메뉴 건너뛰기




Volumn 23, Issue 20, 2003, Pages 7363-7376

Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; NUCLEAR PROTEIN; OLIGONUCLEOTIDE; PNN PROTEIN; POLYADENYLATED RNA; RIBONUCLEASE H; RIBONUCLEOPROTEIN; RIBONUCLEOPROTEIN S1; UNCLASSIFIED DRUG;

EID: 0141752774     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.20.7363-7376.2003     Document Type: Article
Times cited : (60)

References (49)
  • 1
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi, U., J. Cohn, L. Buhle, and L. Gerace. 1986. The nuclear lamina is a meshwork of intermediate-type filaments. Nature 323:560-564.
    • (1986) Nature , vol.323 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 3
    • 0031441091 scopus 로고    scopus 로고
    • Evidence that "pnn," reportedly a differentiation-specific desmosomal protein, is actually a widespread nuclear protein
    • Brandner, J. M., S. Reidenbach, and W. W. Franke. 1997. Evidence that "pnn," reportedly a differentiation-specific desmosomal protein, is actually a widespread nuclear protein. Differentiation 62:119-127.
    • (1997) Differentiation , vol.62 , pp. 119-127
    • Brandner, J.M.1    Reidenbach, S.2    Franke, W.W.3
  • 4
    • 0031966818 scopus 로고    scopus 로고
    • Identification and characterization of a novel kind of nuclear protein occurring free in the nucleoplasm and in ribonucleoprotein structures of the "speckle" type
    • Brandner, J. M., S. Reidenbach, C. Kuhn, and W. W. Franke. 1998. Identification and characterization of a novel kind of nuclear protein occurring free in the nucleoplasm and in ribonucleoprotein structures of the "speckle" type. Eur. J. Cell Biol. 75:295-308.
    • (1998) Eur. J. Cell Biol. , vol.75 , pp. 295-308
    • Brandner, J.M.1    Reidenbach, S.2    Kuhn, C.3    Franke, W.W.4
  • 5
    • 0034544815 scopus 로고    scopus 로고
    • Pre-mRNA processing factors are required for nuclear export
    • Brodsky, A. S., and P. A. Silver. 2000. Pre-mRNA processing factors are required for nuclear export. RNA 6:1737-1749.
    • (2000) RNA , vol.6 , pp. 1737-1749
    • Brodsky, A.S.1    Silver, P.A.2
  • 7
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D., R. M. Lebovitz, and R. G. Roeder. 1983. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 8
    • 0037046798 scopus 로고    scopus 로고
    • Translation is required to remove Y14 from mRNAs in the cytoplasm
    • Dostie, J., and G. Dreyfuss. 2002. Translation is required to remove Y14 from mRNAs in the cytoplasm. Curr. Biol. 12:1060-1067.
    • (2002) Curr. Biol. , vol.12 , pp. 1060-1067
    • Dostie, J.1    Dreyfuss, G.2
  • 9
    • 0026437581 scopus 로고
    • General splicing factors SF2 and SC35 have equivalent activities in vitro, and both affect alternative 5′ and 3′ splice site selection
    • Fu, X., A. Mayeda, T. Maniatis, and A. R. Krainer. 1992. General splicing factors SF2 and SC35 have equivalent activities in vitro, and both affect alternative 5′ and 3′ splice site selection. Proc. Natl. Acad. Sci. USA 89:11224-11228.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11224-11228
    • Fu, X.1    Mayeda, A.2    Maniatis, T.3    Krainer, A.R.4
  • 10
    • 0035976612 scopus 로고    scopus 로고
    • Delineation of mRNA export pathways by the use of cell-permeable peptides
    • Gallouzi, I. E., and J. A. Steitz. 2001. Delineation of mRNA export pathways by the use of cell-permeable peptides. Science 294:1895-1901.
    • (2001) Science , vol.294 , pp. 1895-1901
    • Gallouzi, I.E.1    Steitz, J.A.2
  • 11
    • 0037175374 scopus 로고    scopus 로고
    • REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export
    • Gatfield, D., and E. Izaurralde. 2002. REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export. J. Cell Biol. 159:579-588.
    • (2002) J. Cell Biol. , vol.159 , pp. 579-588
    • Gatfield, D.1    Izaurralde, E.2
  • 13
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley, B. R. 2000. Sorting out the complexity of SR protein functions. RNA 6:1197-1211.
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 14
    • 0035975970 scopus 로고    scopus 로고
    • Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport
    • Hachet, O., and A. Ephrussi. 2001. Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport. Curr. Biol. 11:1666-1674.
    • (2001) Curr. Biol. , vol.11 , pp. 1666-1674
    • Hachet, O.1    Ephrussi, A.2
  • 15
    • 0033525169 scopus 로고    scopus 로고
    • A perfect message: RNA surveillance and nonsense-mediated decay
    • Hentze, M. W., and A. E. Kulozik. 1999. A perfect message: RNA surveillance and nonsense-mediated decay. Cell 96:307-310.
    • (1999) Cell , vol.96 , pp. 307-310
    • Hentze, M.W.1    Kulozik, A.E.2
  • 16
    • 0035671563 scopus 로고    scopus 로고
    • NXF1/p15 heterodimers are essential for mRNA nuclear export in Drosophila
    • Herold, A., T. Klymenko, and E. Izaurralde. 2001. NXF1/p15 heterodimers are essential for mRNA nuclear export in Drosophila. RNA 7:1768-1780.
    • (2001) RNA , vol.7 , pp. 1768-1780
    • Herold, A.1    Klymenko, T.2    Izaurralde, E.3
  • 17
    • 0344211508 scopus 로고    scopus 로고
    • SR splicing factors serve as adapter proteins for TAP-dependent mRNA export
    • Huang, Y., R. Gattoni, J. Stevenin, and J. A. Steitz. 2003. SR splicing factors serve as adapter proteins for TAP-dependent mRNA export. Mol. Cell 11:837-843.
    • (2003) Mol. Cell , vol.11 , pp. 837-843
    • Huang, Y.1    Gattoni, R.2    Stevenin, J.3    Steitz, J.A.4
  • 18
    • 0036343646 scopus 로고    scopus 로고
    • Nuclear localization of the tight junction protein ZO-2 in epithelial cells
    • Islas, S., J. Vega, L. Ponce, and L. Gonzalea-Mariscal. 2002. Nuclear localization of the tight junction protein ZO-2 in epithelial cells. Exp. Cell. Res. 274:138-148.
    • (2002) Exp. Cell. Res. , vol.274 , pp. 138-148
    • Islas, S.1    Vega, J.2    Ponce, L.3    Gonzalea-Mariscal, L.4
  • 19
    • 0036242097 scopus 로고    scopus 로고
    • Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis
    • Jurica, M. S., L. J. Licklider, S. R. Gygi, N. Grigorieff, and M. J. Moore. 2002. Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. RNA 8:426-439.
    • (2002) RNA , vol.8 , pp. 426-439
    • Jurica, M.S.1    Licklider, L.J.2    Gygi, S.R.3    Grigorieff, N.4    Moore, M.J.5
  • 20
    • 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., J. Yong, V. N. Kim, F. Velazquez, R. A. Perkinson, F. Wang, and G. Dreyfuss. 2000. 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) Mol. Cell , vol.6 , pp. 673-682
    • Kataoka, N.1    Yong, J.2    Kim, V.N.3    Velazquez, F.4    Perkinson, R.A.5    Wang, F.6    Dreyfuss, G.7
  • 21
    • 0035823150 scopus 로고    scopus 로고
    • Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex
    • Kim, V. N., N. Kataoka, and G. Dreyfuss. 2001. Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex. Science 293:1832-1836.
    • (2001) Science , vol.293 , pp. 1832-1836
    • Kim, V.N.1    Kataoka, N.2    Dreyfuss, G.3
  • 22
    • 0029891101 scopus 로고    scopus 로고
    • The structure and function of proteins involved in mammalian pre-mRNA splicing
    • Kramer, A. 1996. The structure and function of proteins involved in mammalian pre-mRNA splicing. Annu. Rev. Biochem. 65:367-409.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 367-409
    • Kramer, A.1
  • 23
    • 0039550795 scopus 로고    scopus 로고
    • A human papillomavirus E2 transcriptional activator. The interactions with cellular splicing factors and potential function in pre-mRNA processing
    • Lai, M. C., B. H. Teh, and W. Y. Tarn. 1999. A human papillomavirus E2 transcriptional activator. The interactions with cellular splicing factors and potential function in pre-mRNA processing. J. Biol. Chem. 274:11832-11841.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11832-11841
    • Lai, M.C.1    Teh, B.H.2    Tarn, W.Y.3
  • 24
    • 0034193569 scopus 로고    scopus 로고
    • Pre-mRNA splicing alters mRNP composition: Evidence for stable association of proteins at exon-exon junction
    • Le Hir, H., M. J. Moore, and L. E. Maquat. 2000. Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junction. Genes Dev. 14:1098-1108.
    • (2000) Genes Dev. , vol.14 , pp. 1098-1108
    • Le Hir, H.1    Moore, M.J.2    Maquat, L.E.3
  • 25
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
    • Le Hir, H., E. Izaurralde, L. E. Maquat, and M. J. Moore. 2000. The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. EMBO J. 19:6860-6869.
    • (2000) EMBO J. , vol.19 , pp. 6860-6869
    • Le Hir, H.1    Izaurralde, E.2    Maquat, L.E.3    Moore, M.J.4
  • 26
    • 0035801373 scopus 로고    scopus 로고
    • The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated decay
    • Le Hir, H., D. Gatfield, E. Izaurralde, and M. J. Moore. 2001. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated decay. EMBO J. 20:4987-4997.
    • (2001) EMBO J. , vol.20 , pp. 4987-4997
    • Le Hir, H.1    Gatfield, D.2    Izaurralde, E.3    Moore, M.J.4
  • 27
    • 0037407941 scopus 로고    scopus 로고
    • Analysis of the stimulatory effect of splicing on mRNA production and utilization in mammalian cells
    • Lu, S., and B. R. Cullen. 2003. Analysis of the stimulatory effect of splicing on mRNA production and utilization in mammalian cells. RNA 9:618-630.
    • (2003) RNA , vol.9 , pp. 618-630
    • Lu, S.1    Cullen, B.R.2
  • 28
    • 0033592896 scopus 로고    scopus 로고
    • Splicing is required for rapid and efficient mRNA export in metazoans
    • Luo, M., and R. Reed. 1999. Splicing is required for rapid and efficient mRNA export in metazoans. Proc. Natl. Acad. Sci. USA 96:14937-14942.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14937-14942
    • Luo, M.1    Reed, R.2
  • 29
    • 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., M. D. Shu, and J. A. Steitz. 2001. Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1. Science 293:1836-1839.
    • (2001) Science , vol.293 , pp. 1836-1839
    • Lykke-Andersen, J.1    Shu, M.D.2    Steitz, J.A.3
  • 30
    • 0036132667 scopus 로고    scopus 로고
    • SRm160 splicing coactivator promotes transcript 3′-end cleavage
    • McCracken, S., M. Lambermon, and B. J. Blencowe. 2002. SRm160 splicing coactivator promotes transcript 3′-end cleavage. Mol. Cell. Biol. 22:148-160.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 148-160
    • McCracken, S.1    Lambermon, M.2    Blencowe, B.J.3
  • 31
    • 0032055114 scopus 로고    scopus 로고
    • Nuclear history of a pre-mRNA determines the translational activity of cytoplasmic mRNA
    • Matsumoto, K., K. M. Wassarman, and A. P. Wolffe. 1998. Nuclear history of a pre-mRNA determines the translational activity of cytoplasmic mRNA. EMBO J. 17:2107-2121.
    • (1998) EMBO J. , vol.17 , pp. 2107-2121
    • Matsumoto, K.1    Wassarman, K.M.2    Wolffe, A.P.3
  • 32
    • 0033575702 scopus 로고    scopus 로고
    • Purification and characterization of human RNPS1: A general activator of pre-mRNA splicing
    • Mayeda, A., J. Badolato, R. Kobayashi, M. Q. Zhang, E. M., Gardiner, and A. R. Krainer. 1999. Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing. EMBO J. 16:4560-4570.
    • (1999) EMBO J. , vol.16 , pp. 4560-4570
    • Mayeda, A.1    Badolato, J.2    Kobayashi, R.3    Zhang, M.Q.4    Gardiner, E.M.5    Krainer, A.R.6
  • 34
    • 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., S. T. Dillon, and R. Boswell. 2001. 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) Genes Dev. , vol.15 , pp. 2886-2899
    • Mohr, S.E.1    Dillon, S.T.2    Boswell, R.3
  • 35
    • 0037406116 scopus 로고    scopus 로고
    • A quantitative analysis of intron effects on mammalian gene expression
    • Nott, A., S. H. Meislin, and M. J. Moore. 2003. A quantitative analysis of intron effects on mammalian gene expression. RNA 9:607-617.
    • (2003) RNA , vol.9 , pp. 607-617
    • Nott, A.1    Meislin, S.H.2    Moore, M.J.3
  • 36
    • 0036211993 scopus 로고    scopus 로고
    • Identity elements used in export of mRNAs
    • Ohno, M., A. Segref, S. Kuersten, and I. W. Mattaj. 2002. Identity elements used in export of mRNAs. Mol. Cell 9:659-671.
    • (2002) Mol. Cell , vol.9 , pp. 659-671
    • Ohno, M.1    Segref, A.2    Kuersten, S.3    Mattaj, I.W.4
  • 37
    • 0026709315 scopus 로고
    • Identification of an epithelial protein related to the desmosome and intermediate filament network
    • Ouyang, P., and S. P. Sugrue. 1992. Identification of an epithelial protein related to the desmosome and intermediate filament network. J. Cell Biol. 118:1477-1488.
