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Volumn 1, Issue 5, 2010, Pages

Binding properties and dynamic localization of an alternative isoform of the cap-binding complex subunit CBP20

Author keywords

7 methyl guanosine; Alternative splicing; CBC; CBP20; Nucleolar caps

Indexed keywords

7 METHYL GUANOSINE CAP BINDING PROTEIN; CAP BINDING COMPLEX CBP20; CAP BINDING COMPLEX CBP20S; CAP BINDING COMPLEX CBP80; CAP BINDING PROTEIN; MESSENGER RNA; NUCLEAR CAP BINDING PROTEIN; NUCLEIC ACID BINDING PROTEIN; PROTEIN; RNA; UNCLASSIFIED DRUG; CAPPED RNA; ISOPROTEIN;

EID: 77957679852     PISSN: 19491034     EISSN: 19491042     Source Type: Journal    
DOI: 10.4161/nucl.1.5.12839     Document Type: Article
Times cited : (18)

References (45)
  • 1
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: Design principles of a dynamic RNP machine
    • Wahl MC, Will CL, Luhrmann R. The spliceosome: Design principles of a dynamic RNP machine. Cell 2009; 136:701-18.
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1    Will, C.L.2    Luhrmann, R.3
  • 2
    • 75849145292 scopus 로고    scopus 로고
    • Expansion of the eukaryotic proteome by alternative splicing
    • Nilsen TW, Graveley BR. Expansion of the eukaryotic proteome by alternative splicing. Nature 2010; 463:457-63.
    • (2010) Nature , vol.463 , pp. 457-463
    • Nilsen, T.W.1    Graveley, B.R.2
  • 3
    • 0013394889 scopus 로고    scopus 로고
    • Mechanisms of alternative pre-messenger RNA splicing
    • Black DL. Mechanisms of alternative pre-messenger RNA splicing. Annu Rev Biochem 2003; 72:291-336.
    • (2003) Annu Rev Biochem , vol.72 , pp. 291-336
    • Black, D.L.1
  • 5
    • 33947305594 scopus 로고    scopus 로고
    • Ultraconserved elements are associated with homeostatic control of splicing regulators by alternative splicing and nonsense-mediated decay
    • Ni JZ, Grate L, Donohue JP, Preston C, Nobida N, O'Brien G, et al. Ultraconserved elements are associated with homeostatic control of splicing regulators by alternative splicing and nonsense-mediated decay. Genes Dev 2007; 21:708-18.
    • (2007) Genes Dev , vol.21 , pp. 708-718
    • Ni, J.Z.1    Grate, L.2    Donohue, J.P.3    Preston, C.4    Nobida, N.5    O'Brien, G.6
  • 7
    • 0346124413 scopus 로고    scopus 로고
    • Autoregulation of polypyrimidine tract binding protein by alternative splicing leading to nonsense-mediated decay
    • Wollerton MC, Gooding C, Wagner EJ, Garcia-Blanco MA, Smith CW. Autoregulation of polypyrimidine tract binding protein by alternative splicing leading to nonsense-mediated decay. Mol Cell 2004; 13:91-100.
    • (2004) Mol Cell , vol.13 , pp. 91-100
    • Wollerton, M.C.1    Gooding, C.2    Wagner, E.J.3    Garcia-Blanco, M.A.4    Smith, C.W.5
  • 8
    • 75149194407 scopus 로고    scopus 로고
    • Autoregulation of Fox protein expression to produce dominant negative splicing factors
    • Damianov A, Black DL. Autoregulation of Fox protein expression to produce dominant negative splicing factors. RNA 2010; 16:405-16.
    • (2010) RNA , vol.16 , pp. 405-416
    • Damianov, A.1    Black, D.L.2
  • 11
    • 34247552158 scopus 로고    scopus 로고
    • NELF interacts with CBC and participates in 3' end processing of replication-dependent histone mRNAs
    • Narita T, Yung TM, Yamamoto J, Tsuboi Y, Tanabe H, Tanaka K, et al. NELF interacts with CBC and participates in 3' end processing of replication-dependent histone mRNAs. Mol Cell 2007; 26:349-65.
    • (2007) Mol Cell , vol.26 , pp. 349-365
    • Narita, T.1    Yung, T.M.2    Yamamoto, J.3    Tsuboi, Y.4    Tanabe, H.5    Tanaka, K.6
  • 12
    • 27144478105 scopus 로고    scopus 로고
    • CBP80 promotes interaction of Upf1 with Upf2 during nonsense- mediated mRNA decay in mammalian cells
