메뉴 건너뛰기




Volumn 30, Issue 21, 2010, Pages 4996-5008

Nuclear import of cytoplasmic poly(A) binding protein restricts gene expression via hyperadenylation and nuclear retention of mRNA

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; POLYADENYLIC ACID BINDING PROTEIN; POLYADENYLIC ACID BINDING PROTEIN 1; POLYADENYLIC ACID BINDING PROTEIN 4; RNA POLYMERASE II; UNCLASSIFIED DRUG; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; RECOMBINANT PROTEIN; SMALL INTERFERING RNA; VIRUS PROTEIN;

EID: 77957853228     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00600-10     Document Type: Article
Times cited : (90)

References (75)
  • 1
    • 0032557655 scopus 로고    scopus 로고
    • The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm
    • Afonina, E., R. Stauber, and G. N. Pavlakis. 1998. The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm. J. Biol. Chem. 273:13015-13021.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13015-13021
    • Afonina, E.1    Stauber, R.2    Pavlakis, G.N.3
  • 2
    • 65649125644 scopus 로고    scopus 로고
    • Nuclear RNA surveillance: No sign of substrates tailing off
    • Anderson, J. T., and X. Wang. 2009. Nuclear RNA surveillance: no sign of substrates tailing off. Crit. Rev. Biochem. Mol. Biol. 44:16-24.
    • (2009) Crit. Rev. Biochem. Mol. Biol. , vol.44 , pp. 16-24
    • Anderson, J.T.1    Wang, X.2
  • 3
    • 60149100371 scopus 로고    scopus 로고
    • Activation of host translational control pathways by a viral developmental switch
    • Arias, C., D. Walsh, J. Harbell, A. C. Wilson, and I. Mohr. 2009. Activation of host translational control pathways by a viral developmental switch. PLoS Pathog. 5:e1000334.
    • (2009) PLoS Pathog. , vol.5
    • Arias, C.1    Walsh, D.2    Harbell, J.3    Wilson, A.C.4    Mohr, I.5
  • 4
    • 0038523775 scopus 로고    scopus 로고
    • Host range of Kaposi's sarcoma-associated herpesvirus in cultured cells
    • Bechtel, J. T., Y. Liang, J. Hvidding, and D. Ganem. 2003. Host range of Kaposi's sarcoma-associated herpesvirus in cultured cells. J. Virol. 77:6474-6481.
    • (2003) J. Virol. , vol.77 , pp. 6474-6481
    • Bechtel, J.T.1    Liang, Y.2    Hvidding, J.3    Ganem, D.4
  • 5
    • 33947609704 scopus 로고    scopus 로고
    • A conserved role for cytoplasmic poly(A)-binding protein 1 (PABPC1) in nonsense-mediated mRNA decay
    • DOI 10.1038/sj.emboj.7601588, PII 7601588
    • Behm-Ansmant, I., D. Gatfield, J. Rehwinkel, V. Hilgers, and E. Izaurralde. 2007. A conserved role for cytoplasmic poly(A)-binding protein 1 (PABPC1) in nonsense-mediated mRNA decay. EMBO J. 26:1591-1601. (Pubitemid 46480926)
    • (2007) EMBO Journal , vol.26 , Issue.6 , pp. 1591-1601
    • Behm-Ansmant, I.1    Gatfield, D.2    Rehwinkel, J.3    Hilgers, V.4    Izaurralde, E.5
  • 6
    • 43149099925 scopus 로고    scopus 로고
    • Nuclear exclusion of the HIV-1 host defense factor APOBEC3G requires a novel cytoplasmic retention signal and is not dependent on RNA binding
    • Bennett, R. P., V. Presnyak, J. E. Wedekind, and H. C. Smith. 2008. Nuclear exclusion of the HIV-1 host defense factor APOBEC3G requires a novel cytoplasmic retention signal and is not dependent on RNA binding. J. Biol. Chem. 283:7320-7327.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7320-7327
    • Bennett, R.P.1    Presnyak, V.2    Wedekind, J.E.3    Smith, H.C.4
  • 7
    • 0024591905 scopus 로고
    • The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro
    • Bernstein, P., S. W. Peltz, and J. Ross. 1989. The poly(A)-poly(A)- binding protein complex is a major determinant of mRNA stability in vitro. Mol. Cell. Biol. 9:659-670.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 659-670
    • Bernstein, P.1    Peltz, S.W.2    Ross, J.3
  • 8
    • 64049115323 scopus 로고    scopus 로고
    • Bunyamwera orthobunyavirus S-segment untranslated regions mediate poly(A) tail-independent translation
    • Blakqori, G., I. van Knippenberg, and R. M. Elliott. 2009. Bunyamwera orthobunyavirus S-segment untranslated regions mediate poly(A) tail-independent translation. J. Virol. 83:3637-3646.
    • (2009) J. Virol. , vol.83 , pp. 3637-3646
    • Blakqori, G.1    Van Knippenberg, I.2    Elliott, R.M.3
  • 9
    • 0035872818 scopus 로고    scopus 로고
    • A novel poly(A)-binding protein gene (PABPC5) maps to an X-specific subinterval in the Xq21.3/Yp11.2 homology block of the human sex chromosomes
    • Blanco, P., C. A. Sargent, C. A. Boucher, G. Howell, M. Ross, and N. A. Affara. 2001. A novel poly(A)-binding protein gene (PABPC5) maps to an X-specific subinterval in the Xq21.3/Yp11.2 homology block of the human sex chromosomes. Genomics 74:1-11.
    • (2001) Genomics , vol.74 , pp. 1-11
    • Blanco, P.1    Sargent, C.A.2    Boucher, C.A.3    Howell, G.4    Ross, M.5    Affara, N.A.6
  • 10
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: The ins and outs of translation
    • Buchan, J. R., and R. Parker. 2009. Eukaryotic stress granules: the ins and outs of translation. Mol. Cell 36:932-941.
    • (2009) Mol. Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 11
    • 0025762042 scopus 로고
    • The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities
    • Burd, C. G., E. L. Matunis, and G. Dreyfuss. 1991. The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities. Mol. Cell. Biol. 11:3419-3424.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3419-3424
    • