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Volumn 19, Issue 9, 2009, Pages 465-474

To localize or not to localize: mRNA fate is in 3′UTR ends

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PROTEIN;

EID: 69549135202     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2009.06.001     Document Type: Review
Times cited : (279)

References (112)
  • 1
    • 60149086205 scopus 로고    scopus 로고
    • mRNA localization: gene expression in the spatial dimension
    • Martin K.C., and Ephrussi A. mRNA localization: gene expression in the spatial dimension. Cell 136 (2009) 719-730
    • (2009) Cell , vol.136 , pp. 719-730
    • Martin, K.C.1    Ephrussi, A.2
  • 2
    • 0035674402 scopus 로고    scopus 로고
    • Translational regulation and RNA localization in Drosophila oocytes and embryos
    • Johnstone O., and Lasko P. Translational regulation and RNA localization in Drosophila oocytes and embryos. Annu. Rev. Genet. 35 (2001) 365-406
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 365-406
    • Johnstone, O.1    Lasko, P.2
  • 3
    • 34848918150 scopus 로고    scopus 로고
    • Global analysis of mRNA localization reveals a prominent role in organizing cellular architecture and function
    • Lecuyer E., et al. Global analysis of mRNA localization reveals a prominent role in organizing cellular architecture and function. Cell 131 (2007) 174-187
    • (2007) Cell , vol.131 , pp. 174-187
    • Lecuyer, E.1
  • 4
    • 0034432846 scopus 로고    scopus 로고
    • Protein synthesis in axons and its possible functions
    • Campenot R.B., and Eng H. Protein synthesis in axons and its possible functions. J. Neurocytol. 29 (2000) 793-798
    • (2000) J. Neurocytol. , vol.29 , pp. 793-798
    • Campenot, R.B.1    Eng, H.2
  • 5
    • 0037101970 scopus 로고    scopus 로고
    • Function and regulation of CREB family transcription factors in the nervous system
    • Lonze B.E., and Ginty D.D. Function and regulation of CREB family transcription factors in the nervous system. Neuron 35 (2002) 605-623
    • (2002) Neuron , vol.35 , pp. 605-623
    • Lonze, B.E.1    Ginty, D.D.2
  • 6
    • 55849130994 scopus 로고    scopus 로고
    • Communication between the synapse and the nucleus in neuronal development, plasticity, and disease
    • Cohen S., and Greenberg M.E. Communication between the synapse and the nucleus in neuronal development, plasticity, and disease. Annu. Rev. Cell Dev. Biol. 24 (2008) 183-209
    • (2008) Annu. Rev. Cell Dev. Biol. , vol.24 , pp. 183-209
    • Cohen, S.1    Greenberg, M.E.2
  • 7
    • 46149096244 scopus 로고    scopus 로고
    • Signaling mechanisms linking neuronal activity to gene expression and plasticity of the nervous system
    • Flavell S.W., and Greenberg M.E. Signaling mechanisms linking neuronal activity to gene expression and plasticity of the nervous system. Annu. Rev. Neurosci. 31 (2008) 563-590
    • (2008) Annu. Rev. Neurosci. , vol.31 , pp. 563-590
    • Flavell, S.W.1    Greenberg, M.E.2
  • 8
    • 60149110358 scopus 로고    scopus 로고
    • Pre-mRNA processing reaches back to transcription and ahead to translation
    • Moore M.J., and Proudfoot N.J. Pre-mRNA processing reaches back to transcription and ahead to translation. Cell 136 (2009) 688-700
    • (2009) Cell , vol.136 , pp. 688-700
    • Moore, M.J.1    Proudfoot, N.J.2
  • 9
    • 12344281782 scopus 로고    scopus 로고
    • The implications of structured 5′ untranslated regions on translation and disease
    • Pickering B.M., and Willis A.E. The implications of structured 5′ untranslated regions on translation and disease. Semin. Cell Dev. Biol. 16 (2005) 39-47
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 39-47
    • Pickering, B.M.1    Willis, A.E.2
  • 10
    • 24644502657 scopus 로고    scopus 로고
    • From birth to death: the complex lives of eukaryotic mRNAs
    • Moore M.J. From birth to death: the complex lives of eukaryotic mRNAs. Science 309 (2005) 1514-1518
    • (2005) Science , vol.309 , pp. 1514-1518
    • Moore, M.J.1
  • 12
    • 34247329067 scopus 로고    scopus 로고
    • Cis-acting determinants of asymmetric, cytoplasmic RNA transport
    • Jambhekar A., and Derisi J.L. Cis-acting determinants of asymmetric, cytoplasmic RNA transport. RNA 13 (2007) 625-642
    • (2007) RNA , vol.13 , pp. 625-642
    • Jambhekar, A.1    Derisi, J.L.2
  • 13
    • 0034990497 scopus 로고    scopus 로고
    • Dynamic visualization of local protein synthesis in hippocampal neurons
    • Aakalu G., et al. Dynamic visualization of local protein synthesis in hippocampal neurons. Neuron 30 (2001) 489-502
    • (2001) Neuron , vol.30 , pp. 489-502
    • Aakalu, G.1
  • 14
    • 2342439151 scopus 로고    scopus 로고
    • Splicing of oskar RNA in the nucleus is coupled to its cytoplasmic localization
    • Hachet O., and Ephrussi A. Splicing of oskar RNA in the nucleus is coupled to its cytoplasmic localization. Nature 428 (2004) 959-963
    • (2004) Nature , vol.428 , pp. 959-963
    • Hachet, O.1    Ephrussi, A.2
  • 15
    • 0033607521 scopus 로고    scopus 로고
    • Mutational analysis of a heterogeneous nuclear ribonucleoprotein A2 response element for RNA trafficking
