메뉴 건너뛰기




Volumn 3, Issue 3, 2002, Pages 195-205

Messenger-RNA-binding proteins and the messages they carry

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 1; MESSENGER RNA; MESSENGER RNA PRECURSOR; RNA BINDING PROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; MESSENGER RIBONUCLEOPROTEIN; RIBONUCLEOPROTEIN;

EID: 0036512117     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm760     Document Type: Review
Times cited : (1226)

References (163)
  • 2
    • 0033153348 scopus 로고    scopus 로고
    • hnRNP complexes: Composition, structure, and function
    • Krecic, A. M. & Swanson, M. S. hnRNP complexes: composition, structure, and function. Curr. Opin. Cell Biol. 11, 363-371 (1999).
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 363-371
    • Krecic, A.M.1    Swanson, M.S.2
  • 3
    • 0034697972 scopus 로고    scopus 로고
    • The double lives of shutting mRNA binding proteins
    • Shyu, A. B. & Wilkinson, M. F. The double lives of shutting mRNA binding proteins. Cell 102, 135-138 (2000).
    • (2000) Cell , vol.102 , pp. 135-138
    • Shyu, A.B.1    Wilkinson, M.F.2
  • 4
    • 0028881190 scopus 로고
    • Cell type-specific expression of hnRNP proteins
    • Kamma, H., Portman, D. S. & Dreyfuss, G. Cell type-specific expression of hnRNP proteins. Exp. Cell Res. 221, 187-196 (1995).
    • (1995) Exp. Cell Res. , vol.221 , pp. 187-196
    • Kamma, H.1    Portman, D.S.2    Dreyfuss, G.3
  • 5
    • 0344074646 scopus 로고    scopus 로고
    • Regulated tissue-specific expression of antagonistic pre-mRNA splicing factors
    • Hanamura, A., Caceres, J. F., Mayeda, A., Franza, B. R. Jr & Krainer, A. R. Regulated tissue-specific expression of antagonistic pre-mRNA splicing factors. RNA 4, 430-444 (1998).
    • (1998) RNA , vol.4 , pp. 430-444
    • Hanamura, A.1    Caceres, J.F.2    Mayeda, A.3    Franza B.R., Jr.4    Krainer, A.R.5
  • 6
    • 0033800453 scopus 로고    scopus 로고
    • Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein
    • Markovtsov, V. et al. Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein. Mol. Cell. Biol. 20, 7463-7479 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7463-7479
    • Markovtsov, V.1
  • 7
    • 0024835141 scopus 로고
    • A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts
    • Pinol-Roma, S., Swanson, M. S., Gall, J. G. & Dreyfuss, G. A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts. J. Cell Biol. 109, 2575-2587 (1989).
    • (1989) J. Cell Biol. , vol.109 , pp. 2575-2587
    • Pinol-Roma, S.1    Swanson, M.S.2    Gall, J.G.3    Dreyfuss, G.4
  • 8
    • 0007570010 scopus 로고    scopus 로고
    • The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation
    • Van der Houven van Oordt, W. et al. The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation. J. Cell Biol. 149, 307-316 (2000). This study shows that the MKK(3/6)-p38 pathway can mediate the cytoplasmic accumulation of hnRNP A1, and indicates that signal transduction mechanisms can regulate pre-mRNA splicing in vivo.
    • (2000) J. Cell Biol. , vol.149 , pp. 307-316
    • Van der Houven van Oordt, W.1
  • 9
    • 0035971083 scopus 로고    scopus 로고
    • Growth factors regulate heterogeneous nuclear ribonucleoprotein K expression and function
    • Mandal, M. et al. Growth factors regulate heterogeneous nuclear ribonucleoprotein K expression and function. J. Biol. Chem. 276, 9699-9704 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 9699-9704
    • Mandal, M.1
  • 10
    • 0035095885 scopus 로고    scopus 로고
    • ERK phosphorylation drives cytoplasmic accumulation of hnRNP-K and inhibition of mRNA translation
    • Habelhah, H. et al. ERK phosphorylation drives cytoplasmic accumulation of hnRNP-K and inhibition of mRNA translation. Nature Cell Biol. 3, 325-330 (2001). This study shows that hnRNP K is phosphorylated by mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) both in vitro and in vivo. This phosphorylation leads to the cytoplasmic localization of hnRNP K, which is required for its ability to silence mRNA translation. These findings indicate a role for hnRNP proteins in signal-transduction pathways.
    • (2001) Nature Cell Biol. , vol.3 , pp. 325-330
    • Habelhah, H.1
  • 11
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd, C. G. & Dreyfuss, G. Conserved structures and diversity of functions of RNA-binding proteins. Science 265, 615-621 (1994).
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 12
    • 0028930155 scopus 로고
    • A nuclear localization domain in the hnRNP A1 protein
    • Siomi, H. & Dreyfuss, G. A nuclear localization domain in the hnRNP A1 protein. J. Cell Biol. 129, 551-560 (1995).
    • (1995) J. Cell Biol. , vol.129 , pp. 551-560
    • Siomi, H.1    Dreyfuss, G.2
  • 13
    • 0028845313 scopus 로고
    • A nuclear export signal in hnRNP A1: A signal-mediated, temperature-dependent nuclear protein export pathway
    • Michael, W. M., Choi, M. & Dreyfuss, G. A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway. Cell 83, 415-422 (1995).
    • (1995) Cell , vol.83 , pp. 415-422
    • Michael, W.M.1    Choi, M.2    Dreyfuss, G.3
  • 14
    • 0028963968 scopus 로고
    • Nucleo-cytoplasmic distribution of human hnRNP proteins: A search for the targeting domains in hnRNP A1
    • Weighardt, F., Biamonti, G. & Riva, S. Nucleo-cytoplasmic distribution of human hnRNP proteins: a search for the targeting domains in hnRNP A1. J. Cell Sci. 108, 545-555 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 545-555
    • Weighardt, F.1    Biamonti, G.2    Riva, S.3
  • 15
    • 0028905957 scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K is a DNA-binding transactivator
    • Tomonaga, T. & Levens, D. Heterogeneous nuclear ribonucleoprotein K is a DNA-binding transactivator. J. Biol. Chem. 270, 4875-4881 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 4875-4881
    • Tomonaga, T.1    Levens, D.2
  • 16
  • 17
    • 0032584731 scopus 로고    scopus 로고
    • Differential effects of heterogeneous nuclear ribonucleoprotein K on Sp1- and Sp3-mediated transcriptional activation of a neuronal nicotinic acetylcholine receptor promoter
    • Du, Q., Melnikova, I. N. & Gardner, P. D. Differential effects of heterogeneous nuclear ribonucleoprotein K on Sp1- and Sp3-mediated transcriptional activation of a neuronal nicotinic acetylcholine receptor promoter. J. Biol. Chem. 278, 19877-19883 (1998).
    • (1998) J. Biol. Chem. , vol.278 , pp. 19877-19883
    • Du, Q.1    Melnikova, I.N.2    Gardner, P.D.3
  • 18
    • 0032562765 scopus 로고    scopus 로고
    • Identification of heterogeneous nuclear ribonucleoprotein K (hnRNP K) as a repressor of C/EBPβ-mediated gene activation
    • Miau, L. H., Chang, C. J., Shen, B. J., Tsai, W. H. & Lee, S. C. Identification of heterogeneous nuclear ribonucleoprotein K (hnRNP K) as a repressor of C/EBPβ-mediated gene activation. J. Biol. Chem. 278, 10784-10791 (1998).
    • (1998) J. Biol. Chem. , vol.278 , pp. 10784-10791
    • Miau, L.H.1    Chang, C.J.2    Shen, B.J.3    Tsai, W.H.4    Lee, S.C.5
  • 19
    • 0027263365 scopus 로고
    • Nuclear proteins that bind the pre-mRNA 3′ splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n
    • Ishikawa, F., Matunis, M. J., Dreyfuss, G. & Cech, T. R. Nuclear proteins that bind the pre-mRNA 3′ splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n. Mol. Cell. Biol. 13, 4301-4310 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4301-4310
    • Ishikawa, F.1    Matunis, M.J.2    Dreyfuss, G.3    Cech, T.R.4
  • 20
    • 0031800617 scopus 로고    scopus 로고
    • Telomere elongation by hnRNP A1 and a derivative that interacts with telomeric repeats and telomerase
    • La Branche, H. et al. Telomere elongation by hnRNP A1 and a derivative that interacts with telomeric repeats and telomerase. Nature Genet. 19, 199-202 (1998).
    • (1998) Nature Genet. , vol.19 , pp. 199-202
    • La Branche, H.1
  • 21
    • 0033927902 scopus 로고    scopus 로고
    • In vitro properties of the conserved mammalian protein hnRNP D suggest a role in telomere maintenance
    • Eversole, A. & Maizels, N. In vitro properties of the conserved mammalian protein hnRNP D suggest a role in telomere maintenance. Mol. Cell. Biol. 20, 5425-5432 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5425-5432
    • Eversole, A.1    Maizels, N.2
  • 22
    • 0035368412 scopus 로고    scopus 로고
    • hnRNP A1 may interact simultaneously with telomeric DNA and the human telomerase RNA in vitro
    • Fiset, S. & Chabot, B. hnRNP A1 may interact simultaneously with telomeric DNA and the human telomerase RNA in vitro. Nucleic Acids Res. 29, 2268-2275 (2001).
