. Adenylyl cyclase-dependent form of chemical long-term potentiation triggers translational regulation at the elongation step. Neuroscience 116: 743-752.
    • (2003) Neuroscience , vol.116 , pp. 743-752
    • Chotiner, J.K.1    Khorasani, H.2    Nairn, A.C.3    O'Dell, T.J.4    Watson, J.B.5
  • 18
    • 10744226084 scopus 로고    scopus 로고
    • Protein processing and plasticity
    • Cushman, S. 2003. Protein processing and plasticity. Learn. Mem. 10: 305.
    • (2003) Learn. Mem. , vol.10 , pp. 305
    • Cushman, S.1
  • 19
    • 0021523971 scopus 로고
    • Protein synthesis and memory: A review
    • Davis, H.P. and Squire, L.R. 1984. Protein synthesis and memory: A review. Psychol. Bull. 96: 518-559.
    • (1984) Psychol. Bull. , vol.96 , pp. 518-559
    • Davis, H.P.1    Squire, L.R.2
  • 21
  • 22
    • 0033213918 scopus 로고    scopus 로고
    • Translation initiation: Adept at adapting
    • Dever, T.E. 1999. Translation initiation: Adept at adapting. Trends. Biochem. Sci. 24: 398-403.
    • (1999) Trends. Biochem. Sci. , vol.24 , pp. 398-403
    • Dever, T.E.1
  • 23
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • -. 2002. Gene-specific regulation by general translation factors. Cell 108: 545-556.
    • (2002) Cell , vol.108 , pp. 545-556
  • 24
    • 0033604521 scopus 로고    scopus 로고
    • Ribosomal S6 kinase signaling and the control of translation
    • Dufner, A. and Thomas, G. 1999. Ribosomal S6 kinase signaling and the control of translation. Exp. Cell Res. 253: 100-109.
    • (1999) Exp. Cell Res. , vol.253 , pp. 100-109
    • Dufner, A.1    Thomas, G.2
  • 25
    • 0033929169 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor 4E phosphorylation in the nervous system of Aplysia californica
    • Dyer, J.R. and Sossin, W.S. 2000. Regulation of eukaryotic initiation factor 4E phosphorylation in the nervous system of Aplysia californica. J. Neurochem. 75: 872-881.
    • (2000) J. Neurochem. , vol.75 , pp. 872-881
    • Dyer, J.R.1    Sossin, W.S.2
  • 26
    • 0345505221 scopus 로고    scopus 로고
    • An activity-dependent switch to cap-independent translation triggered by eIF4E dephosphorylation
    • Dyer, J.R., Michel, S., Lee, W., Castellucci, V.F., Wayne, N.L., and Sossin, W.S. 2003. An activity-dependent switch to cap-independent translation triggered by eIF4E dephosphorylation. Nat. Neurosci. 6: 219-220.
    • (2003) Nat. Neurosci. , vol.6 , pp. 219-220
    • Dyer, J.R.1    Michel, S.2    Lee, W.3    Castellucci, V.F.4    Wayne, N.L.5    Sossin, W.S.6
  • 27
    • 0031046778 scopus 로고    scopus 로고
    • Fragile X mental retardation protein: Nucleocytoplasmic shuttling and association with somatodendritic ribosomes
    • Feng, Y., Gutekunst, C.A., Eberhart, D.E., Yi, H., Warren, S.T., and Hersch, S.M. 1997. Fragile X mental retardation protein: Nucleocytoplasmic shuttling and association with somatodendritic ribosomes. J. Neurosci. 17: 1539-1547.
    • (1997) J. Neurosci. , vol.17 , pp. 1539-1547
    • Feng, Y.1    Gutekunst, C.A.2    Eberhart, D.E.3    Yi, H.4    Warren, S.T.5    Hersch, S.M.6
  • 28
    • 0031024891 scopus 로고    scopus 로고
    • Synaptic tagging and long-term potentiation
    • Frey, U. and Morris, R.G. 1997. Synaptic tagging and long-term potentiation. Nature 385: 533-536.
    • (1997) Nature , vol.385 , pp. 533-536
    • Frey, U.1    Morris, R.G.2
  • 29
    • 0001798492 scopus 로고    scopus 로고
    • S6 phosphorylation and signal transduction
    • (eds. N. Sonenberg, J.W.B. Hershey, and M.B. Matthews). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Fumagalli, S. and Thomas, G. 2000. S6 phosphorylation and signal transduction. In Translational control of gene expression (eds. N. Sonenberg, J.W.B. Hershey, and M.B. Matthews), pp. 695-718. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , pp. 695-718
    • Fumagalli, S.1    Thomas, G.2
  • 30
    • 2442637740 scopus 로고    scopus 로고
    • Extracellular signal-regulated protein kinase activation is required for metabotropic glutamate receptor-dependent long-term depression in hippocampal area CA1
    • Gallagher, S.M., Daly, C.A., Bear, M.F., and Huber, K.M. 2004. Extracellular signal-regulated protein kinase activation is required for metabotropic glutamate receptor-dependent long-term depression in hippocampal area CA1. J. Neurosci. 24: 4859-4864.
    • (2004) J. Neurosci. , vol.24 , pp. 4859-4864
    • Gallagher, S.M.1    Daly, C.A.2    Bear, M.F.3    Huber, K.M.4
  • 31
    • 0026038913 scopus 로고
    • The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency
    • Gallie, D.R. 1991. The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency. Genes & Dev. 5: 2108-2116.
    • (1991) Genes & Dev. , vol.5 , pp. 2108-2116
    • Gallie, D.R.1
  • 32
    • 0032520009 scopus 로고    scopus 로고
    • 4E-BP1, a represser of mRNA translation, is phosphorylated and inactivated by the Akt (PKB) signaling pathway
    • Gingras, A.C., Kennedy, S.G., O'Leary, M.A., Sonenberg, N., and Hay, N. 1998. 4E-BP1, a represser of mRNA translation, is phosphorylated and inactivated by the Akt (PKB) signaling pathway. Genes & Dev. 12: 502-513.
    • (1998) Genes & Dev. , vol.12 , pp. 502-513
    • Gingras, A.C.1    Kennedy, S.G.2    O'Leary, M.A.3    Sonenberg, N.4    Hay, N.5
  • 33
    • 0035885153 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase regulates early phosphorylation and delayed expression of Ca2+/calmodulin-dependent protein kinase II in long-term potentiation
    • Giovannini, M.G., Blitzer, R.D., Wong, T., Asoma, K., Tsokas, P., Morrison, J.H., Iyengar, R., and Landau, E.M. 2001. Mitogen-activated protein kinase regulates early phosphorylation and delayed expression of Ca2+/calmodulin-dependent protein kinase II in long-term potentiation. J. Neurosci. 21: 7053-7062.
    • (2001) J. Neurosci. , vol.21 , pp. 7053-7062
    • Giovannini, M.G.1    Blitzer, R.D.2    Wong, T.3    Asoma, K.4    Tsokas, P.5    Morrison, J.H.6    Iyengar, R.7    Landau, E.M.8
  • 34
    • 0035396727 scopus 로고    scopus 로고
    • Internal ribosome entry sites in eukaryotic mRNA molecules
    • Hellen, C.U. and Sarnow, P. 2001. Internal ribosome entry sites in eukaryotic mRNA molecules. Genes & Dev. 15: 1593-1612.
    • (2001) Genes & Dev. , vol.15 , pp. 1593-1612
    • Hellen, C.U.1    Sarnow, P.2
  • 35
    • 0000091608 scopus 로고    scopus 로고
    • Pathway and mechanism of initiation of protein synthesis
    • (eds. N. Sonenberg et al.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hershey, J.W.B. and Merrick, W.C. 2000. Pathway and mechanism of initiation of protein synthesis. In Translational control of gene expression (eds. N. Sonenberg et al.), pp. 33-88. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , pp. 33-88
    • Hershey, J.W.B.1    Merrick, W.C.2
  • 36
    • 3242724040 scopus 로고    scopus 로고
    • Activation of the phosphoinositide 3-kinase-Akt-mammalian target of rapamycin signaling pathway is required for metabotropic glutamate receptor-dependent long-term depression
    • Hou, L. and Klann, E. 2004. Activation of the phosphoinositide 3-kinase-Akt-mammalian target of rapamycin signaling pathway is required for metabotropic glutamate receptor-dependent long-term depression. J. Neurosci. 24: 6352-6361.
    • (2004) J. Neurosci. , vol.24 , pp. 6352-6361
    • Hou, L.1    Klann, E.2
  • 37
    • 0034685813 scopus 로고    scopus 로고
    • Role for rapid dendritic protein synthesis in hippocampal mGluR-dependent long-term depression
    • Huber, K.M., Kayser, M.S., and Bear, M.F. 2000. Role for rapid dendritic protein synthesis in hippocampal mGluR-dependent long-term depression. Science 288: 1254-1257.
    • (2000) Science , vol.288 , pp. 1254-1257
    • Huber, K.M.1    Kayser, M.S.2    Bear, M.F.3
  • 38
    • 0034942216 scopus 로고    scopus 로고
    • Chemical induction of mGluRS- and protein synthesis-dependent long-term depression in hippocampal area CA1
    • Huber, K.M, Roder, J.C., and Bear, M.F. 2001. Chemical induction of mGluRS- and protein synthesis-dependent long-term depression in hippocampal area CA1. J. Neurophysiol. 86: 321-325.
    • (2001) J. Neurophysiol. , vol.86 , pp. 321-325
    • Huber, K.M.1    Roder, J.C.2    Bear, M.F.3
  • 39
    • 0037188502 scopus 로고    scopus 로고
    • Altered synaptic plasticity in a mouse model of fragile X mental retardation
    • Huber, K.M., Gallagher, S.M., Warren, S.T., and Bear, M.F. 2002. Altered synaptic plasticity in a mouse model of fragile X mental retardation. Proc. Natl. Acad. Sci. 99: 7746-7750.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 7746-7750
    • Huber, K.M.1    Gallagher, S.M.2    Warren, S.T.3    Bear, M.F.4
  • 40
    • 0344356146 scopus 로고    scopus 로고
    • Cellular and subcellular distributions of translation initiation, elongation and release factors in rat hippocampus
    • Inamura, N., Hoshino, S., Uchiumi, T., Nawa, H., and Takei, N. 2003. Cellular and subcellular distributions of translation initiation, elongation and release factors in rat hippocampus. Mol. Brain Res. 111: 165-174.
    • (2003) Mol. Brain Res. , vol.111 , pp. 165-174
    • Inamura, N.1    Hoshino, S.2    Uchiumi, T.3    Nawa, H.4    Takei, N.5
  • 41
    • 0037333288 scopus 로고    scopus 로고
    • New insights into fragile X syndrome: From molecules to neurobehaviors
    • Jin, P. and Warren, S.T. 2003. New insights into fragile X syndrome: From molecules to neurobehaviors. Trends Biochem. Sci. 28: 152-158.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 152-158
    • Jin, P.1    Warren, S.T.2
  • 42
    • 0029794770 scopus 로고    scopus 로고
    • A requirement for local protein synthesis in neurotrophin-induced hippocampal synaptic plasticity
    • Kang, H. and Schuman, E.M. 1996. A requirement for local protein synthesis in neurotrophin-induced hippocampal synaptic plasticity. Science 273: 1402-1406.
    • (1996) Science , vol.273 , pp. 1402-1406
    • Kang, H.1    Schuman, E.M.2
  • 43
    • 1342322145 scopus 로고    scopus 로고
    • Translational control by MAPK signaling in long-term synaptic plasticity and memory
    • Kelleher III, R.J., Govindarajan, A., Jung, H.-Y., Kang, H., and Tonegawa, S. 2004. Translational control by MAPK signaling in long-term synaptic plasticity and memory. Cell 116: 1-20.
    • (2004) Cell , vol.116 , pp. 1-20
    • Kelleher III, R.J.1    Govindarajan, A.2    Jung, H.-Y.3    Kang, H.4    Tonegawa, S.5
  • 44
    • 0033977099 scopus 로고    scopus 로고
    • Long-term potentiation in dentate gyrus of the rat is inhibited by the phosphoinositide 3-kinase inhibitor wortmannin
    • Kelly, A. and Lynch, M.A. 2000. Long-term potentiation in dentate gyrus of the rat is inhibited by the phosphoinositide 3-kinase inhibitor wortmannin. Neuropharmacology 39: 643-651.
    • (2000) Neuropharmacology , vol.39 , pp. 643-651
    • Kelly, A.1    Lynch, M.A.2
  • 45
    • 0035862960 scopus 로고    scopus 로고
    • Serotonin activates S6 kinase in a rapamycin-sensitive manner is Aplysia synaptosomes
    • Khan, A., Pepio, A.M., and Sossin, W.S. 2001. Serotonin activates S6 kinase in a rapamycin-sensitive manner is Aplysia synaptosomes. J. Neurosci. 21: 382-391.
    • (2001) J. Neurosci. , vol.21 , pp. 382-391
    • Khan, A.1    Pepio, A.M.2    Sossin, W.S.3
  • 46
  • 47
    • 0035368955 scopus 로고    scopus 로고
    • The fragile X mental retardation protein inhibits translation via interacting with mRNA
    • Li, Z., Zhang, Y., Ku, L., Wilkinson, K.D., Warren, S.T., and Feng, Y. 2001. The fragile X mental retardation protein inhibits translation via interacting with mRNA. Nucleic Acids Res. 29: 2276-2283.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2276-2283
    • Li, Z.1    Zhang, Y.2    Ku, L.3    Wilkinson, K.D.4    Warren, S.T.5    Feng, Y.6
  • 49
    • 0037414701 scopus 로고    scopus 로고
    • The cytoplasmic polyadenylation element binding protein and polyadenylation of messenger RNAs in Aplysia neurons
    • Liu, J. and Schwartz, J.H. 2003. The cytoplasmic polyadenylation element binding protein and polyadenylation of messenger RNAs in Aplysia neurons. Brain Res. 959: 68-76.
    • (2003) Brain Res. , vol.959 , pp. 68-76
    • Liu, J.1    Schwartz, J.H.2
  • 51
    • 0028245588 scopus 로고
    • Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2α kinase
    • Mellor, H., Flowers, K., Kimball, S.R., and Jefferson, L.S. 1994. Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2α kinase. J. Biol. Chem. 269: 10201-10204.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10201-10204
    • Mellor, H.1    Flowers, K.2    Kimball, S.R.3    Jefferson, L.S.4
  • 53
    • 0033634850 scopus 로고    scopus 로고
    • Phosphorylation of CPEB by Eg2 mediates recruitment of CPSF into an active cytoplasmic polyadenylation complex
    • Mendez, R., Murphy, K.G., Ryan, K., Manley, J.L., and Richter, J.D. 2000b. Phosphorylation of CPEB by Eg2 mediates recruitment of CPSF into an active cytoplasmic polyadenylation complex. Mol. Cell 6: 1253-1259.
    • (2000) Mol. Cell , vol.6 , pp. 1253-1259
    • Mendez, R.1    Murphy, K.G.2    Ryan, K.3    Manley, J.L.4    Richter, J.D.5
  • 54
    • 0002921709 scopus 로고    scopus 로고
    • Translational control of top mRNAs
    • (eds. N. Sonenberg et al.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Meyhaus, O. and Hornstein, E. 2000. Translational control of top mRNAs. In Translational control of gene expression (eds. N. Sonenberg et al.), pp. 671-694. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , pp. 671-694
    • Meyhaus, O.1    Hornstein, E.2
  • 55
    • 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., and Rhoads, R.E. 1994. 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. 91: 7668-7672.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 7668-7672
    • Minich, W.B.1    Balasta, M.L.2    Goss, D.J.3    Rhoads, R.E.4
  • 56
    • 0021891865 scopus 로고
    • Eukaryotic protein synthesis
    • Moldave, K. 1985. Eukaryotic protein synthesis. Annu. Rev. Biochem. 54: 1109-1149.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 1109-1149
    • Moldave, K.1
  • 57
    • 0022835911 scopus 로고
    • A critical period for macromolecular synthesis in long-term heterosynaptic facilitation in Aplysia
    • Montarolo, P.G., Goelet, P., Castellucci, V.F., Morgan, J., Kandel, E.R., and Schacher, S. 1986. A critical period for macromolecular synthesis in long-term heterosynaptic facilitation in Aplysia. Science 234: 1249-1254.
    • (1986) Science , vol.234 , pp. 1249-1254
    • Montarolo, P.G.1    Goelet, P.2    Castellucci, V.F.3    Morgan, J.4    Kandel, E.R.5    Schacher, S.6
  • 59
    • 0030799633 scopus 로고    scopus 로고
    • Brief θ burst stimulation induced a transcription-dependent late phase of LTP requiring cAMP in area CA1 of the mouse hippocampus
    • Nguyen, P.V., Abel, T., and Kandel, E.R. 1997. Brief θ burst stimulation induced a transcription-dependent late phase of LTP requiring cAMP in area CA1 of the mouse hippocampus. Learn. Mem. 4: 230-243.
    • (1997) Learn. Mem. , vol.4 , pp. 230-243
    • Nguyen, P.V.1    Abel, T.2    Kandel, E.R.3
  • 60
    • 0037868947 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase regulates the induction of long-term potentiatioh through extracellular signal-regulated kinase-independent mechanisms
    • Opazo, P., Watabe, A.M., Grant, S.G., and O'Dell, T.J. 2003. Phosphatidylinositol 3-kinase regulates the induction of long-term potentiatioh through extracellular signal-regulated kinase-independent mechanisms. J. Neurosci. 23: 3679-3688.
    • (2003) J. Neurosci. , vol.23 , pp. 3679-3688
    • Opazo, P.1    Watabe, A.M.2    Grant, S.G.3    O'Dell, T.J.4
  • 61
    • 16944366067 scopus 로고    scopus 로고
    • Visualization of the distribution of autophosphorylated calcium/calmodulin-dependent protein kinase II after tetanic stimulation in the CA1 area of the hippocampus
    • Ouyang, Y., Kantor, D.B., Harris, K.M., Schuman, E.M., and Kennedy, M.B. 1997. Visualization of the distribution of autophosphorylated calcium/calmodulin-dependent protein kinase II after tetanic stimulation in the CA1 area of the hippocampus. J. Neurosci. 17: 5416-5427.
    • (1997) J. Neurosci. , vol.17 , pp. 5416-5427
    • Ouyang, Y.1    Kantor, D.B.2    Harris, K.M.3    Schuman, E.M.4    Kennedy, M.B.5
  • 63
    • 0027273725 scopus 로고
    • Regulation of elongation factor-2 by multisite phosphorylation
    • Redpath, N.T., Price, N.T., Severinov, K.V., and Proud, C.G. 1993. Regulation of elongation factor-2 by multisite phosphorylation. Eur. J. Biochem. 213: 689-699.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 689-699
    • Redpath, N.T.1    Price, N.T.2    Severinov, K.V.3    Proud, C.G.4
  • 64
    • 0001364237 scopus 로고    scopus 로고
    • Influence of polyadenylation-induced translation on metazoan development and neuronal synaptic function
    • (eds. N. Sonenberg et al.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Richter, J.D. 2000. Influence of polyadenylation-induced translation on metazoan development and neuronal synaptic function. In Translational control of gene expression (eds. N. Sonenberg et al.), pp. 785-805. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , pp. 785-805
    • Richter, J.D.1
  • 65
    • 0024365118 scopus 로고
    • Mechanism of elongation factor 2 (EF-2) inactivation upon phosphorylation. Phosphorylated EF-2 is unable to catalyze translocation
    • Ryazanov, A.G. and Davydova, E.K. 1989. Mechanism of elongation factor 2 (EF-2) inactivation upon phosphorylation. Phosphorylated EF-2 is unable to catalyze translocation. FEBS Lett. 251: 187-190.
    • (1989) FEBS Lett. , vol.251 , pp. 187-190
    • Ryazanov, A.G.1    Davydova, E.K.2
  • 66
    • 0002411516 scopus 로고    scopus 로고
    • Physical and functional interactions between the mRNA cap structure and the poly(A) tail
    • (eds. N. Sonenberg et al.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sachs, A. 2000. Physical and functional interactions between the mRNA cap structure and the poly(A) tail. In Translational control of gene expression (eds. N. Sonenberg et al.), pp. 447-466. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , pp. 447-466
    • Sachs, A.1
  • 67
    • 0036580702 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is required for the expression but not for the induction or the maintenance of long-term potentiation in the hippocampal CA1 region
    • Sanna, P.P., Cammalleri, M., Berton, F., Simpson, C., Lutjens, R., Bloom, F.E. and Francesconi, W. 2002. Phosphatidylinositol 3-kinase is required for the expression but not for the induction or the maintenance of long-term potentiation in the hippocampal CA1 region. J. Neurosci. 22: 3359-3365.
    • (2002) J. Neurosci. , vol.22 , pp. 3359-3365
    • Sanna, P.P.1    Cammalleri, M.2    Berton, F.3    Simpson, C.4    Lutjens, R.5    Bloom, F.E.6    Francesconi, W.7
  • 68
    • 0031464793 scopus 로고    scopus 로고
    • N-methyl-D-aspartate receptor activation and visual activity induce elongation factor-2 phosphorylation in amphibian tecta: A role for N-methyl-D-aspartate receptors in controlling protein synthesis
    • Scheetz, A.J., Nairn, A.C., and Constantine-Paton, M. 1997. N-methyl-D-aspartate receptor activation and visual activity induce elongation factor-2 phosphorylation in amphibian tecta: A role for N-methyl-D-aspartate receptors in controlling protein synthesis. Proc. Natl. Acad. Sci. 94: 14770-14775.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 14770-14775
    • Scheetz, A.J.1    Nairn, A.C.2    Constantine-Paton, M.3
  • 69
    • 0034005882 scopus 로고    scopus 로고
    • NMDA receptor-mediated control of protein synthesis at developing synapses
    • Scheetz, A.J., Nairn, A.C., and Constantine-Paton, M. 2000. NMDA receptor-mediated control of protein synthesis at developing synapses. Nat. Neurosci. 3: 211-216.
    • (2000) Nat. Neurosci. , vol.3 , pp. 211-216
    • Scheetz, A.J.1    Nairn, A.C.2    Constantine-Paton, M.3
  • 70
    • 0036438924 scopus 로고    scopus 로고
    • Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation?
    • Scheper, G.C. and Proud, C.G. 2002. Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation? Eur. J. Biochem. 269: 5350-5359.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5350-5359
    • Scheper, G.C.1    Proud, C.G.2
  • 71
    • 0036479313 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA
    • Scheper, G.C., van Kollenberg, B., Hu, J., Luo, Y., Goss, D.J., and Proud, C.G. 2002. Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA. J. Biol. Chem. 277: 3303-3309.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3303-3309
    • Scheper, G.C.1    Van Kollenberg, B.2    Hu, J.3    Luo, Y.4    Goss, D.J.5    Proud, C.G.6
  • 72
    • 0031755020 scopus 로고    scopus 로고
    • Identification and characterization of pancreatic eukaryotic initiation factor 2α-subunit kinase, PEK, involved in translational control
    • Shi, Y., Vattem, K.M., Sood, R., Liang, J., Stramm, L., and Wek, R.C. 1998. Identification and characterization of pancreatic eukaryotic initiation factor 2α-subunit kinase, PEK, involved in translational control. Mol. Cell Biol. 18: 7499-7509.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 7499-7509
    • Shi, Y.1    Vattem, K.M.2    Sood, R.3    Liang, J.4    Stramm, L.5    Wek, R.C.6
  • 73
    • 0346186101 scopus 로고    scopus 로고
    • A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in Aplysia
    • Si, K., Giustetto, M., Etkin, A., Hsu, R., Janisiewicz, A.M., Miniaci, M.C., Kim, J.-H., Zhu, H., and Kandel, E.R. 2003. A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in Aplysia. Cell 115: 893-904.
    • (2003) Cell , vol.115 , pp. 893-904
    • Si, K.1    Giustetto, M.2    Etkin, A.3    Hsu, R.4    Janisiewicz, A.M.5    Miniaci, M.C.6    Kim, J.-H.7    Zhu, H.8    Kandel, E.R.9
  • 74
    • 0037311233 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factors and regulators
    • Sonenberg, N. and Dever, T.E. 2003. Eukaryotic translation initiation factors and regulators. Curr. Opin. Struct. Biol. 13: 56-63.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 56-63
    • Sonenberg, N.1    Dever, T.E.2
  • 75
    • 0033962298 scopus 로고    scopus 로고
    • A mammalian homologue of GCN2 piotein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2α
    • Sood, R., Porter, A.C., Olsen, D.A., Cavener, D.R., and Wek, R.C. 2000. A mammalian homologue of GCN2 piotein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2α. Genetics 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
  • 76
    • 0033394199 scopus 로고    scopus 로고
    • Maskin is a CPEB-associated factor that transiently interacts with eIF-4E
    • Stebbins-Boaz, B., Cao, Q., de Moor, C.H., Mendez, R., and Richter, J.D. 1999. Maskin is a CPEB-associated factor that transiently interacts with eIF-4E. Mol. Cell 4: 1017-1027.
    • (1999) Mol. Cell , vol.4 , pp. 1017-1027
    • Stebbins-Boaz, B.1    Cao, Q.2    De Moor, C.H.3    Mendez, R.4    Richter, J.D.5
  • 77
    • 0020063563 scopus 로고
    • Preferential localization of polyribosomes under the base of dendritic spines in granule cells of the dentate gyrus
    • Steward, O. and Levy, W.B. 1982. Preferential localization of polyribosomes under the base of dendritic spines in granule cells of the dentate gyrus. J. Neurosci. 2: 284-291.