    • Munro T.P., et al. Mutational analysis of a heterogeneous nuclear ribonucleoprotein A2 response element for RNA trafficking. J. Biol. Chem. 274 (1999) 34389-34395
    • (1999) J. Biol. Chem. , vol.274 , pp. 34389-34395
    • Munro, T.P.1
  • 16
    • 0030987508 scopus 로고    scopus 로고
    • Transport and localization elements in myelin basic protein mRNA
    • Ainger K., et al. Transport and localization elements in myelin basic protein mRNA. J. Cell Biol. 138 (1997) 1077-1087
    • (1997) J. Cell Biol. , vol.138 , pp. 1077-1087
    • Ainger, K.1
  • 17
    • 19344378943 scopus 로고    scopus 로고
    • Rules of engagement: co-transcriptional recruitment of pre-mRNA processing factors
    • Bentley D.L. Rules of engagement: co-transcriptional recruitment of pre-mRNA processing factors. Curr. Opin. Cell Biol. 17 (2005) 251-256
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 251-256
    • Bentley, D.L.1
  • 18
    • 38449094616 scopus 로고    scopus 로고
    • Cross-talks between transcription and post-transcriptional events within a 'mRNA factory'
    • Hagiwara M., and Nojima T. Cross-talks between transcription and post-transcriptional events within a 'mRNA factory'. J. Biochem. 142 (2007) 11-15
    • (2007) J. Biochem. , vol.142 , pp. 11-15
    • Hagiwara, M.1    Nojima, T.2
  • 19
    • 33646516400 scopus 로고    scopus 로고
    • Transport of messenger RNA from the nucleus to the cytoplasm
    • Cole C.N., and Scarcelli J.J. Transport of messenger RNA from the nucleus to the cytoplasm. Curr. Opin. Cell Biol. 18 (2006) 299-306
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 299-306
    • Cole, C.N.1    Scarcelli, J.J.2
  • 20
    • 33344471142 scopus 로고    scopus 로고
    • Regulation of gene expression by alternative untranslated regions
    • Hughes T.A. Regulation of gene expression by alternative untranslated regions. Trends Genet. 22 (2006) 119-122
    • (2006) Trends Genet. , vol.22 , pp. 119-122
    • Hughes, T.A.1
  • 21
    • 56549101959 scopus 로고    scopus 로고
    • Alternative isoform regulation in human tissue transcriptomes
    • Wang E.T., et al. Alternative isoform regulation in human tissue transcriptomes. Nature 456 (2008) 470-476
    • (2008) Nature , vol.456 , pp. 470-476
    • Wang, E.T.1
  • 22
    • 33644858553 scopus 로고    scopus 로고
    • The Muscleblind family of proteins: an emerging class of regulators of developmentally programmed alternative splicing
    • Pascual M., et al. The Muscleblind family of proteins: an emerging class of regulators of developmentally programmed alternative splicing. Differentiation 74 (2006) 65-80
    • (2006) Differentiation , vol.74 , pp. 65-80
    • Pascual, M.1
  • 23
    • 28544440718 scopus 로고    scopus 로고
    • RNA-dependent integrin α3 protein localization regulated by the Muscleblind-like protein MLP1
    • Adereth Y., et al. RNA-dependent integrin α3 protein localization regulated by the Muscleblind-like protein MLP1. Nat. Cell Biol. 7 (2005) 1240-1247
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1240-1247
    • Adereth, Y.1
  • 24
    • 13844312668 scopus 로고    scopus 로고
    • Zipcodes and postage stamps: mRNA localisation signals and their trans-acting binding proteins
    • Chabanon H., et al. Zipcodes and postage stamps: mRNA localisation signals and their trans-acting binding proteins. Brief. Funct. Genomics Proteomics 3 (2004) 240-256
    • (2004) Brief. Funct. Genomics Proteomics , vol.3 , pp. 240-256
    • Chabanon, H.1
  • 25
    • 34250735674 scopus 로고    scopus 로고
    • RNA regulons: coordination of post-transcriptional events
    • Keene J.D. RNA regulons: coordination of post-transcriptional events. Nat. Rev. Genet. 8 (2007) 533-543
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 533-543
    • Keene, J.D.1
  • 26
    • 0012928775 scopus 로고    scopus 로고
    • Gene regulation at the RNA layer: RNA binding proteins in intercellular signaling networks
    • Lasko P. Gene regulation at the RNA layer: RNA binding proteins in intercellular signaling networks. Sci. STKE 2003 (2003) re6
    • (2003) Sci. STKE , vol.2003
    • Lasko, P.1
  • 27
    • 42449098125 scopus 로고    scopus 로고
    • Splicing regulation: from a parts list of regulatory elements to an integrated splicing code
    • Wang Z., and Burge C.B. Splicing regulation: from a parts list of regulatory elements to an integrated splicing code. RNA 14 (2008) 802-813
    • (2008) RNA , vol.14 , pp. 802-813
    • Wang, Z.1    Burge, C.B.2
  • 28
    • 0034235156 scopus 로고    scopus 로고
    • Destabilization and mislocalization of myelin basic protein mRNAs in quaking dysmyelination lacking the QKI RNA-binding proteins
    • Li Z., et al. Destabilization and mislocalization of myelin basic protein mRNAs in quaking dysmyelination lacking the QKI RNA-binding proteins. J. Neurosci. 20 (2000) 4944-4953
    • (2000) J. Neurosci. , vol.20 , pp. 4944-4953
    • Li, Z.1
  • 29
    • 37049231008 scopus 로고
    • Mutant mice (quaking and jimpy) with deficient myelination in the central nervous system
    • Sidman R.L., et al. Mutant mice (quaking and jimpy) with deficient myelination in the central nervous system. Science 144 (1964) 309-311
    • (1964) Science , vol.144 , pp. 309-311
    • Sidman, R.L.1
  • 30
    • 35548940665 scopus 로고    scopus 로고
    • Neuronal regulation of alternative pre-mRNA splicing
    • Li Q., et al. Neuronal regulation of alternative pre-mRNA splicing. Nat. Rev. Neurosci. 8 (2007) 819-831
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 819-831
    • Li, Q.1
  • 31
    • 23044431574 scopus 로고    scopus 로고
    • Nova regulates brain-specific splicing to shape the synapse
    • Ule J., et al. Nova regulates brain-specific splicing to shape the synapse. Nat. Genet. 37 (2005) 844-852
    • (2005) Nat. Genet. , vol.37 , pp. 844-852
    • Ule, J.1
  • 32
    • 0033757702 scopus 로고    scopus 로고
    • Nova-1 regulates neuron-specific alternative splicing and is essential for neuronal viability
    • Jensen K.B., et al. Nova-1 regulates neuron-specific alternative splicing and is essential for neuronal viability. Neuron 25 (2000) 359-371
    • (2000) Neuron , vol.25 , pp. 359-371
    • Jensen, K.B.1
  • 33
    • 56549105330 scopus 로고    scopus 로고
    • HITS-CLIP yields genome-wide insights into brain alternative RNA processing
    • Licatalosi D.D., et al. HITS-CLIP yields genome-wide insights into brain alternative RNA processing. Nature 456 (2008) 464-469
    • (2008) Nature , vol.456 , pp. 464-469
    • Licatalosi, D.D.1
  • 34
    • 28044453909 scopus 로고    scopus 로고
    • RNA splicing capability of live neuronal dendrites
    • Glanzer J., et al. RNA splicing capability of live neuronal dendrites. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 16859-16864
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 16859-16864
    • Glanzer, J.1
  • 35
    • 41149085493 scopus 로고    scopus 로고
    • Ca channel intron-containing mRNAs contribute to the intrinsic excitability of hippocampal neurons
    • Ca channel intron-containing mRNAs contribute to the intrinsic excitability of hippocampal neurons. Proc. Natl. Acad. Sci. U. S. Am. 105 (2008) 1901-1906
    • (2008) Proc. Natl. Acad. Sci. U. S. Am. , vol.105 , pp. 1901-1906
    • Bell, T.J.1
  • 36
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
    • Le Hir H., et al. The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. EMBO J. 19 (2000) 6860-6869
    • (2000) EMBO J. , vol.19 , pp. 6860-6869
    • Le Hir, H.1
  • 37
    • 2342540912 scopus 로고    scopus 로고
    • The ever-increasing complexities of the exon junction complex
    • Tange T.O., et al. The ever-increasing complexities of the exon junction complex. Curr. Opin. Cell Biol. 16 (2004) 279-284
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 279-284
    • Tange, T.O.1
  • 38
    • 41949101770 scopus 로고    scopus 로고
    • SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs
    • Ma X.M., et al. SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs. Cell 133 (2008) 303-313
    • (2008) Cell , vol.133 , pp. 303-313
    • Ma, X.M.1
  • 39
    • 41949113083 scopus 로고    scopus 로고
    • Upf1 phosphorylation triggers translational repression during nonsense-mediated mRNA decay
    • Isken O., et al. Upf1 phosphorylation triggers translational repression during nonsense-mediated mRNA decay. Cell 133 (2008) 314-327
    • (2008) Cell , vol.133 , pp. 314-327
    • Isken, O.1
  • 40
    • 0035687504 scopus 로고    scopus 로고
    • The protein Mago provides a link between splicing and mRNA localization
    • Le Hir H., et al. The protein Mago provides a link between splicing and mRNA localization. EMBO Rep. 2 (2001) 1119-1124
    • (2001) EMBO Rep. , vol.2 , pp. 1119-1124
    • Le Hir, H.1
  • 41
    • 34447092677 scopus 로고    scopus 로고
    • The EJC factor eIF4AIII modulates synaptic strength and neuronal protein expression
    • Giorgi C., et al. The EJC factor eIF4AIII modulates synaptic strength and neuronal protein expression. Cell 130 (2007) 179-191
    • (2007) Cell , vol.130 , pp. 179-191
    • Giorgi, C.1
  • 42
    • 0035912719 scopus 로고    scopus 로고
    • A cellular mechanism for targeting newly synthesized mRNAs to synaptic sites on dendrites
    • Steward O., and Worley P.F. A cellular mechanism for targeting newly synthesized mRNAs to synaptic sites on dendrites. Proc. Natl. Acad. Sci. U. S. Am. 98 (2001) 7062-7068
    • (2001) Proc. Natl. Acad. Sci. U. S. Am. , vol.98 , pp. 7062-7068
    • Steward, O.1    Worley, P.F.2
  • 43
    • 0035036344 scopus 로고    scopus 로고
    • Selective targeting of newly synthesized Arc mRNA to active synapses requires NMDA receptor activation
    • Steward O., and Worley P.F. Selective targeting of newly synthesized Arc mRNA to active synapses requires NMDA receptor activation. Neuron 30 (2001) 227-240
    • (2001) Neuron , vol.30 , pp. 227-240
    • Steward, O.1    Worley, P.F.2
  • 44
    • 58149328474 scopus 로고    scopus 로고
    • The immediate early gene arc/arg3.1: regulation, mechanisms, and function
    • Bramham C.R., et al. The immediate early gene arc/arg3.1: regulation, mechanisms, and function. J. Neurosci. 28 (2008) 11760-11767
    • (2008) J. Neurosci. , vol.28 , pp. 11760-11767
    • Bramham, C.R.1
  • 45
    • 48149095822 scopus 로고    scopus 로고
    • Alternative splicing resulting in nonsense-mediated mRNA decay: what is the meaning of nonsense?