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2268-2275
    • Fiset, S.1    Chabot, B.2
  • 23
    • 0033534467 scopus 로고    scopus 로고
    • G4 DNA binding by LR1 and its subunits, nucleolin and hnRNP D. A role for G-G pairing in immunoglobulin switch recombination
    • Dempsey, L. A., Sun, H., Hanakahi, L. A. & Maizels, N. G4 DNA binding by LR1 and its subunits, nucleolin and hnRNP D. A role for G-G pairing in immunoglobulin switch recombination. J. Biol. Chem. 274, 1066-1071 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 1066-1071
    • Dempsey, L.A.1    Sun, H.2    Hanakahi, L.A.3    Maizels, N.4
  • 24
    • 0026543785 scopus 로고
    • Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2
    • Mayeda, A. & Krainer, A. R. Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2. Cell 68, 365-375 (1992). This paper reports that the relative concentrations of hnRNP A1 and the essential splicing factor SF2 modulate 5′ splice site selection in vitro.
    • (1992) Cell , vol.68 , pp. 365-375
    • Mayeda, A.1    Krainer, A.R.2
  • 25
    • 0028077730 scopus 로고
    • Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors
    • Caceres, J. F., Stamm, S., Helfman, D. M. & Krainer, A. R. Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors. Science 265, 1706-1709 (1994).
    • (1994) Science , vol.265 , pp. 1706-1709
    • Caceres, J.F.1    Stamm, S.2    Helfman, D.M.3    Krainer, A.R.4
  • 26
    • 0028178987 scopus 로고
    • The A1 and A1B proteins of heterogeneous nuclear ribonucleoparticles modulate 5′ splice site selection in vivo
    • Yang, X. et al. The A1 and A1B proteins of heterogeneous nuclear ribonucleoparticles modulate 5′ splice site selection in vivo. Proc. Natl Acad. Sci. USA 91, 6924-6928 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6924-6928
    • Yang, X.1
  • 27
    • 0028867814 scopus 로고
    • The generally expressed hnRNP F is involved in a neural-specific pre-mRNA splicing event
    • Min, H., Chan, R. C. & Black, D. L. The generally expressed hnRNP F is involved in a neural-specific pre-mRNA splicing event. Genes Dev. 9, 2659-2671 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 2659-2671
    • Min, H.1    Chan, R.C.2    Black, D.L.3
  • 28
    • 0030872401 scopus 로고    scopus 로고
    • The polypyrimidine tract binding protein binds upstream of neural cell-specific c-src exon N1 to repress the splicing of the intron downstream
    • Chan, R. C. & Black, D. L. The polypyrimidine tract binding protein binds upstream of neural cell-specific c-src exon N1 to repress the splicing of the intron downstream. Mol. Cell. Biol. 17, 4667-4676 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4667-4676
    • Chan, R.C.1    Black, D.L.2
  • 29
    • 0030952320 scopus 로고    scopus 로고
    • An intron element modulating 5′ splice site selection in the hnRNP A1 pre-mRNA interacts with hnRNP A1
    • Chabot, B., Blanchette, M., Lapierre, I. & La Branche, H. An intron element modulating 5′ splice site selection in the hnRNP A1 pre-mRNA interacts with hnRNP A1. Mol. Cell. Biol. 17, 1776-1786 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1776-1786
    • Chabot, B.1    Blanchette, M.2    Lapierre, I.3    La Branche, H.4
  • 30
    • 0030777180 scopus 로고    scopus 로고
    • A neuron-specific splicing switch mediated by an array of pre-mRNA repressor sites: Evidence of a regulatory role for the polypyrimidine tract binding protein and a brain-specific PTB counterpart
    • Ashiya, M. & Grabowski, P. J. A neuron-specific splicing switch mediated by an array of pre-mRNA repressor sites: evidence of a regulatory role for the polypyrimidine tract binding protein and a brain-specific PTB counterpart. RNA 3, 996-1015 (1997).
    • (1997) RNA , vol.3 , pp. 996-1015
    • Ashiya, M.1    Grabowski, P.J.2
  • 31
    • 0032953308 scopus 로고    scopus 로고
    • hnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells
    • Chou, M. Y., Rooke, N., Turck, C. W. & Black, D. L. hnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells. Mol. Cell. Biol. 19, 69-77 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 69-77
    • Chou, M.Y.1    Rooke, N.2    Turck, C.W.3    Black, D.L.4
  • 32
    • 0032962535 scopus 로고    scopus 로고
    • hnRNP A1 recruited to an exon in vivo can function as an exon splicing silencer
    • Del Gatto-Konczak, F., Olive, M., Gesnel, M. C. & Breathnach, R. hnRNP A1 recruited to an exon in vivo can function as an exon splicing silencer. Mol. Cell. Biol. 19, 251-260 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 251-260
    • Del Gatto-Konczak, F.1    Olive, M.2    Gesnel, M.C.3    Breathnach, R.4
  • 33
    • 0033105787 scopus 로고    scopus 로고
    • Binding of hnRNP H to an exonic splicing silencer is involved in the regulation of alternative splicing of the rat β-tropomyosin gene
    • Chen, C. D., Kobayashi, R. & Helfman, D. M. Binding of hnRNP H to an exonic splicing silencer is involved in the regulation of alternative splicing of the rat β-tropomyosin gene. Genes Dev. 13, 593-606 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 593-606
    • Chen, C.D.1    Kobayashi, R.2    Helfman, D.M.3
  • 34
    • 0035476679 scopus 로고    scopus 로고
    • SMN interacts with a novel family of hnRNP and spliceosomal proteins
    • Mourelatos, Z., Abel, L., Yong, J., Kataoka, N. & Dreyfuss, G. SMN interacts with a novel family of hnRNP and spliceosomal proteins. EMBO J. 20, 5443-5452 (2001).
    • (2001) EMBO J. , vol.20 , pp. 5443-5452
    • Mourelatos, Z.1    Abel, L.2    Yong, J.3    Kataoka, N.4    Dreyfuss, G.5
  • 35
    • 0035886048 scopus 로고    scopus 로고
    • The hnRNP A1 protein regulates HIV-1 tat splicing via a novel intron silencer element
    • Tange, T. O., Damgaard, C. K., Guth, S., Valcarcel, J. & Kjems, J. The hnRNP A1 protein regulates HIV-1 tat splicing via a novel intron silencer element. EMBO J. 20, 5748-5758 (2001).
    • (2001) EMBO J. , vol.20 , pp. 5748-5758
    • Tange, T.O.1    Damgaard, C.K.2    Guth, S.3    Valcarcel, J.4    Kjems, J.5
  • 36
    • 0026478895 scopus 로고
    • NOP3 is an essential yeast protein which is required for pre-rRNA processing
    • Russell, I. D. & Tollervey, D. NOP3 is an essential yeast protein which is required for pre-rRNA processing. J. Cell Biol. 119, 737-747 (1992).
    • (1992) J. Cell Biol. , vol.119 , pp. 737-747
    • Russell, I.D.1    Tollervey, D.2
  • 37
    • 0030803670 scopus 로고    scopus 로고
    • Hrp1, a sequence-specific RNA-binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3′ -end formation in yeast
    • Kessler, M. M. et al. Hrp1, a sequence-specific RNA-binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3′ -end formation in yeast. Genes Dev. 11, 2545-2556 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 2545-2556
    • Kessler, M.M.1
  • 38
    • 0032529163 scopus 로고    scopus 로고
    • The upstream sequence element of the C2 complement poly(A) signal activates mRNA 3′ end formation by two distinct mechanisms
    • Moreira, A. et al. The upstream sequence element of the C2 complement poly(A) signal activates mRNA 3′ end formation by two distinct mechanisms. Genes Dev. 12, 2522-2534 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 2522-2534
    • Moreira, A.1
  • 39
    • 0032535492 scopus 로고    scopus 로고
    • Control of cleavage site selection during mRNA 3′ end formation by a yeast hnRNR
    • Minvielle-Sebastia, L. et al. Control of cleavage site selection during mRNA 3′ end formation by a yeast hnRNR. EMBO J. 17, 7454-7468 (1998).
    • (1998) EMBO J. , vol.17 , pp. 7454-7468
    • Minvielle-Sebastia, L.1
  • 40
    • 0032404113 scopus 로고    scopus 로고
    • DSEF-1 is a member of the hnRNP H family of RNA-binding proteins and stimulates pre-mRNA cleavage and polyadenylation in vitro
    • Bagga, P. S., Arhin, G. K. & Wilusz, J. DSEF-1 is a member of the hnRNP H family of RNA-binding proteins and stimulates pre-mRNA cleavage and polyadenylation in vitro. Nucleic Acids Res. 26, 5343-5350 (1998).
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5343-5350
    • Bagga, P.S.1    Arhin, G.K.2    Wilusz, J.3
  • 41
    • 0029994329 scopus 로고    scopus 로고
    • A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export
    • Lee, M. S., Henry, M. & Silver, P. A. A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export. Genes Dev. 10, 1233-1246 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 1233-1246
    • Lee, M.S.1    Henry, M.2    Silver, P.A.3
  • 42
    • 0029142841 scopus 로고
    • HnRNP L binds a cis-acting RNA sequence element that enables intron-dependent gene expression
    • Liu, X. & Mertz, J. E. HnRNP L binds a cis-acting RNA sequence element that enables intron-dependent gene expression. Genes Dev. 9, 1766-1780 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 1766-1780
    • Liu, X.1    Mertz, J.E.2
  • 43
    • 0030943323 scopus 로고    scopus 로고
    • A role for the M9 transport signal of hnRNP A1 in mRNA nuclear export
    • Izaurralde, E. et al. A role for the M9 transport signal of hnRNP A1 in mRNA nuclear export. J. Cell Biol. 137, 27-35 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 27-35
    • Izaurralde, E.1
  • 44
    • 0035976612 scopus 로고    scopus 로고
    • Delineation of mRNA export pathways by the use of cell-permeable peptides
    • Gallouzi, I. E. & Steitz, J. A. Delineation of mRNA export pathways by the use of cell-permeable peptides. Science 294, 1895-1901 (2001). This paper provides evidence that there are many export pathways for specific mRNAs. Cell-permeable peptides fused to nuclear-export signals inhibit interactions between particular receptor and adaptor pairs, and block the corresponding export pathway. This allowed the authors to attribute the export of c-myc mRNA to two independent pathways; one mediated by CRM1, and another by transportin 2.
    • (2001) Science , vol.294 , pp. 1895-1901
    • Gallouzi, I.E.1    Steitz, J.A.2
  • 45
    • 0032510715 scopus 로고    scopus 로고
    • hnRNP A2 selectively binds the cytoplasmic transport sequence of myelin basic protein mRNA
    • Hoek, K. S., Kidd, G. J., Carson, J. H. & Smith, R. hnRNP A2 selectively binds the cytoplasmic transport sequence of myelin basic protein mRNA. Biochemistry 37, 7021-7029 (1998).
    • (1998) Biochemistry , vol.37 , pp. 7021-7029
    • Hoek, K.S.1    Kidd, G.J.2    Carson, J.H.3    Smith, R.4
  • 46
    • 0028224527 scopus 로고
    • Essential role for a heterogeneous nuclear ribonucleoprotein (hnRNP) in oogenesis: hrp40 is absent from the germ line in the dorsoventral mutant squid
    • Matunis, E. L., Kelley, R. & Dreyfuss, G. Essential role for a heterogeneous nuclear ribonucleoprotein (hnRNP) in oogenesis: hrp40 is absent from the germ line in the dorsoventral mutant squid. Proc. Natl Acad. Sci. USA 91, 2781-2784 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2781-2784
    • Matunis, E.L.1    Kelley, R.2    Dreyfuss, G.3
  • 47
    • 0033197874 scopus 로고    scopus 로고
    • A Xenopus protein related to hnRNP I has a role in cytoplasmic RNA localization
    • Cote, C. A. et al. A Xenopus protein related to hnRNP I has a role in cytoplasmic RNA localization. Mol. Cell 4, 431-437 (1999). Localization of Vg1 RNA within the Xenopus oocyte is mediated by recognition of a localization element within its 3′ untranslated region. VgRBP60, which is homologous to a human hnRNP I (PTB), is shown to be a specific binder of this sequence and to co-localize with Vg1 RNA.
    • (1999) Mol. Cell , vol.4 , pp. 431-437
    • Cote, C.A.1
  • 48
    • 0034999923 scopus 로고    scopus 로고
    • RNA trafficking signals in human immunodeficiency virus type 1
    • Mouland, A. J. et al. RNA trafficking signals in human immunodeficiency virus type 1. Mol. Cell. Biol. 21, 2133-2143 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2133-2143
    • Mouland, A.J.1
  • 50
    • 0030772963 scopus 로고    scopus 로고
    • mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end
    • Ostareck, D. H. et al. mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end. Cell 89, 597-606 (1997).
    • (1997) Cell , vol.89 , pp. 597-606
    • Ostareck, D.H.1
  • 51
    • 0032575526 scopus 로고    scopus 로고
    • Translational inhibition in vitro of human papillomavirus type 16 L2 mRNA mediated through interaction with heterogenous ribonucleoprotein K and poly(rC)-binding proteins 1 and 2
    • Collier, B., Goobar-Larsson, L., Sokolowski, M. & Schwartz, S. Translational inhibition in vitro of human papillomavirus type 16 L2 mRNA mediated through interaction with heterogenous ribonucleoprotein K and poly(rC)-binding proteins 1 and 2. J. Biol. Chem. 273, 22648-22656 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 22648-22656
    • Collier, B.1    Goobar-Larsson, L.2    Sokolowski, M.3    Schwartz, S.4
  • 52
    • 0033621483 scopus 로고    scopus 로고
    • The N-terminal K homology domain of the poly(rC)-binding protein is a major determinant for binding to the poliovirus 5′-untranslated region and acts as an inhibitor of viral translation
    • Silvera, D., Gamarnik, A. V. & Andino, R. The N-terminal K homology domain of the poly(rC)-binding protein is a major determinant for binding to the poliovirus 5′-untranslated region and acts as an inhibitor of viral translation. J. Biol. Chem. 274, 38163-38170 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 38163-38170
    • Silvera, D.1    Gamarnik, A.V.2    Andino, R.3
  • 53
    • 0035951373 scopus 로고    scopus 로고
    • Lipoxygenase mRNA silencing in erythroid differentiation: The 3′ UTR regulatory complex controls 60S ribosomal subunit joining
    • Ostareck, D. H., Ostareck-Lederer, A., Shatsky, I. N. & Hentze, M. W. Lipoxygenase mRNA silencing in erythroid differentiation: the 3′ UTR regulatory complex controls 60S ribosomal subunit joining. Cell 104, 281-290 (2001). LOX mRNA translation is controlled by the differentiation control element in the 3′ untranslated region and by hnRNPs K and E1. This paper shows that the crucial step is joining of the 60S subunit to mRNA.
    • (2001) Cell , vol.104 , pp. 281-290
    • Ostareck, D.H.1    Ostareck-Lederer, A.2    Shatsky, I.N.3    Hentze, M.W.4
  • 54
    • 0029125496 scopus 로고
    • Identification of two KH domain proteins in the α-globin mRNP stability complex
    • Kiledjian, M., Wang, X. & Liebhaber, S. A. Identification of two KH domain proteins in the α-globin mRNP stability complex. EMBO J. 14, 4357-4364 (1995).
    • (1995) EMBO J. , vol.14 , pp. 4357-4364
    • Kiledjian, M.1    Wang, X.2    Liebhaber, S.A.3
  • 55
    • 0030856470 scopus 로고    scopus 로고
    • Identification of AUF1 (heterogeneous nuclear ribonucleoprotein D) as a component of the α-globin mRNA stability complex
    • Kiledjian, M., DeMada, C. T., Brewer, G. & Novick, K. Identification of AUF1 (heterogeneous nuclear ribonucleoprotein D) as a component of the α-globin mRNA stability complex. Mol. Cell. Biol. 17, 4870-4876 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4870-4876
    • Kiledjian, M.1    DeMada, C.T.2    Brewer, G.3    Novick, K.4
  • 56
    • 0032528304 scopus 로고    scopus 로고
    • hnRNP C increases amyloid precursor protein (APP) production by stabilizing APP mRNA
    • Rajagopalan, L. E., Westmark, C. J., Jarzembowski, J. A. & Matter, J. S. hnRNP C increases amyloid precursor protein (APP) production by stabilizing APP mRNA. Nucleic Acids Res. 26, 3418-3423 (1998).
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3418-3423
    • Rajagopalan, L.E.1    Westmark, C.J.2    Jarzembowski, J.A.3    Matter, J.S.4
  • 57
    • 0033031221 scopus 로고    scopus 로고
    • Assembly of the α-globin mRNA stability complex reflects binary interaction between the pyrimidine-rich 3′ untranslated region determinant and poly(C) binding protein αCP
    • Chkheidze, A. N. et al. Assembly of the α-globin mRNA stability complex reflects binary interaction between the pyrimidine-rich 3′ untranslated region determinant and poly(C) binding protein αCP. Mol. Cell. Biol. 19, 4572-4581 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4572-4581
    • Chkheidze, A.N.1
  • 58
    • 0033555522 scopus 로고    scopus 로고
    • Regulation of human vascular endothelial growth factor mRNA stability in hypoxia by heterogeneous nuclear ribonucleoprotein L
    • Shih, S. C. & Claffey, K. P. Regulation of human vascular endothelial growth factor mRNA stability in hypoxia by heterogeneous nuclear ribonucleoprotein L. J. Biol. Chem. 274, 1359-1365 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 1359-1365
    • Shih, S.C.1    Claffey, K.P.2
  • 59
    • 0033565383 scopus 로고    scopus 로고
    • Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element
    • Loflin, P., Chen, C. Y. & Shyu, A. B. Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element. Genes Dev. 13, 1884-1897 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1884-1897
    • Loflin, P.1    Chen, C.Y.2    Shyu, A.B.3
  • 60
    • 0034806974 scopus 로고    scopus 로고
    • Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover
    • Xu, N., Chen, C. Y. & Shyu, A. B. Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover. Mol. Cell. Biol. 21, 6960-6971 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6960-6971
    • Xu, N.1    Chen, C.Y.2    Shyu, A.B.3
  • 61
    • 0026527447 scopus 로고
    • Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
    • Pinol-Roma, S. & Dreyfuss, G. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature 355, 730-732 (1992). This paper shows that several of the abundant hnRNP proteins, such as A1, shuttle rapidly and continuously between the nucleus and the cytoplasm. It further shows that these shuttling proteins are also bound to mRNAs in the cytoplasm, and proposes functions for shuttling proteins in mRNA export, mRNA function in the cytoplasm, and nucleo-cytoplasmic signal transduction.