    • (1982) J. Neurosci. , vol.2 , pp. 284-291
    • Steward, O.1    Levy, W.B.2
  • 78
    • 0036889291 scopus 로고    scopus 로고
    • Transduction of growth or mitogenic signals into translational activation of TOP mRNAs is fully reliant on the phosphatidylinositol 3-kinase-mediated pathway but requires neither S6K1 nor rpS6 phosphorylation
    • Stolovich, M., Tang, H., Horstein, E., Levy, G., Cohen, R., Bae, S.S., Birnbaum, M.J., and Meyhaus, O. 2002. Transduction of growth or mitogenic signals into translational activation of TOP mRNAs is fully reliant on the phosphatidylinositol 3-kinase-mediated pathway but requires neither S6K1 nor rpS6 phosphorylation. Mol. Cell Biol. 22:8101-8113.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 8101-8113
    • Stolovich, M.1    Tang, H.2    Horstein, E.3    Levy, G.4    Cohen, R.5    Bae, S.S.6    Birnbaum, M.J.7    Meyhaus, O.8
  • 79
    • 0035166616 scopus 로고    scopus 로고
    • The neuronal MAP kinase cascade: A biochemical signal integration system subserving synaptic plasticity and memory
    • Sweatt, J.D. 2001. The neuronal MAP kinase cascade: A biochemical signal integration system subserving synaptic plasticity and memory. J. Neurochem. 76: 1-10.
    • (2001) J. Neurochem. , vol.76 , pp. 1-10
    • Sweatt, J.D.1
  • 80
    • 0035900712 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor enhances neuronal translation by activating multiple initiation processes: Comparison with the effects of insulin
    • Takei, N., Kawamura, M., Hara, K., Yonezawa, K., and Nawa, H. 2001. Brain-derived neurotrophic factor enhances neuronal translation by activating multiple initiation processes: Comparison with the effects of insulin. J. Biol. Chem. 276: 42818-42825.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42818-42825
    • Takei, N.1    Kawamura, M.2    Hara, K.3    Yonezawa, K.4    Nawa, H.5
  • 81
    • 0037039358 scopus 로고    scopus 로고
    • A rapamycin-sensitive signaling pathway contributes to long-term synaptic plasticity in the hippocampus
    • Tang, S.J., Reis, G., Kang, H., Gingras, A.-C., Sonenberg, N., and Schuman, E.M. 2002. A rapamycin-sensitive signaling pathway contributes to long-term synaptic plasticity in the hippocampus. Proc. Natl. Acad. Sci. 99: 467-472.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 467-472
    • Tang, S.J.1    Reis, G.2    Kang, H.3    Gingras, A.-C.4    Sonenberg, N.5    Schuman, E.M.6
  • 82
    • 0035207605 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase, synaptic plasticity, and memory
    • Thiels, E. and Klann, E. 2001. Extracellular signal-regulated kinase, synaptic plasticity, and memory. Rev. Neurosci. 12: 327-345.
    • (2001) Rev. Neurosci. , vol.12 , pp. 327-345
    • Thiels, E.1    Klann, E.2
  • 84
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
    • Waskiewicz, A.J., Flynn, A., Proud, C.G., and Cooper, J.A. 1997. Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J. 16: 1909-1920.
    • (1997) EMBO J. , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3    Cooper, J.A.4
  • 85
    • 0032981328 scopus 로고    scopus 로고
    • Phosphorylation of the cap-binding protein eukaryotic translation initation factor 4E by protein kinase Mnk1 in vivo
    • Waskiewicz, A.J., Johnson, J.C., Penn, B., Mahalingam, M., Kimaball, S.R., and Cooper, J.A. 1999. Phosphorylation of the cap-binding protein eukaryotic translation initation factor 4E by protein kinase Mnk1 in vivo. Mol. Cell Biol. 19: 1871-1880.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1871-1880
    • Waskiewicz, A.J.1    Johnson, J.C.2    Penn, B.3    Mahalingam, M.4    Kimaball, S.R.5    Cooper, J.A.6
  • 87
    • 0032112017 scopus 로고    scopus 로고
    • Circularization of mRNA by eukaryotic translation initiation factors
    • Wells, S.E., Hillner, P.E., Vale, R.D., and Sachs, A.B. 1998. Circularization of mRNA by eukaryotic translation initiation factors. Mol. Cell 2: 135-140.