    • McGlincy N.J., and Smith C.W. Alternative splicing resulting in nonsense-mediated mRNA decay: what is the meaning of nonsense?. Trends Biochem. Sci. 33 (2008) 385-393
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 385-393
    • McGlincy, N.J.1    Smith, C.W.2
  • 46
    • 14044265166 scopus 로고    scopus 로고
    • Spatial exploration-induced Arc mRNA and protein expression: evidence for selective, network-specific reactivation
    • Ramirez-Amaya V., et al. Spatial exploration-induced Arc mRNA and protein expression: evidence for selective, network-specific reactivation. J. Neurosci. 25 (2005) 1761-1768
    • (2005) J. Neurosci. , vol.25 , pp. 1761-1768
    • Ramirez-Amaya, V.1
  • 47
    • 13744254695 scopus 로고    scopus 로고
    • A large-scale analysis of mRNA polyadenylation of human and mouse genes
    • Tian B., et al. A large-scale analysis of mRNA polyadenylation of human and mouse genes. Nucleic Acids Res. 33 (2005) 201-212
    • (2005) Nucleic Acids Res. , vol.33 , pp. 201-212
    • Tian, B.1
  • 48
    • 58149527754 scopus 로고    scopus 로고
    • Identification of gene 3′ ends by automated EST cluster analysis
    • Muro E.M., et al. Identification of gene 3′ ends by automated EST cluster analysis. Proc. Natl. Acad. Sci. U. S. Am. 105 (2008) 20286-20290
    • (2008) Proc. Natl. Acad. Sci. U. S. Am. , vol.105 , pp. 20286-20290
    • Muro, E.M.1
  • 49
    • 58149144383 scopus 로고    scopus 로고
    • Alternative polyadenylation: a twist on mRNA 3′ end formation
    • Lutz C.S. Alternative polyadenylation: a twist on mRNA 3′ end formation. ACS Chem. Biol. 3 (2008) 609-617
    • (2008) ACS Chem. Biol. , vol.3 , pp. 609-617
    • Lutz, C.S.1
  • 50
    • 33646950851 scopus 로고    scopus 로고
    • Biased alternative polyadenylation in human tissues
    • Zhang H., et al. Biased alternative polyadenylation in human tissues. Genome Biol. 6 (2005) R100
    • (2005) Genome Biol. , vol.6
    • Zhang, H.1
  • 51
    • 0037359267 scopus 로고    scopus 로고
    • BDNF and activity-dependent synaptic modulation
    • Lu B. BDNF and activity-dependent synaptic modulation. Learn. Mem. 10 (2003) 86-98
    • (2003) Learn. Mem. , vol.10 , pp. 86-98
    • Lu, B.1
  • 52
    • 0027402152 scopus 로고
    • Multiple promoters direct tissue-specific expression of the rat BDNF gene
    • Timmusk T., et al. Multiple promoters direct tissue-specific expression of the rat BDNF gene. Neuron 10 (1993) 475-489
    • (1993) Neuron , vol.10 , pp. 475-489
    • Timmusk, T.1
  • 53
    • 31144467231 scopus 로고    scopus 로고
    • Rodent BDNF genes, novel promoters, novel splice variants, and regulation by cocaine
    • Liu Q.R., et al. Rodent BDNF genes, novel promoters, novel splice variants, and regulation by cocaine. Brain Res. 1067 (2006) 1-12
    • (2006) Brain Res. , vol.1067 , pp. 1-12
    • Liu, Q.R.1
  • 54
    • 3342967633 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor mRNA and protein are targeted to discrete dendritic laminas by events that trigger epileptogenesis
    • Tongiorgi E., et al. Brain-derived neurotrophic factor mRNA and protein are targeted to discrete dendritic laminas by events that trigger epileptogenesis. J. Neurosci. 24 (2004) 6842-6852
    • (2004) J. Neurosci. , vol.24 , pp. 6842-6852
    • Tongiorgi, E.1
  • 55
    • 46149100739 scopus 로고    scopus 로고
    • Distinct role of long 3′ UTR BDNF mRNA in spine morphology and synaptic plasticity in hippocampal neurons
    • An J.J., et al. Distinct role of long 3′ UTR BDNF mRNA in spine morphology and synaptic plasticity in hippocampal neurons. Cell 134 (2008) 175-187
    • (2008) Cell , vol.134 , pp. 175-187
    • An, J.J.1
  • 56
    • 47749146105 scopus 로고    scopus 로고
    • Localized regulation of axonal RanGTPase controls retrograde injury signaling in peripheral nerve
    • Yudin D., et al. Localized regulation of axonal RanGTPase controls retrograde injury signaling in peripheral nerve. Neuron 59 (2008) 241-252
    • (2008) Neuron , vol.59 , pp. 241-252
    • Yudin, D.1
  • 57
    • 56049121431 scopus 로고    scopus 로고
    • MicroRNA-mediated up-regulation of an alternatively polyadenylated variant of the mouse cytoplasmic β-actin gene
    • Ghosh T., et al. MicroRNA-mediated up-regulation of an alternatively polyadenylated variant of the mouse cytoplasmic β-actin gene. Nucleic Acids Res. 36 (2008) 6318-6332
    • (2008) Nucleic Acids Res. , vol.36 , pp. 6318-6332
    • Ghosh, T.1
  • 58
    • 57649211993 scopus 로고    scopus 로고
    • Genome-wide analysis of MEF2 transcriptional program reveals synaptic target genes and neuronal activity-dependent polyadenylation site selection
    • Flavell S.W., et al. Genome-wide analysis of MEF2 transcriptional program reveals synaptic target genes and neuronal activity-dependent polyadenylation site selection. Neuron 60 (2008) 1022-1038
    • (2008) Neuron , vol.60 , pp. 1022-1038
    • Flavell, S.W.1
  • 59
    • 33144467591 scopus 로고    scopus 로고
    • Activity-dependent regulation of MEF2 transcription factors suppresses excitatory synapse number
    • Flavell S.W., et al. Activity-dependent regulation of MEF2 transcription factors suppresses excitatory synapse number. Science 311 (2006) 1008-1012
    • (2006) Science , vol.311 , pp. 1008-1012
    • Flavell, S.W.1
  • 60
    • 12344290346 scopus 로고    scopus 로고
    • Mechanisms of translational control by the 3′ UTR in development and differentiation
    • de Moor C.H., et al. Mechanisms of translational control by the 3′ UTR in development and differentiation. Semin. Cell Dev. Biol. 16 (2005) 49-58
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 49-58
    • de Moor, C.H.1
  • 61
    • 46249092601 scopus 로고    scopus 로고
    • Proliferating cells express mRNAs with shortened 3′ untranslated regions and fewer microRNA target sites
    • Sandberg R., et al. Proliferating cells express mRNAs with shortened 3′ untranslated regions and fewer microRNA target sites. Science 320 (2008) 1643-1647
    • (2008) Science , vol.320 , pp. 1643-1647
    • Sandberg, R.1
  • 62
    • 62649119218 scopus 로고    scopus 로고
    • Translational regulation of GluR2 mRNAs in rat hippocampus by alternative 3′ untranslated regions
    • Irier H.A., et al. Translational regulation of GluR2 mRNAs in rat hippocampus by alternative 3′ untranslated regions. J. Neurochem. 109 (2009) 584-594
    • (2009) J. Neurochem. , vol.109 , pp. 584-594
    • Irier, H.A.1
  • 63
    • 0028292005 scopus 로고
    • The organization of the gene for the functionally dominant α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor subunit GluR-B
    • Kohler M., et al. The organization of the gene for the functionally dominant α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor subunit GluR-B. J. Biol. Chem. 269 (1994) 17367-17370
    • (1994) J. Biol. Chem. , vol.269 , pp. 17367-17370
    • Kohler, M.1
  • 64
    • 0028029983 scopus 로고
    • CPEB is a specificity factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation
    • Hake L.E., and Richter J.D. CPEB is a specificity factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation. Cell 79 (1994) 617-627
    • (1994) Cell , vol.79 , pp. 617-627
    • Hake, L.E.1    Richter, J.D.2
  • 65
    • 0029998640 scopus 로고    scopus 로고
    • CPEB controls the cytoplasmic polyadenylation of cyclin, Cdk2 and c-mos mRNAs and is necessary for oocyte maturation in Xenopus
    • Stebbins-Boaz B., et al. CPEB controls the cytoplasmic polyadenylation of cyclin, Cdk2 and c-mos mRNAs and is necessary for oocyte maturation in Xenopus. EMBO J. 15 (1996) 2582-2592
    • (1996) EMBO J. , vol.15 , pp. 2582-2592
    • Stebbins-Boaz, B.1
  • 66
    • 41549097210 scopus 로고    scopus 로고
    • Translational control by cytoplasmic polyadenylation in Xenopus oocytes
    • Radford H.E., et al. Translational control by cytoplasmic polyadenylation in Xenopus oocytes. Biochim. Biophys. Acta 1779 (2008) 217-229
    • (2008) Biochim. Biophys. Acta , vol.1779 , pp. 217-229
    • Radford, H.E.1
  • 67
    • 34249908103 scopus 로고    scopus 로고
    • CPEB: a life in translation
    • Richter J.D. CPEB: a life in translation. Trends Biochem. Sci. 32 (2007) 279-285
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 279-285
    • Richter, J.D.1
  • 68
    • 63349111035 scopus 로고    scopus 로고
    • Cytoplasmic polyadenylation and cytoplasmic polyadenylation element-dependent mRNA regulation are involved in Xenopus retinal axon development
    • Lin A.C., et al. Cytoplasmic polyadenylation and cytoplasmic polyadenylation element-dependent mRNA regulation are involved in Xenopus retinal axon development. Neural Dev. 4 (2009) 8
    • (2009) Neural Dev. , vol.4 , pp. 8
    • Lin, A.C.1
  • 69
    • 0032215079 scopus 로고    scopus 로고
    • CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of α-CaMKII mRNA at synapses
    • Wu L., et al. CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of α-CaMKII mRNA at synapses. Neuron 21 (1998) 1129-1139
    • (1998) Neuron , vol.21 , pp. 1129-1139
    • Wu, L.1
  • 70
    • 0036565678 scopus 로고    scopus 로고
    • N-Methyl-D-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and αCaMKII mRNA polyadenylation at synapses
    • Huang Y.S., et al. N-Methyl-D-aspartate receptor signaling results in Aurora kinase-catalyzed CPEB phosphorylation and αCaMKII mRNA polyadenylation at synapses. EMBO J. 21 (2002) 2139-2148
    • (2002) EMBO J. , vol.21 , pp. 2139-2148
    • Huang, Y.S.1
  • 71
    • 24044462931 scopus 로고    scopus 로고
    • Activity-dependent polyadenylation in neurons
    • Du L., and Richter J.D. Activity-dependent polyadenylation in neurons. RNA 11 (2005) 1340-1347
    • (2005) RNA , vol.11 , pp. 1340-1347
    • Du, L.1    Richter, J.D.2
  • 72
    • 20444377630 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II and protein phosphatase 1 during hippocampal long-term potentiation
    • 2+/calmodulin-dependent protein kinase II and protein phosphatase 1 during hippocampal long-term potentiation. J. Neurosci. 25 (2005) 5604-5610