    • (1992) Nature , vol.355 , pp. 730-732
    • Pinol-Roma, S.1    Dreyfuss, G.2
  • 62
    • 0029807798 scopus 로고    scopus 로고
    • A protein of the SR family of splicing factors binds extensively to exonic Balbiani ring pre-mRNA and accompanies the RNA from the gene to the nuclear pore
    • Alzhanova-Ericsson, A. T. et al. A protein of the SR family of splicing factors binds extensively to exonic Balbiani ring pre-mRNA and accompanies the RNA from the gene to the nuclear pore. Genes Dev. 10, 2881-2893 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 2881-2893
    • Alzhanova-Ericsson, A.T.1
  • 63
    • 0031929940 scopus 로고    scopus 로고
    • A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm
    • Caceres, J. F., Screaton, G. R. & Krainer, A. R. A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm. Genes Dev. 12, 55-66 (1998). This paper shows that some, but not all, of the SR proteins shuttle between the nucleus and the cytoplasm.
    • (1998) Genes Dev. , vol.12 , pp. 55-66
    • Caceres, J.F.1    Screaton, G.R.2    Krainer, A.R.3
  • 64
    • 0025762042 scopus 로고
    • The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities
    • Burd, C. G., Matunis, E. L. & Dreyfuss, G. The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities. Mol. Cell. Biol. 11, 3419-3424 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3419-3424
    • Burd, C.G.1    Matunis, E.L.2    Dreyfuss, G.3
  • 65
    • 0032535452 scopus 로고    scopus 로고
    • A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation
    • Imataka, H., Gradi, A. & Sonenberg, N. A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBO J. 17, 7480-7489 (1998).
    • (1998) EMBO J. , vol.17 , pp. 7480-7489
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 66
    • 0028884380 scopus 로고
    • A common function for mRNA 5′ and 3′ ends in translation initiation in yeast
    • Tarun, S. Z. Jr & Sachs, A. B. A common function for mRNA 5′ and 3′ ends in translation initiation in yeast. Genes Dev. 9, 2997-3007 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 2997-3007
    • Tarun S.Z., Jr.1    Sachs, A.B.2
  • 67
    • 0032190508 scopus 로고    scopus 로고
    • Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F
    • Piron, M., Vende, P., Cohen, J. & Poncet, D. Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F. EMBO J. 17, 5811-5821 (1998).
    • (1998) EMBO J. , vol.17 , pp. 5811-5821
    • Piron, M.1    Vende, P.2    Cohen, J.3    Poncet, D.4
  • 68
    • 0030034421 scopus 로고    scopus 로고
    • A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into polysomes
    • Visa, N. et al. A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into polysomes. Cell 84, 253-264 (1996). This study describes how electron microscopy with Balbiani ring pre-mRNA for C. tentans was used to describe hrp36, which is similar to the mammalian hnRNP A1. When hrp36 is added to Balbiani ring RNA during transcription, it stays on the nucleoplasmic Balbiani ring particles, and remains associated with Balbiani ring RNA after export.
    • (1996) Cell , vol.84 , pp. 253-264
    • Visa, N.1
  • 69
    • 0034659241 scopus 로고    scopus 로고
    • RNA polymerase II and the integration of nuclear events
    • Hirose, Y. & Manley, J. L. RNA polymerase II and the integration of nuclear events. Genes Dev. 14, 1415-1429 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 1415-1429
    • Hirose, Y.1    Manley, J.L.2
  • 70
    • 0033788228 scopus 로고    scopus 로고
    • The ends of the affair: Capping and polyadenylation
    • Shatkin, A. J. & Manley, J. L. The ends of the affair: capping and polyadenylation. Nature Struct. Biol. 7, 838-842 (2000).
    • (2000) Nature Struct. Biol. , vol.7 , pp. 838-842
    • Shatkin, A.J.1    Manley, J.L.2
  • 71
    • 0025818887 scopus 로고
    • Small nuclear ribonucleoproteins and heterogeneous nuclear ribonucleoproteins in the amphibian germinal vesicle: Loops, spheres, and snurposomes
    • Wu, Z. A., Murphy, C., Callan, H. G. & Gall, J. G. Small nuclear ribonucleoproteins and heterogeneous nuclear ribonucleoproteins in the amphibian germinal vesicle: loops, spheres, and snurposomes. J. Cell Biol. 113, 465-483 (1991).
    • (1991) J. Cell Biol. , vol.113 , pp. 465-483
    • Wu, Z.A.1    Murphy, C.2    Callan, H.G.3    Gall, J.G.4
  • 72
    • 0035912782 scopus 로고    scopus 로고
    • Assembly and transport of a premessenger RNP particle
    • Daneholt, B. Assembly and transport of a premessenger RNP particle. Proc. Natl Acad. Sci. USA 98, 7012-7017 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7012-7017
    • Daneholt, B.1
  • 73
    • 0029870388 scopus 로고    scopus 로고
    • A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscriptionally and accompanies the ribonucleoprotein particle during nuclear export
    • Visa, N., Izaurralde, E., Ferreira, J., Daneholt, B. & Mattaj, I. W. A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscriptionally and accompanies the ribonucleoprotein particle during nuclear export. J. Cell Biol. 133, 5-14 (1996).
    • (1996) J. Cell Biol. , vol.133 , pp. 5-14
    • Visa, N.1    Izaurralde, E.2    Ferreira, J.3    Daneholt, B.4    Mattaj, I.W.5
  • 74
    • 0032494088 scopus 로고    scopus 로고
    • The hrp23 protein in the balbiani ring pre-mRNP particles is released just before or at the binding of the particles to the nuclear pore complex
    • Sun, X. et al. The hrp23 protein in the balbiani ring pre-mRNP particles is released just before or at the binding of the particles to the nuclear pore complex. J Cell Biol. 142, 1181-1193 (1998).
    • (1998) J Cell Biol. , vol.142 , pp. 1181-1193
    • Sun, X.1
  • 75
    • 0033592896 scopus 로고    scopus 로고
    • Splicing is required for rapid and efficient mRNA export in metazoans
    • Luo, M. J. & Reed, R. Splicing is required for rapid and efficient mRNA export in metazoans. Proc. Natl Acad. Sci. USA 96, 14937-14942 (1999). The authors show that spliced mRNAs are exported at a higher rate than intronless mRNAs, and that the spliced mRNP complex has a different protein composition from that of the intronless mRNP complex. This indicates the presence of an export-promoting factor(s) that is recruited to the mRNA by the process of splicing.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14937-14942
    • Luo, M.J.1    Reed, R.2
  • 76
    • 0034193569 scopus 로고    scopus 로고
    • Pre-mRNA splicing alters mRNP composition: Evidence for stable association of proteins at exon-exon junctions
    • 32P at exon-exon junctions. After in vitro splicing and crosslinking, only proteins that are bound to the junction can be labelled. The results show that splicing recruits a new set of proteins near the exon-exon junction.
    • (2000) Genes Dev. , vol.14 , pp. 1098-1108
    • Le Hir, H.1    Moore, M.J.2    Maquat, L.E.3
  • 78
    • 0033634824 scopus 로고    scopus 로고
    • Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm
    • Kataoka, N. et al. Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm. Mol. Cell 6, 673-682 (2000). This study shows that a new RNA-binding protein, Y14, binds preferentially to mRNAs that are produced by splicing both in vitro and in vivo. These results also show that pre-mRNA splicing results in the binding of specific proteins to the mRNAs. Binding of these proteins persists on the same mRNAs after export to the cytoplasm.
    • (2000) Mol. Cell , vol.6 , pp. 673-682
    • Kataoka, N.1
  • 79
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
    • Le Hir, H., Izaurralde, E., Maquat, L. E. & Moore, M. J. The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. EMBO J. 19, 6860-6869 (2000). This study identifies the binding site of mRNA-specific proteins (SRm160, DEK, Y14, Aly and RNPS1) on spliced mRNAs near exon-exon junctions, and further characterizes the multi-protein complex.
    • (2000) EMBO J. , vol.19 , pp. 6860-6869
    • Le Hir, H.1    Izaurralde, E.2    Maquat, L.E.3    Moore, M.J.4
  • 80
    • 0035901565 scopus 로고    scopus 로고
    • The Y14 protein communicates to the cytoplasm the position of exon-exon junctions
    • Kim, V. N. et al. The Y14 protein communicates to the cytoplasm the position of exon-exon junctions. EMBO J. 20, 2062-2068 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2062-2068
    • Kim, V.N.1
  • 81
    • 0033575702 scopus 로고    scopus 로고
    • Purification and characterization of human RNPS1: A general activator of pre-mRNA splicing
    • Mayeda, A. et al. Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing. EMBO J. 18, 4560-4570 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4560-4570
    • Mayeda, A.1
  • 82
    • 0033625090 scopus 로고    scopus 로고
    • REF, an evolutionarily conserved family of hnRNP-like proteins, interacts with TAP/Mex67p and participates in mRNA nuclear export
    • Stutz, F. et al. REF, an evolutionarily conserved family of hnRNP-like proteins, interacts with TAP/Mex67p and participates in mRNA nuclear export. RNA 6, 638-650 (2000). The authors show that Mex67 directly interacts with Yra1, and that this interaction is evolutionarily conserved, as Yra1 can also interact with TAP, the mammalian homologue of Mex67. Using database searches with Yra1, it turned out that Yra1 belongs to an evolutionarily conserved family of hnRNP-like proteins across several species. These proteins were named REF-bps, as they bind to both RNA and export factors.