    • Hosoda N, Kim YK, Lejeune F, Maquat LE. CBP80 promotes interaction of Upf1 with Upf2 during nonsense- mediated mRNA decay in mammalian cells. Nat Struct Mol Biol 2005; 12:893-901.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 893-901
    • Hosoda, N.1    Kim, Y.K.2    Lejeune, F.3    Maquat, L.E.4
  • 13
    • 0036645697 scopus 로고    scopus 로고
    • The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: Dynamics of mRNP remodeling
    • Lejeune F, Ishigaki Y, Li X, Maquat LE. The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: Dynamics of mRNP remodeling. EMBO J 2002; 21:3536-45.
    • (2002) EMBO J , vol.21 , pp. 3536-3545
    • Lejeune, F.1    Ishigaki, Y.2    Li, X.3    Maquat, L.E.4
  • 15
    • 33845626622 scopus 로고    scopus 로고
    • Human mRNA export machinery recruited to the 5' end of mRNA
    • Cheng H, Dufu K, Lee CS, Hsu JL, Dias A, Reed R. Human mRNA export machinery recruited to the 5' end of mRNA. Cell 2006; 127:1389-400.
    • (2006) Cell , vol.127 , pp. 1389-1400
    • Cheng, H.1    Dufu, K.2    Lee, C.S.3    Hsu, J.L.4    Dias, A.5    Reed, R.6
  • 16
    • 47249089938 scopus 로고    scopus 로고
    • Dual roles of the nuclear cap-binding complex and SERRATE in pre-mRNA splicing and microRNA processing in Arabidopsis thaliana
    • Laubinger S, Sachsenberg T, Zeller G, Busch W, Lohmann JU, Ratsch G, et al. Dual roles of the nuclear cap-binding complex and SERRATE in pre-mRNA splicing and microRNA processing in Arabidopsis thaliana. Proc Natl Acad Sci USA 2008; 105:8795-800.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8795-8800
    • Laubinger, S.1    Sachsenberg, T.2    Zeller, G.3    Busch, W.4    Lohmann, J.U.5    Ratsch, G.6
  • 17
    • 67650590937 scopus 로고    scopus 로고
    • Ars2 links the nuclear cap-binding complex to RNA interference and cell proliferation
    • Gruber JJ, Zatechka DS, Sabin LR, Yong J, Lum JJ, Kong M, et al. Ars2 links the nuclear cap-binding complex to RNA interference and cell proliferation. Cell 2009; 138:328-39.
    • (2009) Cell , vol.138 , pp. 328-339
    • Gruber, J.J.1    Zatechka, D.S.2    Sabin, L.R.3    Yong, J.4    Lum, J.J.5    Kong, M.6
  • 18
    • 67650638926 scopus 로고    scopus 로고
    • Ars2 regulates both miRNA- and siRNA-dependent silencing and suppresses RNA virus infection in Drosophila
    • Sabin LR, Zhou R, Gruber JJ, Lukinova N, Bambina S, Berman A, et al. Ars2 regulates both miRNA- and siRNA-dependent silencing and suppresses RNA virus infection in Drosophila. Cell 2009; 138:340-51.
    • (2009) Cell , vol.138 , pp. 340-351
    • Sabin, L.R.1    Zhou, R.2    Gruber, J.J.3    Lukinova, N.4    Bambina, S.5    Berman, A.6
  • 19
    • 0034852936 scopus 로고    scopus 로고
    • Crystal structure of the human nuclear cap binding complex
    • Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. Crystal structure of the human nuclear cap binding complex. Mol Cell 2001; 8:383-96.
    • (2001) Mol Cell , vol.8 , pp. 383-396
    • Mazza, C.1    Ohno, M.2    Segref, A.3    Mattaj, I.W.4    Cusack, S.5
  • 20
    • 0037107401 scopus 로고    scopus 로고
    • Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex
    • Mazza C, Segref A, Mattaj IW, Cusack S. Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex. EMBO J 2002; 21:5548-57.
    • (2002) EMBO J , vol.21 , pp. 5548-5557
    • Mazza, C.1    Segref, A.2    Mattaj, I.W.3    Cusack, S.4
  • 22
    • 0035252410 scopus 로고    scopus 로고
    • Alternative splicing: Increasing diversity in the proteomic world
    • Graveley BR. Alternative splicing: Increasing diversity in the proteomic world. Trends Genet 2001; 17:100-7.
    • (2001) Trends Genet , vol.17 , pp. 100-107
    • Graveley, B.R.1
  • 23
    • 0036337915 scopus 로고    scopus 로고
    • A genomic view of alternative splicing
    • Modrek B, Lee C. A genomic view of alternative splicing. Nat Genet 2002; 30:13-9.
    • (2002) Nat Genet , vol.30 , pp. 13-19
    • Modrek, B.1    Lee, C.2
  • 24
    • 1642473041 scopus 로고    scopus 로고
    • How prevalent is functional alternative splicing in the human genome?
    • Sorek R, Shamir R, Ast G. How prevalent is functional alternative splicing in the human genome? Trends Genet 2004; 20:68-71.
    • (2004) Trends Genet , vol.20 , pp. 68-71
    • Sorek, R.1    Shamir, R.2    Ast, G.3
  • 25
    • 69049116283 scopus 로고    scopus 로고
    • Stochastic noise in splicing machinery
    • Melamud E, Moult J. Stochastic noise in splicing machinery. Nucleic Acids Res 2009; 37:4873-86.
    • (2009) Nucleic Acids Res , vol.37 , pp. 4873-4886
    • Melamud, E.1    Moult, J.2
  • 27
  • 29
    • 18244366043 scopus 로고    scopus 로고
    • Dynamic sorting of nuclear components into distinct nucleolar caps during transcriptional inhibition
    • Shav-Tal Y, Blechman J, Darzacq X, Montagna C, Dye BT, Patton JG, et al. Dynamic sorting of nuclear components into distinct nucleolar caps during transcriptional inhibition. Mol Biol Cell 2005; 16:2395-413.
    • (2005) Mol Biol Cell , vol.16 , pp. 2395-2413
    • Shav-Tal, Y.1    Blechman, J.2    Darzacq, X.3    Montagna, C.4    Dye, B.T.5    Patton, J.G.6
  • 30
    • 0037669010 scopus 로고    scopus 로고
    • Low conservation of alternative splicing patterns in the human and mouse genomes
    • Nurtdinov RN, Artamonova II, Mironov AA, Gelfand MS. Low conservation of alternative splicing patterns in the human and mouse genomes. Hum Mol Genet 2003; 12:1313-20.
    • (2003) Hum Mol Genet , vol.12 , pp. 1313-1320
    • Nurtdinov, R.N.1    Artamonova, I.I.2    Mironov, A.A.3    Gelfand, M.S.4
  • 31
    • 0026016404 scopus 로고
    • A naturally occurring truncated form of FosB that inhibits Fos/Jun transcriptional activity
    • Nakabeppu Y, Nathans D. A naturally occurring truncated form of FosB that inhibits Fos/Jun transcriptional activity. Cell 1991; 64:751-9.
    • (1991) Cell , vol.64 , pp. 751-759
    • Nakabeppu, Y.1    Nathans, D.2
  • 32
    • 0026587115 scopus 로고
    • Transformation by FosB requires a trans-activation domain missing in FosB2 that can be substituted by heterologous activation domains
    • Wisdom R, Yen J, Rashid D, Verma IM. Transformation by FosB requires a trans-activation domain missing in FosB2 that can be substituted by heterologous activation domains. Genes Dev 1992; 6:667-75.
    • (1992) Genes Dev , vol.6 , pp. 667-675
    • Wisdom, R.1    Yen, J.2    Rashid, D.3    Verma, I.M.4
  • 33
    • 0030272377 scopus 로고    scopus 로고
    • Importin provides a link between nuclear protein import and U snRNA export
    • Gorlich D, Kraft R, Kostka S, Vogel F, Hartmann E, Laskey RA, et al. Importin provides a link between nuclear protein import and U snRNA export. Cell 1996; 87:21-32.
    • (1996) Cell , vol.87 , pp. 21-32
    • Gorlich, D.1    Kraft, R.2    Kostka, S.3    Vogel, F.4    Hartmann, E.5    Laskey, R.A.6
  • 35
    • 77957659003 scopus 로고    scopus 로고
    • Unloading RNAs in the cytoplasm: An "importin" task
    • Dias, et al. Unloading RNAs in the cytoplasm: An "importin" task. Nucleus 2010; 1(2):139.
    • (2010) Nucleus , vol.1 , Issue.2 , pp. 139
    • Dias1
  • 36
    • 63449132795 scopus 로고    scopus 로고
    • Nuclear functions of heterogeneous nuclear ribonucleoproteins A/B
    • He Y, Smith R. Nuclear functions of heterogeneous nuclear ribonucleoproteins A/B. Cell Mol Life Sci 2009; 66:1239-56.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1239-1256
    • He, Y.1    Smith, R.2
  • 37
    • 0037032415 scopus 로고    scopus 로고
    • PSF and p54(nrb)/NonO- multi-functional nuclear proteins
    • Shav-Tal Y, Zipori D. PSF and p54(nrb)/NonO- multi-functional nuclear proteins. FEBS Lett 2002; 531:109-14.