    • (1992) J. Cell Biol. , vol.118 , pp. 1477-1488
    • Ouyang, P.1    Sugrue, S.P.2
  • 38
    • 0029836931 scopus 로고    scopus 로고
    • Characterization of Pinin, a novel protein associated with the desmosome-intermediate filament complex
    • Ouyang, P., and S. P. Sugrue. 1996. Characterization of Pinin, a novel protein associated with the desmosome-intermediate filament complex. J. Cell Biol. 135:1027-1042.
    • (1996) J. Cell Biol. , vol.135 , pp. 1027-1042
    • Ouyang, P.1    Sugrue, S.P.2
  • 39
    • 0033575934 scopus 로고    scopus 로고
    • Antibodies differentiate desmosome-form and nucleus-form Pinin: Evidence that Pinin is a moonlighting protein with dual location at the desmosome and within the nucleus
    • Ouyang, P. 1999. Antibodies differentiate desmosome-form and nucleus-form Pinin: evidence that Pinin is a moonlighting protein with dual location at the desmosome and within the nucleus. Biochem. Biophys. Res. Commun. 263:192-200.
    • (1999) Biochem. Biophys. Res. Commun. , vol.263 , pp. 192-200
    • Ouyang, P.1
  • 40
    • 0037154964 scopus 로고    scopus 로고
    • A conserved mRNA export machinery coupled to pre-mRNA splicing
    • Reed, R., and E. Hurt. 2002. A conserved mRNA export machinery coupled to pre-mRNA splicing. Cell 108:523-531.
    • (2002) Cell , vol.108 , pp. 523-531
    • Reed, R.1    Hurt, E.2
  • 43
    • 0034642508 scopus 로고    scopus 로고
    • Characterization of the gene encoding pnn/DRS/memA and evidence for its potential tumor suppressor function
    • Shi, Y., P. Ouyang, and S. P. Sugrue. 2000. Characterization of the gene encoding pnn/DRS/memA and evidence for its potential tumor suppressor function. Oncogene 19:289-297.
    • (2000) Oncogene , vol.19 , pp. 289-297
    • Shi, Y.1    Ouyang, P.2    Sugrue, S.P.3
  • 45
    • 0033984159 scopus 로고    scopus 로고
    • Complex protein interactions within the human polyadenylation machinery identify a novel component
    • Takagaki, Y., and J. L. Manley. 2000. Complex protein interactions within the human polyadenylation machinery identify a novel component. Mol. Cell. Biol. 20:1515-1525.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1515-1525
    • Takagaki, Y.1    Manley, J.L.2
  • 46
    • 0028072388 scopus 로고
    • SR proteins can compensate for the loss of U1 snRNP functions in vitro
    • Tarn, W. Y., and J. A. Steitz. 1994. SR proteins can compensate for the loss of U1 snRNP functions in vitro. Genes Dev. 8:2704-2717.
    • (1994) Genes Dev. , vol.8 , pp. 2704-2717
    • Tarn, W.Y.1    Steitz, J.A.2
  • 47
    • 0036289156 scopus 로고    scopus 로고
    • Modulation of alternative pre-mRNA splicing in vivo by Pinin
    • Wang, P., P. J. Lou, S. Leu, and P. Ouyang. 2002. Modulation of alternative pre-mRNA splicing in vivo by Pinin. Biochem. Biophy. Res. Commun. 294:448-455.
    • (2002) Biochem. Biophy. Res. Commun. , vol.294 , pp. 448-455
    • Wang, P.1    Lou, P.J.2    Leu, S.3    Ouyang, P.4
  • 48
    • 0026716104 scopus 로고
    • SR proteins: A conserved family of pre-mRNA splicing factors
    • Zahler, A. M., W. S. Lane, J. A. Stolk, and M. B. Roth. 1992. SR proteins: a conserved family of pre-mRNA splicing factors. Genes Dev. 6:837-847.
    • (1992) Genes Dev. , vol.6 , pp. 837-847
    • Zahler, A.M.1    Lane, W.S.2    Stolk, J.A.3    Roth, M.B.4
  • 49
    • 0034699472 scopus 로고    scopus 로고
    • The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans
    • Zhou, Z., M. J. Luo, K. Straesser, J. Katahira, E. Hurt, and R. Reed. 2000. The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans. Nature 407:401-405.
    • (2000) Nature , vol.407 , pp. 401-405
    • Zhou, Z.1    Luo, M.J.2    Straesser, K.3    Katahira, J.4    Hurt, E.5    Reed, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.