    • (1998) Mol. Cell , vol.2 , pp. 135-140
    • Wells, S.E.1    Hillner, P.E.2    Vale, R.D.3    Sachs, A.B.4
  • 88
    • 0035894857 scopus 로고    scopus 로고
    • A role for the cytoplasmic polyadenylation element in NMDA receptor-regulated mRNA translation in neurons
    • Wells, D.G., Dong, X., Quinlan, E.M., Huan, Y.S., Bear, M.F., Richter, J.D., and Fallon, J.R. 2001. A role for the cytoplasmic polyadenylation element in NMDA receptor-regulated mRNA translation in neurons. J. Neurosci. 21: 9541-9548.
    • (2001) J. Neurosci. , vol.21 , pp. 9541-9548
    • Wells, D.G.1    Dong, X.2    Quinlan, E.M.3    Huan, Y.S.4    Bear, M.F.5    Richter, J.D.6    Fallon, J.R.7
  • 89
    • 0032215079 scopus 로고    scopus 로고
    • CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of a-CaMKII mRNA at synapses
    • Wu, L., Wells, D., Tay, J., Mendis, D., Abbott, M.-A., Barnitt, A., Quinlan, E., Heynen, A., Fallon, J.R., and Richter, J.D. 1998. CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of a-CaMKII mRNA at synapses. Neuron 21: 1129-1139.
    • (1998) Neuron , vol.21 , pp. 1129-1139
    • Wu, L.1    Wells, D.2    Tay, J.3    Mendis, D.4    Abbott, M.-A.5    Barnitt, A.6    Quinlan, E.7    Heynen, A.8    Fallon, J.R.9    Richter, J.D.10
  • 90
    • 0037133172 scopus 로고    scopus 로고
    • The brain-derived neurotrophic factor enhances synthesis of Arc in synaptoneurosomes
    • Yin, Y., Edelman, G.M., and Vanderklish, P.W. 2002. The brain-derived neurotrophic factor enhances synthesis of Arc in synaptoneurosomes. Proc. Natl. Acad. Sci. 99: 2368-2373.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 2368-2373
    • Yin, Y.1    Edelman, G.M.2    Vanderklish, P.W.3
  • 91
    • 0037423293 scopus 로고    scopus 로고
    • The fragile X syndrome protein FMRP associates with BC1 RNA and regulates the translation of specific mRNAs at synapses
    • Zalfa, F., Giorgi, M., Primerano, B., Moro, A., DiPenta, A., Reis, S., Oostra, B., and Bagni, C. 2003. The fragile X syndrome protein FMRP associates with BC1 RNA and regulates the translation of specific mRNAs at synapses. Cell 112: 317-327.
    • (2003) Cell , vol.112 , pp. 317-327
    • Zalfa, F.1    Giorgi, M.2    Primerano, B.3    Moro, A.4    DiPenta, A.5    Reis, S.6    Oostra, B.7    Bagni, C.8
  • 92
    • 0035977134 scopus 로고    scopus 로고
    • Drosophila fragile X-related gene regulates the MAP1B homolog Futsch to control synaptic structure and function
    • Zhang, Y.Q., Bailey, A.M., Matthies, H.J., Renden, R.B., Smith, M.A., Speese, S.D., Rubin, G.M., and Broadie, K. 2001. Drosophila fragile X-related gene regulates the MAP1B homolog Futsch to control synaptic structure and function. Cell 107: 591-603.
    • (2001) Cell , vol.107 , pp. 591-603
    • Zhang, Y.Q.1    Bailey, A.M.2    Matthies, H.J.3    Renden, R.B.4    Smith, M.A.5    Speese, S.D.6    Rubin, G.M.7    Broadie, K.8
  • 93
    • 0037109732 scopus 로고    scopus 로고
    • The group I metabotropic glutamate receptor agonist (S)-3,5- dihydroxyphenyl-glycine induces a novel form of depotentiation in the CA1 region of the hippocampus
    • Zho, W.M., You, J.L., Huang, C.C., and Hsu, K.S. 2002. The group I metabotropic glutamate receptor agonist (S)-3,5-dihydroxyphenyl-glycine induces a novel form of depotentiation in the CA1 region of the hippocampus. J. Neurosci. 22: 8838-8849.
    • (2002) J. Neurosci. , vol.22 , pp. 8838-8849
    • Zho, W.M.1    You, J.L.2    Huang, C.C.3    Hsu, K.S.4


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