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REF, an evolutionary conserved family of hnRNP-like proteins, interacts with TAP/Mex67p and participates in mRNA nuclear export
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This report shows that RNAi knockdown in Drosophila cells of the EJC protein REF/Aly as well as several other EJC factors yields no significant nuclear accumulation of polyA RNA, suggesting that these proteins are not essential for mRNA export. However, codepletion of RNPS1 and REF/Aly or all EJC proteins at the same time does lead to some nuclear RNA accumulation, indicating that these factors can enhance mRNA export.
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This study uses RNAi in C. elegans to demonstrate that all known REF isoforms are dispensable for mRNA export and normal development, whereas NXF1/Tap is essential.
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Longman D., Johnstone I.L., Caceres J.F. The Ref/Aly proteins are dispensable for mRNA export and development in Caenorhabditis elegans. RNA. 9:2003;881-891 This study uses RNAi in C. elegans to demonstrate that all known REF isoforms are dispensable for mRNA export and normal development, whereas NXF1/Tap is essential.
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Longman, D.1
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UAP56 levels affect viability and mRNA export in Caenorhabditis elegans
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MacMorris M., Brocker C., Blumenthal T. UAP56 levels affect viability and mRNA export in Caenorhabditis elegans. RNA. 9:2003;847-857
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The RNA-binding protein Tsunagi interacts with Mago Nashi to establish polarity and localize oskar mRNA during Drosophila oogenesis
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Mohr S.E., Dillon S.T., Boswell R.E. The RNA-binding protein Tsunagi interacts with Mago Nashi to establish polarity and localize oskar mRNA during Drosophila oogenesis. Genes Dev. 15:2001;2886-2899
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Hachet O., Ephrussi A. Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport. Curr Biol. 11:2001;1666-1674
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Palacios I.M. RNA processing: splicing and the cytoplasmic localisation of mRNA. Curr Biol. 12:2002;R50-R52
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Steward O., Schuman E.M. Compartmentalized synthesis and degradation of proteins in neurons. Neuron. 40:2003;347-359
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Analysis of the stimulatory effect of splicing on mRNA production and utilization in mammalian cells
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Lu, S.1
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A quantitative analysis of intron effects on mammalian gene expression
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••] report quantitative analyses of the effects of splicing on various steps in gene expression and suggest that, in addition to stimulating mRNA production, splicing enhances the amount of protein produced per mRNA molecule.
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••] report quantitative analyses of the effects of splicing on various steps in gene expression and suggest that, in addition to stimulating mRNA production, splicing enhances the amount of protein produced per mRNA molecule.
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Nott, A.1
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An intron is required for dihydrofolate reductase protein stability
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Noe V., MacKenzie S., Ciudad C.J. An intron is required for dihydrofolate reductase protein stability. J Biol Chem. 278:2003;38292-38300
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0141706348
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This study demonstrates that deposition of an EJC is important for the enhanced translation of spliced mRNA in mammalian cells using short first-exon β-globin constructs. It additionally shows that tethering RNPS1 or SRm160 to intronless β-globin mRNA results in efficient translation of the mRNA. Other experiments clearly demonstrate that the EJC-dependent enhancement in mRNA translation is an effect distinct from EJC-dependent mRNA export.
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Wiegand H.L., Lu S., Cullen B.R. Exon junction complexes mediate the enhancing effect of splicing on mRNA expression. Proc Natl Acad Sci USA. 100:2003;11327-11332 This study demonstrates that deposition of an EJC is important for the enhanced translation of spliced mRNA in mammalian cells using short first-exon β-globin constructs. It additionally shows that tethering RNPS1 or SRm160 to intronless β-globin mRNA results in efficient translation of the mRNA. Other experiments clearly demonstrate that the EJC-dependent enhancement in mRNA translation is an effect distinct from EJC-dependent mRNA export.