    • (2005) J. Neurosci. , vol.25 , pp. 5604-5610
    • Atkins, C.M.1
  • 73
    • 2642566171 scopus 로고    scopus 로고
    • Cytoplasmic polyadenylation element binding protein-dependent protein synthesis is regulated by calcium/calmodulin-dependent protein kinase II
    • Atkins C.M., et al. Cytoplasmic polyadenylation element binding protein-dependent protein synthesis is regulated by calcium/calmodulin-dependent protein kinase II. J Neurosci 24 (2004) 5193-5201
    • (2004) J Neurosci , vol.24 , pp. 5193-5201
    • Atkins, C.M.1
  • 74
    • 32044432375 scopus 로고    scopus 로고
    • Reduced extinction of hippocampal-dependent memories in CPEB knockout mice
    • Berger-Sweeney J., et al. Reduced extinction of hippocampal-dependent memories in CPEB knockout mice. Learn. Mem. 13 (2006) 4-7
    • (2006) Learn. Mem. , vol.13 , pp. 4-7
    • Berger-Sweeney, J.1
  • 75
    • 55749109386 scopus 로고    scopus 로고
    • GLD2 poly(A) polymerase is required for long-term memory
    • Kwak J.E., et al. GLD2 poly(A) polymerase is required for long-term memory. Proc. Natl. Acad. Sci. U. S. Am. 105 (2008) 14644-14649
    • (2008) Proc. Natl. Acad. Sci. U. S. Am. , vol.105 , pp. 14644-14649
    • Kwak, J.E.1
  • 76
    • 38849190013 scopus 로고    scopus 로고
    • A combinatorial code for CPE-mediated translational control
    • Pique M., et al. A combinatorial code for CPE-mediated translational control. Cell 132 (2008) 434-448
    • (2008) Cell , vol.132 , pp. 434-448
    • Pique, M.1
  • 77
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: design principles of a dynamic RNP machine
    • Wahl M.C., et al. The spliceosome: design principles of a dynamic RNP machine. Cell 136 (2009) 701-718
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1
  • 78
    • 58249093940 scopus 로고    scopus 로고
    • The SR protein family of splicing factors: master regulators of gene expression
    • Long J.C., and Caceres J.F. The SR protein family of splicing factors: master regulators of gene expression. Biochem. J 417 (2009) 15-27
    • (2009) Biochem. J , vol.417 , pp. 15-27
    • Long, J.C.1    Caceres, J.F.2
  • 79
    • 49349112872 scopus 로고    scopus 로고
    • Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein
    • Sawicka K., et al. Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein. Biochem. Soc. Trans. 36 (2008) 641-647
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 641-647
    • Sawicka, K.1
  • 80
    • 34347384211 scopus 로고    scopus 로고
    • A post-transcriptional regulatory switch in polypyrimidine tract-binding proteins reprograms alternative splicing in developing neurons
    • Boutz P.L., et al. A post-transcriptional regulatory switch in polypyrimidine tract-binding proteins reprograms alternative splicing in developing neurons. Genes Dev. 21 (2007) 1636-1652
    • (2007) Genes Dev. , vol.21 , pp. 1636-1652
    • Boutz, P.L.1
  • 81
    • 34250688780 scopus 로고    scopus 로고
    • Developing global insight into RNA regulation
    • Darnell R.B. Developing global insight into RNA regulation. Cold Spring Harb. Symp. Quant. Biol. 71 (2006) 321-327
    • (2006) Cold Spring Harb. Symp. Quant. Biol. , vol.71 , pp. 321-327
    • Darnell, R.B.1
  • 82
    • 33845380816 scopus 로고    scopus 로고
    • A nuclear function of Hu proteins as neuron-specific alternative RNA processing regulators
    • Zhu H., et al. A nuclear function of Hu proteins as neuron-specific alternative RNA processing regulators. Mol. Biol. Cell 17 (2006) 5105-5114
    • (2006) Mol. Biol. Cell , vol.17 , pp. 5105-5114
    • Zhu, H.1
  • 83
    • 27644455141 scopus 로고    scopus 로고
    • Homologues of the Caenorhabditis elegans Fox-1 protein are neuronal splicing regulators in mammals
    • Underwood J.G., et al. Homologues of the Caenorhabditis elegans Fox-1 protein are neuronal splicing regulators in mammals. Mol. Cell. Biol. 25 (2005) 10005-10016
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10005-10016
    • Underwood, J.G.1
  • 84
    • 51949111100 scopus 로고    scopus 로고
    • Defining the regulatory network of the tissue-specific splicing factors Fox-1 and Fox-2
    • Zhang C., et al. Defining the regulatory network of the tissue-specific splicing factors Fox-1 and Fox-2. Genes Dev. 22 (2008) 2550-2563
    • (2008) Genes Dev. , vol.22 , pp. 2550-2563
    • Zhang, C.1
  • 85
    • 42449084129 scopus 로고    scopus 로고
    • Protein factors in pre-mRNA 3′-end processing
    • Mandel C.R., et al. Protein factors in pre-mRNA 3′-end processing. Cell. Mol. Life Sci. 65 (2008) 1099-1122
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1099-1122
    • Mandel, C.R.1
  • 86
    • 48349091628 scopus 로고    scopus 로고
    • Finishing touches: post-translational modification of protein factors involved in mammalian pre-mRNA 3′ end formation
    • Ryan K., and Bauer D.L. Finishing touches: post-translational modification of protein factors involved in mammalian pre-mRNA 3′ end formation. Int. J. Biochem. Cell Biol. 40 (2008) 2384-2396