    • (2000) RNA , vol.6 , pp. 638-650
    • Stutz, F.1
  • 83
    • 0035890258 scopus 로고    scopus 로고
    • Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex
    • Kataoka, N., Diem, M. D., Kim, V. N., Yong, J. & Dreyfuss, G. Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex. EMBO J. 20, 6424-6433 (2001). This paper shows that a human homologue of Drosophila mago nashi protein is a new component of the exon-exon junction complex, and that it binds specifically to Y14. It further shows that magoh and Y14 bind the mRNA-export factor TAP.
    • (2001) EMBO J. , vol.20 , pp. 6424-6433
    • Kataoka, N.1    Diem, M.D.2    Kim, V.N.3    Yong, J.4    Dreyfuss, G.5
  • 84
    • 0035687504 scopus 로고    scopus 로고
    • The protein Mago provides a link between splicing and mRNA localization
    • Le Hir, H., Gatfield, D., Braun, I. C., Forler, D. & Izaurralde, E. The protein Mago provides a link between splicing and mRNA localization. EMBO Rep. 2, 1119-1124 (2001).
    • (2001) EMBO Rep. , vol.2 , pp. 1119-1124
    • Le Hir, H.1    Gatfield, D.2    Braun, I.C.3    Forler, D.4    Izaurralde, E.5
  • 85
    • 0035823150 scopus 로고    scopus 로고
    • Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex
    • Kim, V. N., Kataoka, N. & Dreyfuss, G. Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex. Science 293, 1832-1836 (2001). This study shows that Upf3 is a bona fide component of the exon-exon junction complex, and provides a probable molecular link between splicing and an effector of nonsense-mediated mRNA decay.
    • (2001) Science , vol.293 , pp. 1832-1836
    • Kim, V.N.1    Kataoka, N.2    Dreyfuss, G.3
  • 86
    • 0035801373 scopus 로고    scopus 로고
    • The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay
    • Le Hir, H., Gatfield, D., Izaurralde, E. & Moore, M. J. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay. EMBO J. 20, 4987-4997 (2001). This shows that both mRNA export factors (TAP and p15) and nonsense-mediated mRNA decay factors (Upf2 and 3) are enriched near exon-exon junctions, which indicates that the exon-exon junction complex might function in both pathways.
    • (2001) EMBO J. , vol.20 , pp. 4987-4997
    • Le Hir, H.1    Gatfield, D.2    Izaurralde, E.3    Moore, M.J.4
  • 87
    • 0034710286 scopus 로고    scopus 로고
    • The acute myeloid leukemia-associated protein, DEK, forms a splicing-dependent interaction with exon-product complexes
    • McGarvey, T. et al. The acute myeloid leukemia-associated protein, DEK, forms a splicing-dependent interaction with exon-product complexes. J. Cell Biol. 150, 309-320 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 309-320
    • McGarvey, T.1
  • 88
    • 0034699472 scopus 로고    scopus 로고
    • The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans
    • Zhou, Z. et al. The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans. Nature 407, 401-405 (2000). This study reports direct evidence for a function for Aly/REF in mRNA export based on oocyte-injection studies. Now it seems, however, that Aly/REF might not be the only component of the exon-exon junction complex that has this activity, and also that Aly/REF might also facilitate the export of intronless mRNAs.
    • (2000) Nature , vol.407 , pp. 401-405
    • Zhou, Z.1
  • 89
    • 0035970063 scopus 로고    scopus 로고
    • REF proteins mediate the export of spliced and unspliced mRNAs from the nucleus
    • Rodrigues, J. P. et al. REF proteins mediate the export of spliced and unspliced mRNAs from the nucleus. Proc. Natl Acad. Sci. USA 98, 1030-1035 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1030-1035
    • Rodrigues, J.P.1
  • 90
    • 0035823247 scopus 로고    scopus 로고
    • Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1
    • 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, 1836-1839 (2001). RNPS1 and, to a lesser extent, Y14 are found to have a role in nonsense-mediated mRNA decay, presumably through their interactions with Upf3.
    • (2001) Science , vol.293 , pp. 1836-1839
    • Lykke-Andersen, J.1    Shu, M.D.2    Steitz, J.A.3
  • 91
    • 0035498967 scopus 로고    scopus 로고
    • The RNA-binding protein Tsunagi interacts with Mago Nashi to establish polarity and localize oskar mRNA during Drosophila oogenesis
    • 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, 2886-2899 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2886-2899
    • Mohr, S.E.1    Dillon, S.T.2    Boswell, R.E.3
  • 92
    • 0035975970 scopus 로고    scopus 로고
    • Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport
    • Hachet, O. & Ephrussi, A. Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport. Curr. Biol. 11, 1666-1674 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1666-1674
    • Hachet, O.1    Ephrussi, A.2
  • 93
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich, D. & Kutay, U. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15, 607-660 (1999).
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 94
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The soluble phase
    • Mattaj, I. W. & Englmeier, L. Nucleocytoplasmic transport: the soluble phase. Annu. Rev. Biochem. 67, 265-306 (1998).
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 95
    • 0033598989 scopus 로고    scopus 로고
    • Transport of proteins and RNAs in and out of the nucleus
    • Nakielny, S. & Dreyfuss, G. Transport of proteins and RNAs in and out of the nucleus. Cell 99, 677-690 (1999).
    • (1999) Cell , vol.99 , pp. 677-690
    • Nakielny, S.1    Dreyfuss, G.2
  • 96
    • 0030911425 scopus 로고    scopus 로고
    • Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores
    • Segref, A. et al. Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores. EMBO J. 16, 3256-3271 (1997). This paper identifies an essential cellular factor for nuclear mRNA export in yeast, called Mex67, through its genetic interaction with nucleoporin Nup85. In the thermosensitive mex67 mutant, accumulation of poly(A) RNA in intranuclear foci is detected shortly after a shift to the restrictive temperature. These results strongly indicate that Mex67 is likely to participate directly in the export of mRNA from the nucleus to the cytoplasm.
    • (1997) EMBO J. , vol.16 , pp. 3256-3271
    • Segref, A.1
  • 97
    • 0032037421 scopus 로고    scopus 로고
    • TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus
    • Gruter, P. et al. TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus. Mol. Cell 1, 649-659 (1998). The constitutive transport element (CTE) of the type D retroviruses has been shown to promote nuclear export of unspliced viral RNAs. This paper identifies TAP as the cellular factor that specifically binds to wild-type CTE and mediates CTE-dependent export. As the excess amount of CTE blocks mRNA export and TAP can overcome this effect, TAP was thought to have a function in mRNA export, like its yeast homologue Mex67.
    • (1998) Mol. Cell , vol.1 , pp. 649-659
    • Gruter, P.1
  • 98
    • 0345643313 scopus 로고    scopus 로고
    • The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human
    • Katahira, J. et al. The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human. EMBO J. 18, 2593-2609 (1999).
    • (1999) EMBO J. , vol.18 , pp. 2593-2609
    • Katahira, J.1
  • 99
    • 0034461573 scopus 로고    scopus 로고
    • Mex67p of Schizosaccharomyces pombe interacts with Rae1p in mediating mRNA export
    • Yoon, J. H., Love, D. C., Guhathakurta, A., Hanover, J. A. & Dhar, R. Mex67p of Schizosaccharomyces pombe interacts with Rae1p in mediating mRNA export. Mol. Cell. Biol. 20, 8767-8782 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8767-8782
    • Yoon, J.H.1    Love, D.C.2    Guhathakurta, A.3    Hanover, J.A.4    Dhar, R.5
  • 100
    • 0032766007 scopus 로고    scopus 로고
    • Identification of novel import and export signals of human TAP, the protein that binds to the constitutive transport element of the type D retrovirus mRNAs
    • Bear, J. et al. Identification of novel import and export signals of human TAP, the protein that binds to the constitutive transport element of the type D retrovirus mRNAs. Mol. Cell. Biol. 19, 6306-6317 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6306-6317
    • Bear, J.1
  • 101
    • 0033119628 scopus 로고    scopus 로고
    • TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleus
    • Braun, I. C., Rohrbach, E., Schmitt, C. & Izaurralde, E. TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleus. EMBO J. 18, 1953-1965 (1999).
    • (1999) EMBO J. , vol.18 , pp. 1953-1965
    • Braun, I.C.1    Rohrbach, E.2    Schmitt, C.3    Izaurralde, E.4
  • 102
    • 0033135976 scopus 로고    scopus 로고
    • The human Tap protein is a nuclear mRNA export factor that contains novel RNA-binding and nucleocytoplasmic transport sequences
    • Kang, Y. & Cullen, B. R. The human Tap protein is a nuclear mRNA export factor that contains novel RNA-binding and nucleocytoplasmic transport sequences. Genes Dev. 13, 1126-1139 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1126-1139
    • Kang, Y.1    Cullen, B.R.2
  • 103
    • 0034541842 scopus 로고    scopus 로고
    • The mRNA export in Caenorhabditis elegans is mediated by Ce-NXF-1, an ortholog of human TAP/NXF and Saccharomyces cerevisiae Mex67p
    • Tan, W., Zolotukhin, A. S., Bear, J., Patenaude, D. J. & Felber, B. K. The mRNA export in Caenorhabditis elegans is mediated by Ce-NXF-1, an ortholog of human TAP/NXF and Saccharomyces cerevisiae Mex67p. RNA 6, 1762-1772 (2000).
    • (2000) RNA , vol.6 , pp. 1762-1772
    • Tan, W.1    Zolotukhin, A.S.2    Bear, J.3    Patenaude, D.J.4    Felber, B.K.5
  • 104
    • 0035827686 scopus 로고    scopus 로고
    • Overexpression of TAP/p15 heterodimers bypasses nuclear retention and stimulates nuclear mRNA export
    • Braun, I. C., Herold, A., Rode, M., Conti, E. & Izaurralde, E. Overexpression of TAP/p15 heterodimers bypasses nuclear retention and stimulates nuclear mRNA export. J. Biol. Chem. 276, 20536-20543 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 20536-20543
    • Braun, I.C.1    Herold, A.2    Rode, M.3    Conti, E.4    Izaurralde, E.5
  • 105
    • 0035102745 scopus 로고    scopus 로고
    • NXT1 (p15) is a crucial cellular cofactor in TAP-dependent export of intron-containing RNA in mammalian cells
    • Guzik, B. W. et al. NXT1 (p15) is a crucial cellular cofactor in TAP-dependent export of intron-containing RNA in mammalian cells. Mol. Cell. Biol. 21, 2545-2554 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2545-2554
    • Guzik, B.W.1
  • 106
    • 0035976970 scopus 로고    scopus 로고
    • RNA export mediated by tap involves NXT1-dependent interactions with the nuclear pore complex
    • Levesque, L. et al. RNA export mediated by tap involves NXT1-dependent interactions with the nuclear pore complex. J. Biol. Chem. 276, 44953-44962 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 44953-44962
    • Levesque, L.1
  • 107
    • 0036132677 scopus 로고    scopus 로고
    • Formation of Tap/NXT1 heterodimers activates Tap-dependent nuclear mRNA export by enhancing recruitment to nuclear pore complexes
    • Wiegand, H. L. et al. Formation of Tap/NXT1 heterodimers activates Tap-dependent nuclear mRNA export by enhancing recruitment to nuclear pore complexes. Mol. Cell. Biol. 22, 245-256 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 245-256
    • Wiegand, H.L.1
  • 108
    • 0034460814 scopus 로고    scopus 로고
    • TAP (NXF1) belongs to a multigene family of putative RNA export factors with a conserved modular architecture
    • Harold, A. et al. TAP (NXF1) belongs to a multigene family of putative RNA export factors with a conserved modular architecture. Mol. Cell. Biol. 20, 8996-9008 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8996-9008
    • Harold, A.1
  • 109
    • 0035908996 scopus 로고    scopus 로고
    • NXF5, a novel member of the nuclear RNA export factor family, is lost in a mate patient with a syndromic form of mental retardation
    • Jun, L. et al. NXF5, a novel member of the nuclear RNA export factor family, is lost in a mate patient with a syndromic form of mental retardation. Curr. Biol. 11, 1381-1391 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1381-1391
    • Jun, L.1
  • 110
    • 0032431026 scopus 로고    scopus 로고
    • HNS, a nuclear-cytoplasmic shuttling sequence in HuR
    • Fan, X. C. & Steitz, J. A. HNS, a nuclear-cytoplasmic shuttling sequence in HuR. Proc. Natl Acad. Sci. USA 95, 15293-15298 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15293-15298
    • Fan, X.C.1    Steitz, J.A.2
  • 111
    • 0028902009 scopus 로고
    • A mutation in the Schizosaccharomyces pombe rae1 gene causes defects in poly(A)+ RNA export and in the cytoskeleton
    • Brown, J. A. et al. A mutation in the Schizosaccharomyces pombe rae1 gene causes defects in poly(A)+ RNA export and in the cytoskeleton. J. Biol. Chem. 270, 7411-7419 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 7411-7419
    • Brown, J.A.1
  • 112
    • 0029804758 scopus 로고    scopus 로고
    • GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function
    • Murphy, R., Watkins, J. L. & Wente, S. R. GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function. Mol. Biol. Cell 7, 1921-1937 (1996).
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1921-1937
    • Murphy, R.1    Watkins, J.L.2    Wente, S.R.3
  • 113
    • 0030707872 scopus 로고    scopus 로고
    • The human RAE1 gene is a functional homologue of Schizosaccharomyces pombe rae1 gene involved in nuclear export of Poly(A)+ RNA
    • Bharathi, A. et al. The human RAE1 gene is a functional homologue of Schizosaccharomyces pombe rae1 gene involved in nuclear export of Poly(A)+ RNA. Gene 198, 251-258 (1997).
    • (1997) Gene , vol.198 , pp. 251-258
    • Bharathi, A.1
  • 114
    • 0344171991 scopus 로고    scopus 로고
    • RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains
    • Pritchard, C. E., Fornerod, M., Kasper, L. H. & van Deursen, J. M. RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains. J. Cell Biol. 145, 237-254 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 237-254
    • Pritchard, C.E.1    Fornerod, M.2    Kasper, L.H.3    Van Deursen, J.M.4
  • 115
    • 0032080030 scopus 로고    scopus 로고
    • Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export
    • Snay-Hodge, C. A., Colot, H. V., Goldstein, A. L. & Cole, C. N. Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export. EMBO J. 17, 2663-2676 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2663-2676
    • Snay-Hodge, C.A.1    Colot, H.V.2    Goldstein, A.L.3    Cole, C.N.4
  • 116
    • 0032079407 scopus 로고    scopus 로고
    • Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export
    • Tseng, S. S. et al. Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export. EMBO J. 17, 2651-2662 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2651-2662
    • Tseng, S.S.1
  • 117
    • 0035025061 scopus 로고    scopus 로고
    • Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA
    • Huang, Y. & Steitz, J. A. Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA. Mol. Cell 7, 899-905 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 899-905
    • Huang, Y.1    Steitz, J.A.2
  • 118
    • 0034847379 scopus 로고    scopus 로고
    • Two closely related human nuclear export factors utilize entirely distinct export pathways
    • Yang, J., Bogerd, H. P., Wang, P. J., Page, D. C. & Cullen, B. R. Two closely related human nuclear export factors utilize entirely distinct export pathways. Mol. Cell 8, 397-406 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 397-406
    • Yang, J.1    Bogerd, H.P.2    Wang, P.J.3    Page, D.C.4    Cullen, B.R.5
  • 119
    • 0024853361 scopus 로고
    • Regulation by HIV Rev depends upon recognition of splice sites
    • Chang, D. D. & Sharp, P. A. Regulation by HIV Rev depends upon recognition of splice sites. Cell 59, 789-795 (1989).
    • (1989) Cell , vol.59 , pp. 789-795
    • Chang, D.D.1    Sharp, P.A.2
  • 120
    • 0024973850 scopus 로고
    • Some cis- and trans-acting mutants for splicing target pre-mRNA to the cytoplasm
    • Legrain, P. & Rosbash, M. Some cis- and trans-acting mutants for splicing target pre-mRNA to the cytoplasm. Cell 57, 573-583 (1989).
    • (1989) Cell , vol.57 , pp. 573-583
    • Legrain, P.1    Rosbash, M.2
  • 121
    • 0041013167 scopus 로고    scopus 로고
    • Inefficient processing impairs release of RNA from the site of transcription
    • Custodio, N. et al. Inefficient processing impairs release of RNA from the site of transcription. EMBO J. 18, 2855-2866 (1999).
    • (1999) EMBO J. , vol.18 , pp. 2855-2866
    • Custodio, N.1
  • 122
    • 0030912154 scopus 로고    scopus 로고
    • YRA1, an essential Saccharomyces cerevisiae gene, encodes a novel nuclear protein with RNA annealing activity
    • Portman, D. S., O'Connor, J. P. & Dreyfuss, G. YRA1, an essential Saccharomyces cerevisiae gene, encodes a novel nuclear protein with RNA annealing activity. RNA 3, 527-537 (1997).
    • (1997) RNA , vol.3 , pp. 527-537
    • Portman, D.S.1    O'Connor, J.P.2    Dreyfuss, G.3
  • 123
    • 0141469976 scopus 로고    scopus 로고
    • Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export
    • Strasser, K. & Hurt, E. Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export. EMBO J. 19, 410-420 (2000). This paper shows that an RNA-binding protein Yra1 binds directly to Mex67. Mutants of YRA1 are impaired in nuclear-poly(A)-RNA export at the restrictive temperature. These results indicate that Yra1 is the mRNA-export factor that bridges the export factor Mex67/Mtr2 to mRNA transport cargoes.
    • (2000) EMBO J. , vol.19 , pp. 410-420
    • Strasser, K.1    Hurt, E.2
  • 124
    • 0035846138 scopus 로고    scopus 로고
    • Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly
    • Luo, M. L. et al. Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly. Nature 413, 644-647 (2001). This paper shows that the conserved DEAD-box helicase UAP56, which is a splicing factor, interacts directly and specifically with Aly/REF. These data indicate that UAP56 can couple pre-mRNA splicing and mRNA export by recruiting Aly/REF to the spliced mRNP.
    • (2001) Nature , vol.413 , pp. 644-647
    • Luo, M.L.1
  • 125
    • 0035846109 scopus 로고    scopus 로고
    • Splicing factor Sub2p is required for nuclear mRNA export through its interaction with Yra1p
    • Strasser, K. & Hurt, E. Splicing factor Sub2p is required for nuclear mRNA export through its interaction with Yra1p. Nature 413, 648-652 (2001). This paper shows a genetic interaction in yeast between mRNA-export factor Yra1 and Sub2, a DEAD-box helicase involved in splicing. Sub2 and Mex67/Mtr2 bind to the same domains of Yra1, and compete with each other for binding. These results indicate that the splicing factor Sub2 (the yeast homologue of the mammalian UAP56) is also important in mRNA export, probably by recruiting Yra1 to the mRNA.
    • (2001) Nature , vol.413 , pp. 648-652
    • Strasser, K.1    Hurt, E.2
  • 126
    • 0035975969 scopus 로고    scopus 로고
    • The DECD box putative ATPase Sub2p is an early mRNA export factor
    • Jensen, T. H., Boulay, J., Rosbash, M. & Libri, D. The DECD box putative ATPase Sub2p is an early mRNA export factor. Curr. Biol. 11, 1711-1715 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1711-1715
    • Jensen, T.H.1    Boulay, J.2    Rosbash, M.3    Libri, D.4
  • 127
    • 0035975942 scopus 로고    scopus 로고
    • The DExH/D box protein HEL/UAP56 is essential for mRNA nuclear export in Drosophila
    • Gatfield, D. et al. The DExH/D box protein HEL/UAP56 is essential for mRNA nuclear export in Drosophila. Curr. Biol. 11, 1716-1721 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1716-1721
    • Gatfield, D.1
  • 128
    • 0031193589 scopus 로고    scopus 로고
    • The mago nashi gene is required for the polarisation of the oocyte and the formation of perpendicular axes in Drosophila
    • Micklem, D. R. et al. The mago nashi gene is required for the polarisation of the oocyte and the formation of perpendicular axes in Drosophila. Curr. Biol. 7, 468-478 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 468-478
    • Micklem, D.R.1
  • 129
    • 0030886559 scopus 로고    scopus 로고
    • Mago nashi mediates the posterior follicle cell-to-oocyte signal to organize axis formation in Drosophila
    • Newmark, P. A., Mohr, S. E., Gong, L. & Boswell, R. E. mago nashi mediates the posterior follicle cell-to-oocyte signal to organize axis formation in Drosophila. Development 124, 3197-3207 (1997).
    • (1997) Development , vol.124 , pp. 3197-3207
    • Newmark, P.A.1    Mohr, S.E.2    Gong, L.3    Boswell, R.E.4
  • 130
    • 0033997355 scopus 로고    scopus 로고
    • MAGOH interacts with a novel RNA-binding protein
    • Zhao, X. F., Nowak, N. J., Shows, T. B. & Aplan, P. D. MAGOH interacts with a novel RNA-binding protein. Genomics 63, 146-148 (2000).
    • (2000) Genomics , vol.63 , pp. 146-148
    • Zhao, X.F.1    Nowak, N.J.2    Shows, T.B.3    Aplan, P.D.4
  • 131
    • 0035898685 scopus 로고    scopus 로고
    • Importin 13: A novel mediator of nuclear import and export
    • Mingot, J. M., Kostka, S., Kraft, R., Hartmann, E. & Gorlich, D. Importin 13: a novel mediator of nuclear import and export. EMBO J. 20, 3685-3694 (2001).
    • (2001) EMBO J. , vol.20 , pp. 3685-3694
    • Mingot, J.M.1    Kostka, S.2    Kraft, R.3    Hartmann, E.4    Gorlich, D.5
  • 132
    • 0033525169 scopus 로고    scopus 로고
    • A perfect message: RNA surveillance and nonsense-mediated decay
    • Hentze, M. W. & Kulozik, A. E. A perfect message: RNA surveillance and nonsense-mediated decay. Cell 96, 307-310 (1999).
    • (1999) Cell , vol.96 , pp. 307-310
    • Hentze, M.W.1    Kulozik, A.E.2
  • 133
    • 0035498978 scopus 로고    scopus 로고
    • Curbing the nonsense: The activation and regulation of mRNA surveillance
    • Wilusz, C. J., Wang, W. & Peltz, S. W. Curbing the nonsense: the activation and regulation of mRNA surveillance. Genes Dev. 15, 2781-2785 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2781-2785
    • Wilusz, C.J.1    Wang, W.2    Peltz, S.W.3
  • 134
    • 0035254681 scopus 로고    scopus 로고
    • Splicing and 3′ end formation in the definition of nonsense-mediated decay-competent human β-globin mRNPs
    • Neu-Yilik, G. et al. Splicing and 3′ end formation in the definition of nonsense-mediated decay-competent human β-globin mRNPs. EMBO J. 20, 532-540 (2001). By using human β-globin mRNA as a model system, this paper shows that the formation of nonsense-mediated mRNA decay-competent mRNP particles in higher eukaryotes depends on splicing, but does not require the presence of a poly(A) tall.
    • (2001) EMBO J. , vol.20 , pp. 532-540
    • Neu-Yilik, G.1
  • 135
    • 0027993583 scopus 로고
    • Introns are cis effectors of the nonsense-codon-mediated reduction in nuclear mRNA abundance
    • Cheng, J., Belgrader, P., Zhou, X. & Maquat, L. E. Introns are cis effectors of the nonsense-codon-mediated reduction in nuclear mRNA abundance. Mol. Cell. Biol. 14, 6317-6325 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6317-6325
    • Cheng, J.1    Belgrader, P.2    Zhou, X.3    Maquat, L.E.4
  • 136
    • 0029908912 scopus 로고    scopus 로고
    • A splicing-dependent regulatory mechanism that detects translation signals
    • Carter, M. S., Li, S. & Wilkinson, M. F. A splicing-dependent regulatory mechanism that detects translation signals. EMBO J. 15, 5965-5975 (1996).
    • (1996) EMBO J. , vol.15 , pp. 5965-5975
    • Carter, M.S.1    Li, S.2    Wilkinson, M.F.3
  • 137
    • 0032526946 scopus 로고    scopus 로고
    • Binary specification of nonsense codons by splicing and cytoplasmic translation
    • Thermann, R. et al. Binary specification of nonsense codons by splicing and cytoplasmic translation. EMBO J. 17, 3484-8494 (1998).
    • (1998) EMBO J. , vol.17 , pp. 3484-8494
    • Thermann, R.1
  • 138
    • 0034282528 scopus 로고    scopus 로고
    • Nonsense-mediated decay of glulathione peroxidase 1 mRNA in the cytoplasm depends on intron position
    • Sun, X., Moriarty, P. M. & Maquat, L. E. Nonsense-mediated decay of glulathione peroxidase 1 mRNA in the cytoplasm depends on intron position. EMBO J. 19, 4734-4744 (2000). This paper shows that a premature termination codon elicits nonsense-mediated mRNA decay when it is located more than 50-55 nt upstream of the last exon-exon junction.
    • (2000) EMBO J. , vol.19 , pp. 4734-4744
    • Sun, X.1    Moriarty, P.M.2    Maquat, L.E.3
  • 139
    • 0032104190 scopus 로고    scopus 로고
    • A rule for termination-codon position within intron-containing genes: When nonsense affects RNA abundance
    • Nagy, E. & Maquat, L. E. A rule for termination-codon position within intron-containing genes: when nonsense affects RNA abundance. Trends Biochem. Sci. 23, 198-199 (1998).
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 198-199
    • Nagy, E.1    Maquat, L.E.2
  • 140
    • 0027330895 scopus 로고
    • T cell receptor-β mRNA splicing during thymic maturation in vivo and in an inducible T cell clone in vitro
    • Qian, L., Vu, M. N., Carter, M. S., Doskow, J. & Wilkinson, M. F. T cell receptor-β mRNA splicing during thymic maturation in vivo and in an inducible T cell clone in vitro. J. Immunol. 151, 6801-6814 (1993).
    • (1993) J. Immunol. , vol.151 , pp. 6801-6814
    • Qian, L.1    Vu, M.N.2    Carter, M.S.3    Doskow, J.4    Wilkinson, M.F.5
  • 141
    • 0027388887 scopus 로고
    • Evidence to implicate translation by ribosomes in the mechanism by which nonsense codons reduce the nuclear level of human triosephosphate isomerase mRNA
    • Belgrader, P., Cheng, J. & Maquat, L. E. Evidence to implicate translation by ribosomes in the mechanism by which nonsense codons reduce the nuclear level of human triosephosphate isomerase mRNA. Proc. Natl Acad. Sci. USA 90, 482-486 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 482-486
    • Belgrader, P.1    Cheng, J.2    Maquat, L.E.3
  • 142
    • 0031004756 scopus 로고    scopus 로고
    • T cell receptor (TCR) mini-gene mRNA expression regulated by nonsense codons: A nuclear-associated translation-like mechanism
    • Li, S., Leonard, D. & Wilkinson, M. F. T cell receptor (TCR) mini-gene mRNA expression regulated by nonsense codons: a nuclear-associated translation-like mechanism. J. Exp. Med. 185, 985-992 (1997).
    • (1997) J. Exp. Med. , vol.185 , pp. 985-992
    • Li, S.1    Leonard, D.2    Wilkinson, M.F.3
  • 143
    • 0026694808 scopus 로고
    • Nonsense mutations inhibit splicing of MVM RNA in cis when they interrupt the reading frame of either exon of the final spliced product
    • Naeger, L. K., Schoborg, R. V., Zhao, Q., Tullis, G. E. & Pintel, D. J. Nonsense mutations inhibit splicing of MVM RNA in cis when they interrupt the reading frame of either exon of the final spliced product. Genes Dev. 6, 1107-1119 (1992).