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Proc Natl Acad Sci USA
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55
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This study shows that the splicing-dependent enhancement of mRNA translation is due to EJC deposition and, in mammalian cells, correlates with a greater percentage of spliced mRNAs being associated with polysomes. Tethering of the EJC proteins Y14, Magoh and RNPS1 or of the Upf proteins Upf1, Upf2 and Upf3b leads to enhanced translation of intronless mRNAs and also correlates with enhanced polysome association.
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Nott A., Le Hir H., Moore M.J. Splicing enhances translation in mammalian cells: an additional function of the exon junction complex. Genes Dev. 18:2004;210-222 This study shows that the splicing-dependent enhancement of mRNA translation is due to EJC deposition and, in mammalian cells, correlates with a greater percentage of spliced mRNAs being associated with polysomes. Tethering of the EJC proteins Y14, Magoh and RNPS1 or of the Upf proteins Upf1, Upf2 and Upf3b leads to enhanced translation of intronless mRNAs and also correlates with enhanced polysome association.
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Schell T, Kulozik AE, Hentze MW: Integration of splicing, transport and translation to achieve mRNA quality control by the nonsense-mediated decay pathway. Genome Biol 2002, 3:REVIEWS1006.
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Culbertson M.R., Leeds P.F. Looking at mRNA decay pathways through the window of molecular evolution. Curr Opin Genet Dev. 13:2003;207-214
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Lykke-Andersen J., Shu M.D., Steitz J.A. Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1. Science. 293:2001;1836-1839
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Y14 and hUpf3b form an NMD-activating complex
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Using the λN - boxB tethering system, more robust Y14-tethered NMD than was previously reported by Lykke-Andersen et al. [58] is demonstrated. Furthermore, Y14 and a conserved amino acid stretch in Upf3b that interacts directly or indirectly with Y14 is essential for Upf3b-tethered NMD.
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Gehring N.H., Neu-Yilik G., Schell T., Hentze M.W., Kulozik A.E. Y14 and hUpf3b form an NMD-activating complex. Mol Cell. 11:2003;939-949 Using the λN - boxB tethering system, more robust Y14-tethered NMD than was previously reported by Lykke-Andersen, et al. [58] is demonstrated. Furthermore, Y14 and a conserved amino acid stretch in Upf3b that interacts directly or indirectly with Y14 is essential for Upf3b-tethered NMD.
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Mol Cell
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Gehring, N.H.1
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Lykke-Andersen J. Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay. Mol Cell Biol. 22:2002;8114-8121
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Chen C.Y., Shyu A.B. Rapid deadenylation triggered by a nonsense codon precedes decay of the RNA body in a mammalian cytoplasmic nonsense-mediated decay pathway. Mol Cell Biol. 23:2003;4805-4813
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Lejeune F., Li X., Maquat L.E. Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Mol Cell. 12:2003;675-687
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Gonzalez C.I., Bhattacharya A., Wang W., Peltz S.W. Nonsense-mediated mRNA decay in Saccharomyces cerevisiae. Gene. 274:2001;15-25
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64
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0042025014
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Nonsense-mediated mRNA decay in Drosophila: At the intersection of the yeast and mammalian pathways
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In this study, it is found that NMD occurs independently of splicing in Drosophila and that RNAi knockdown of several EJC proteins fails to abrogate NMD. Thus, Drosophila NMD seems to be more yeast-like than mammal-like in its mode of PTC recognition.
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Gatfield D., Unterholzner L., Ciccarelli F.D., Bork P., Izaurralde E. Nonsense-mediated mRNA decay in Drosophila: at the intersection of the yeast and mammalian pathways. EMBO J. 22:2003;3960-3970 In this study, it is found that NMD occurs independently of splicing in Drosophila and that RNAi knockdown of several EJC proteins fails to abrogate NMD. Thus, Drosophila NMD seems to be more yeast-like than mammal-like in its mode of PTC recognition.
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EMBO J
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Gatfield, D.1
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