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 2384-2396
    • Ryan, K.1    Bauer, D.L.2
  • 87
    • 19344367418 scopus 로고    scopus 로고
    • Formation of export-competent mRNP: escaping nuclear destruction
    • Saguez C., et al. Formation of export-competent mRNP: escaping nuclear destruction. Curr. Opin. Cell Biol. 17 (2005) 287-293
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 287-293
    • Saguez, C.1
  • 88
    • 58149103297 scopus 로고    scopus 로고
    • Deadenylation is a widespread effect of miRNA regulation
    • Eulalio A., et al. Deadenylation is a widespread effect of miRNA regulation. RNA 15 (2009) 21-32
    • (2009) RNA , vol.15 , pp. 21-32
    • Eulalio, A.1
  • 89
    • 56849103665 scopus 로고    scopus 로고
    • The control of mRNA decapping and P-body formation
    • Franks T.M., and Lykke-Andersen J. The control of mRNA decapping and P-body formation. Mol. Cell 32 (2008) 605-615
    • (2008) Mol. Cell , vol.32 , pp. 605-615
    • Franks, T.M.1    Lykke-Andersen, J.2
  • 90
    • 60149090021 scopus 로고    scopus 로고
    • The many pathways of RNA degradation
    • Houseley J., and Tollervey D. The many pathways of RNA degradation. Cell 136 (2009) 763-776
    • (2009) Cell , vol.136 , pp. 763-776
    • Houseley, J.1    Tollervey, D.2
  • 91
    • 33749662940 scopus 로고    scopus 로고
    • Opposing polymerase-deadenylase activities regulate cytoplasmic polyadenylation
    • Kim J.H., and Richter J.D. Opposing polymerase-deadenylase activities regulate cytoplasmic polyadenylation. Mol. Cell 24 (2006) 173-183
    • (2006) Mol. Cell , vol.24 , pp. 173-183
    • Kim, J.H.1    Richter, J.D.2
  • 92
    • 0037007233 scopus 로고    scopus 로고
    • Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction
    • Mendez R., et al. Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction. EMBO J. 21 (2002) 1833-1844
    • (2002) EMBO J. , vol.21 , pp. 1833-1844
    • Mendez, R.1
  • 93
    • 33646865953 scopus 로고    scopus 로고
    • Translational control by neuroguidin, a eukaryotic initiation factor 4E and CPEB binding protein
    • Jung M.Y., et al. Translational control by neuroguidin, a eukaryotic initiation factor 4E and CPEB binding protein. Mol. Cell. Biol. 26 (2006) 4277-4287
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 4277-4287
    • Jung, M.Y.1
  • 94
    • 0344824639 scopus 로고    scopus 로고
    • Localization of a β-actin messenger ribonucleoprotein complex with zipcode-binding protein modulates the density of dendritic filopodia and filopodial synapses
    • Eom T., et al. Localization of a β-actin messenger ribonucleoprotein complex with zipcode-binding protein modulates the density of dendritic filopodia and filopodial synapses. J. Neurosci. 23 (2003) 10433-10444
    • (2003) J. Neurosci. , vol.23 , pp. 10433-10444
    • Eom, T.1
  • 95
    • 29344473716 scopus 로고    scopus 로고
    • Identification of a cis-acting element required for dendritic targeting of activity-regulated cytoskeleton-associated protein mRNA
    • Kobayashi H., et al. Identification of a cis-acting element required for dendritic targeting of activity-regulated cytoskeleton-associated protein mRNA. Eur. J. Neurosci. 22 (2005) 2977-2984
    • (2005) Eur. J. Neurosci. , vol.22 , pp. 2977-2984
    • Kobayashi, H.1
  • 96
    • 0034965509 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II
    • 2+/calmodulin-dependent protein kinase II. Eur. J. Neurosci. 13 (2001) 1881-1888
    • (2001) Eur. J. Neurosci. , vol.13 , pp. 1881-1888
    • Blichenberg, A.1
  • 97
    • 0033769356 scopus 로고    scopus 로고
    • Two cis-acting elements in the 3′ untranslated region of α-CaMKII regulate its dendritic targeting
    • Mori Y., et al. Two cis-acting elements in the 3′ untranslated region of α-CaMKII regulate its dendritic targeting. Nat. Neurosci. 3 (2000) 1079-1084
    • (2000) Nat. Neurosci. , vol.3 , pp. 1079-1084
    • Mori, Y.1
  • 98
    • 33644788009 scopus 로고    scopus 로고
    • Postsynaptic recruitment of Dendrin depends on both dendritic mRNA transport and synaptic anchoring
    • Kremerskothen J., et al. Postsynaptic recruitment of Dendrin depends on both dendritic mRNA transport and synaptic anchoring. J. Neurochem. 96 (2006) 1659-1666
    • (2006) J. Neurochem. , vol.96 , pp. 1659-1666
    • Kremerskothen, J.1
  • 99
    • 28044452414 scopus 로고    scopus 로고
    • Hzf protein regulates dendritic localization and BDNF-induced translation of type 1 inositol 1,4,5-trisphosphate receptor mRNA
    • Iijima T., et al. Hzf protein regulates dendritic localization and BDNF-induced translation of type 1 inositol 1,4,5-trisphosphate receptor mRNA. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17190-17195
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 17190-17195
    • Iijima, T.1
  • 100
    • 0033570305 scopus 로고    scopus 로고
    • Identification of a cis-acting dendritic targeting element in MAP2 mRNAs
    • Blichenberg A., et al. Identification of a cis-acting dendritic targeting element in MAP2 mRNAs. J. Neurosci. 19 (1999) 8818-8829