    • (2002) FEBS Lett , vol.531 , pp. 109-114
    • Shav-Tal, Y.1    Zipori, D.2
  • 38
    • 0015716692 scopus 로고
    • A rapid, sensitive and specific method for the determination of protein in dilute solution
    • Schaffner W, Weissmann C. A rapid, sensitive and specific method for the determination of protein in dilute solution. Anal Biochem 1973; 56:502-14.
    • (1973) Anal Biochem , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 39
    • 33845411711 scopus 로고    scopus 로고
    • Enhancement of U4/U6 small nuclear ribonucleoprotein particle association in Cajal bodies predicted by mathematical modeling
    • Klingauf M, Stanek D, Neugebauer KM. Enhancement of U4/U6 small nuclear ribonucleoprotein particle association in Cajal bodies predicted by mathematical modeling. Mol Biol Cell 2006; 17:4972-81.
    • (2006) Mol Biol Cell , vol.17 , pp. 4972-4981
    • Klingauf, M.1    Stanek, D.2    Neugebauer, K.M.3
  • 40
    • 33748351186 scopus 로고    scopus 로고
    • Cotranscriptional coupling of splicing factor recruitment and precursor messenger RNA splicing in mammalian cells
    • Listerman I, Sapra AK, Neugebauer KM. Cotranscriptional coupling of splicing factor recruitment and precursor messenger RNA splicing in mammalian cells. Nat Struct Mol Biol 2006; 13:815-22.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 815-822
    • Listerman, I.1    Sapra, A.K.2    Neugebauer, K.M.3
  • 41
    • 26944490411 scopus 로고    scopus 로고
    • A combined approach for the localization and tandem affinity purification of protein complexes from metazoans
    • Cheeseman IM, Desai A. A combined approach for the localization and tandem affinity purification of protein complexes from metazoans. Sci STKE 2005; 11.
    • (2005) Sci STKE , pp. 11
    • Cheeseman, I.M.1    Desai, A.2
  • 42
    • 66249131877 scopus 로고    scopus 로고
    • Comparative profiling identifies C13orf3 as a component of the Ska complex required for mammalian cell division
    • Theis M, Slabicki M, Junqueira M, Paszkowski-Rogacz M, Sontheimer J, Kittler R, et al. Comparative profiling identifies C13orf3 as a component of the Ska complex required for mammalian cell division. EMBO J 2009; 28:1453-65.
    • (2009) EMBO J , vol.28 , pp. 1453-1465
    • Theis, M.1    Slabicki, M.2    Junqueira, M.3    Paszkowski-Rogacz, M.4    Sontheimer, J.5    Kittler, R.6
  • 43
    • 53049085543 scopus 로고    scopus 로고
    • Separating the wheat from the chaff: Unbiased filtering of background tandem mass spectra improves protein identification
    • Junqueira M, Spirin V, Santana Balbuena T, Waridel P, Surendranath V, Kryukov G, et al. Separating the wheat from the chaff: unbiased filtering of background tandem mass spectra improves protein identification. J Proteome Res 2008; 7:3382-95.
    • (2008) J Proteome Res , vol.7 , pp. 3382-3395
    • Junqueira, M.1    Spirin, V.2    Santana Balbuena, T.3    Waridel, P.4    Surendranath, V.5    Kryukov, G.6
  • 44
    • 57949091054 scopus 로고    scopus 로고
    • Chromatin Central: Towards the comparative proteome by accurate mapping of the yeast proteomic environment
    • Shevchenko A, Roguev A, Schaft D, Buchanan L, Habermann B, Sakalar C, et al. Chromatin Central: Towards the comparative proteome by accurate mapping of the yeast proteomic environment. Genome Biol 2008; 9:167.
    • (2008) Genome Biol , vol.9 , pp. 167
    • Shevchenko, A.1    Roguev, A.2    Schaft, D.3    Buchanan, L.4    Habermann, B.5    Sakalar, C.6
  • 45
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A, Nesvizhskii AI, Kolker E, Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 2002; 74:5383-92.
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4


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