    • (1992) Genes Dev. , vol.6 , pp. 1107-1119
    • Naeger, L.K.1    Schoborg, R.V.2    Zhao, Q.3    Tullis, G.E.4    Pintel, D.J.5
  • 144
    • 0028136599 scopus 로고
    • Maintenance of an open reading frame as an additional level of scrutiny during splice site selection
    • Dietz, H. C. & Kendzior, R. J. Jr. Maintenance of an open reading frame as an additional level of scrutiny during splice site selection. Nature Genet. 8, 183-188 (1994).
    • (1994) Nature Genet. , vol.8 , pp. 183-188
    • Dietz, H.C.1    Kendzior R.J., Jr.2
  • 145
    • 0032006979 scopus 로고    scopus 로고
    • Nonsense surveillance in lymphocytes?
    • Li, S. & Wilkinson, M. F. Nonsense surveillance in lymphocytes? Immunity 8, 135-141 (1998).
    • (1998) Immunity , vol.8 , pp. 135-141
    • Li, S.1    Wilkinson, M.F.2
  • 146
    • 0033019838 scopus 로고    scopus 로고
    • A premature termination codon interferes with the nuclear function of an exon splicing enhancer in an open reading frame-dependent manner
    • Gersappe, A. & Pintel, D. J. A premature termination codon interferes with the nuclear function of an exon splicing enhancer in an open reading frame-dependent manner. Mol. Cell. Biol. 19, 1640-1650 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1640-1650
    • Gersappe, A.1    Pintel, D.J.2
  • 147
    • 0031896755 scopus 로고    scopus 로고
    • Selenium deficiency reduces the abundance of mRNA for Se-dependent glutathione peroxidase 1 by a UGA-dependent mechanism likey to be nonsense codon-mediated decay of cytoplasmic mRNA
    • Moriarty, P. M., Reddy, C. C. & Maquat, L. E. Selenium deficiency reduces the abundance of mRNA for Se-dependent glutathione peroxidase 1 by a UGA-dependent mechanism likey to be nonsense codon-mediated decay of cytoplasmic mRNA. Mol. Cell. Biol. 18, 2932-2939 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2932-2939
    • Moriarty, P.M.1    Reddy, C.C.2    Maquat, L.E.3
  • 148
    • 0032509304 scopus 로고    scopus 로고
    • Proofreading and aminoacylation of tRNAs before export from the nucleus
    • Lund, E. & Dahlberg, J. E. Proofreading and aminoacylation of tRNAs before export from the nucleus. Science 282, 2082-2085 (1998).
    • (1998) Science , vol.282 , pp. 2082-2085
    • Lund, E.1    Dahlberg, J.E.2
  • 149
    • 0034707668 scopus 로고    scopus 로고
    • Nuclear eukaryotic initiation factor 4E (eIF4E) colocalizes with splicing factors in speckles
    • Dostie, J., Lejbkowicz, F. & Sonenberg, N. Nuclear eukaryotic initiation factor 4E (eIF4E) colocalizes with splicing factors in speckles. J. Cell Biol. 148, 239-247 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 239-247
    • Dostie, J.1    Lejbkowicz, F.2    Sonenberg, N.3
  • 150
    • 0035839002 scopus 로고    scopus 로고
    • Coupled transcription and translation within nuclei of mammalian cells
    • Iborra, F. J., Jackson, D. A. & Cook, P. R. Coupled transcription and translation within nuclei of mammalian cells. Science 293, 1139-1142 (2001).
    • (2001) Science , vol.293 , pp. 1139-1142
    • Iborra, F.J.1    Jackson, D.A.2    Cook, P.R.3
  • 151
    • 0035823036 scopus 로고    scopus 로고
    • Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20
    • Ishigaki, Y., Li, X., Serin, G. & Maquat, L. E. Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20. Cell 106, 607-617 (2001).
    • (2001) Cell , vol.106 , pp. 607-617
    • Ishigaki, Y.1    Li, X.2    Serin, G.3    Maquat, L.E.4
  • 152
    • 2642656314 scopus 로고    scopus 로고
    • The surveillance complex interacts with the translation release factors to enhance termination and degrade aberrant mRNAs
    • Czaplinski, K. et al. The surveillance complex interacts with the translation release factors to enhance termination and degrade aberrant mRNAs. Genes Dev. 12, 1665-1677 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 1665-1677
    • Czaplinski, K.1
  • 153
    • 0025786141 scopus 로고
    • The product of the yeast UPF1 gene is required for rapid turnover of mRNAs containing a premature translational termination codon
    • Leeds, P., Peltz, S. W., Jacobson, A. & Culbertson, M. R. The product of the yeast UPF1 gene is required for rapid turnover of mRNAs containing a premature translational termination codon. Genes Dev. 5, 2303-2314 (1991).
    • (1991) Genes Dev. , vol.5 , pp. 2303-2314
    • Leeds, P.1    Peltz, S.W.2    Jacobson, A.3    Culbertson, M.R.4
  • 154
    • 0028934876 scopus 로고
    • Identification and characterization of genes that are required for the accelerated degradation of mRNAs containing a premature translational termination codon
    • Cui, Y., Hagan, K. W., Zhang, S. & Peltz, S. W. Identification and characterization of genes that are required for the accelerated degradation of mRNAs containing a premature translational termination codon. Genes Dev. 9, 423-436 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 423-436
    • Cui, Y.1    Hagan, K.W.2    Zhang, S.3    Peltz, S.W.4
  • 155
    • 0033679905 scopus 로고    scopus 로고
    • The yeast hnRNP-like protein Hrp1/Nab4 marks a transcript for nonsense-mediated mRNA decay
    • Gonzalez, C. I., Ruiz-Echevarria, M. J., Vasudevan, S., Henry, M. F. & Peltz, S. W. The yeast hnRNP-like protein Hrp1/Nab4 marks a transcript for nonsense-mediated mRNA decay. Mol. Cell 5, 489-499 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 489-499
    • Gonzalez, C.I.1    Ruiz-Echevarria, M.J.2    Vasudevan, S.3    Henry, M.F.4    Peltz, S.W.5
  • 157
    • 0034460323 scopus 로고    scopus 로고
    • Novel Upf2p orthologues suggest a functional link between translation initiation and nonsense surveillance complexes
    • Mendell, J. T., Medghalchi, S. M., Lake, R. G., Noensie, E. N. & Dietz, H. C. Novel Upf2p orthologues suggest a functional link between translation initiation and nonsense surveillance complexes. Mol. Cell. Biol. 20, 8944-8957 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8944-8957
    • Mendell, J.T.1    Medghalchi, S.M.2    Lake, R.G.3    Noensie, E.N.4    Dietz, H.C.5
  • 158
    • 0034751160 scopus 로고    scopus 로고
    • Identification and characterization of human orthologues to Saccharomyces cerevisiae Upf2 protein and Upf3 protein (Caenorhabditis elegans SMG-4)
    • Serin, G., Gersappe, A., Black, J. D., Aronoff, R. & Maquat, L. E. Identification and characterization of human orthologues to Saccharomyces cerevisiae Upf2 protein and Upf3 protein (Caenorhabditis elegans SMG-4). Mol. Cell. Biol. 21, 209-223 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 209-223
    • Serin, G.1    Gersappe, A.2    Black, J.D.3    Aronoff, R.4    Maquat, L.E.5
  • 159
    • 0027407911 scopus 로고
    • The skipping of constitutive exons in vivo induced by nonsense mutations
    • Dietz, H. C. et al. The skipping of constitutive exons in vivo induced by nonsense mutations. Science 259, 680-683 (1993).
    • (1993) Science , vol.259 , pp. 680-683
    • Dietz, H.C.1
  • 160
    • 0028147091 scopus 로고
    • Low cytoplasmic mRNA levels of immunoglobulin κ light chain genes containing nonsense codons correlate with inefficient splicing
    • Lozano, F., Maertzdorf, B., Pannell, R. & Milstein, C. Low cytoplasmic mRNA levels of immunoglobulin κ light chain genes containing nonsense codons correlate with inefficient splicing. EMBO J. 13, 4617-4622 (1994).
    • (1994) EMBO J. , vol.13 , pp. 4617-4622
    • Lozano, F.1    Maertzdorf, B.2    Pannell, R.3    Milstein, C.4
  • 161
    • 15844406352 scopus 로고    scopus 로고
    • Nonsense mutations inhibit RNA splicing in a cell-free system: Recognition of mutant codon is independent of protein synthesis
    • Aoufouchi, S., Yelamos, J. & Milstein, C. Nonsense mutations inhibit RNA splicing in a cell-free system: recognition of mutant codon is independent of protein synthesis. Cell 85, 415-422 (1996).
    • (1996) Cell , vol.85 , pp. 415-422
    • Aoufouchi, S.1    Yelamos, J.2    Milstein, C.3
  • 162
    • 0034886974 scopus 로고    scopus 로고
    • Precursor RNAs harboring nonsense codons accumulate near the site of transcription
    • Muhlemann, O. et al. Precursor RNAs harboring nonsense codons accumulate near the site of transcription. Mol. Cell 8, 33-43 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 33-43
    • Muhlemann, O.1
  • 163
    • 0034848163 scopus 로고    scopus 로고
    • A new view of mRNA export: Separating the wheat from the chaff
    • Reed, R. & Magni, K. A new view of mRNA export: separating the wheat from the chaff. Nature Cell Biol. 3, E201-E204 (2001).
    • (2001) Nature Cell Biol. , vol.3
    • Reed, R.1    Magni, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.