    • (1999) J. Neurosci. , vol.19 , pp. 8818-8829
    • Blichenberg, A.1
  • 101
    • 43449111190 scopus 로고    scopus 로고
    • Spatial regulation of nanos is required for its function in dendrite morphogenesis
    • Brechbiel J.L., and Gavis E.R. Spatial regulation of nanos is required for its function in dendrite morphogenesis. Curr. Biol. 18 (2008) 745-750
    • (2008) Curr. Biol. , vol.18 , pp. 745-750
    • Brechbiel, J.L.1    Gavis, E.R.2
  • 102
    • 10744230884 scopus 로고    scopus 로고
    • Selective dendrite-targeting of mRNAs of NR1 splice variants without exon 5: identification of a cis-acting sequence and isolation of sequence-binding proteins
    • Pal R., et al. Selective dendrite-targeting of mRNAs of NR1 splice variants without exon 5: identification of a cis-acting sequence and isolation of sequence-binding proteins. Brain Res. 994 (2003) 1-18
    • (2003) Brain Res. , vol.994 , pp. 1-18
    • Pal, R.1
  • 103
    • 10644248874 scopus 로고    scopus 로고
    • Dendritic transport and localization of protein kinase Mζ mRNA: implications for molecular memory consolidation
    • Muslimov I.A., et al. Dendritic transport and localization of protein kinase Mζ mRNA: implications for molecular memory consolidation. J. Biol. Chem. 279 (2004) 52613-52622
    • (2004) J. Biol. Chem. , vol.279 , pp. 52613-52622
    • Muslimov, I.A.1
  • 104
    • 23944433636 scopus 로고    scopus 로고
    • Local translation of RhoA regulates growth cone collapse
    • Wu K.Y., et al. Local translation of RhoA regulates growth cone collapse. Nature 436 (2005) 1020-1024
    • (2005) Nature , vol.436 , pp. 1020-1024
    • Wu, K.Y.1
  • 105
    • 17144466355 scopus 로고    scopus 로고
    • Differential expression and dendritic transcript localization of Shank family members: identification of a dendritic targeting element in the 3′ untranslated region of Shank1 mRNA
    • Bockers T.M., et al. Differential expression and dendritic transcript localization of Shank family members: identification of a dendritic targeting element in the 3′ untranslated region of Shank1 mRNA. Mol. Cell. Neurosci. 26 (2004) 182-190
    • (2004) Mol. Cell. Neurosci. , vol.26 , pp. 182-190
    • Bockers, T.M.1
  • 106
    • 33646946209 scopus 로고    scopus 로고
    • Two mRNA-binding proteins regulate the distribution of syntaxin mRNA in Aplysia sensory neurons
    • Liu J., et al. Two mRNA-binding proteins regulate the distribution of syntaxin mRNA in Aplysia sensory neurons. J. Neurosci. 26 (2006) 5204-5214
    • (2006) J. Neurosci. , vol.26 , pp. 5204-5214
    • Liu, J.1
  • 107
    • 0028914641 scopus 로고
    • cis-Acting signals and trans-acting proteins are involved in tau mRNA targeting into neurites of differentiating neuronal cells
    • Behar L., et al. cis-Acting signals and trans-acting proteins are involved in tau mRNA targeting into neurites of differentiating neuronal cells. Int. J. Dev. Neurosci. 13 (1995) 113-127
    • (1995) Int. J. Dev. Neurosci. , vol.13 , pp. 113-127
    • Behar, L.1
  • 108
    • 0030954897 scopus 로고    scopus 로고
    • Dendritic localization of rat vasopressin mRNA: ultrastructural analysis and mapping of targeting elements
    • Prakash N., et al. Dendritic localization of rat vasopressin mRNA: ultrastructural analysis and mapping of targeting elements. Eur. J. Neurosci. 9 (1997) 523-532
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 523-532
    • Prakash, N.1
  • 109
    • 0037338218 scopus 로고    scopus 로고
    • Facilitation of dendritic mRNA transport by CPEB
    • Huang Y.S., et al. Facilitation of dendritic mRNA transport by CPEB. Genes Dev. 17 (2003) 638-653
    • (2003) Genes Dev. , vol.17 , pp. 638-653
    • Huang, Y.S.1
  • 110
    • 0034705448 scopus 로고    scopus 로고
    • Two trans-acting rat-brain proteins, MARTA1 and MARTA2, interact specifically with the dendritic targeting element in MAP2 mRNAs
    • Rehbein M., et al. Two trans-acting rat-brain proteins, MARTA1 and MARTA2, interact specifically with the dendritic targeting element in MAP2 mRNAs. Mol. Brain Res. 79 (2000) 192-201
    • (2000) Mol. Brain Res. , vol.79 , pp. 192-201
    • Rehbein, M.1
  • 111
    • 9444291294 scopus 로고    scopus 로고
    • Ilf3 and NF90 associate with the axonal targeting element of Tau mRNA
    • Larcher J.C., et al. Ilf3 and NF90 associate with the axonal targeting element of Tau mRNA. FASEB J. 18 (2004) 1761-1763
    • (2004) FASEB J. , vol.18 , pp. 1761-1763
    • Larcher, J.C.1
  • 112
    • 0035912740 scopus 로고    scopus 로고
    • Vasopressin mRNA localization in nerve cells: characterization of cis-acting elements and trans-acting factors
    • Mohr E., et al. Vasopressin mRNA localization in nerve cells: characterization of cis-acting elements and trans-acting factors. Proc. Natl. Acad. Sci. U. S. Am. 98 (2001) 7072-7079
    • (2001) Proc. Natl. Acad. Sci. U. S. Am. , vol.98 , pp. 7072-7079
    • Mohr, E.1


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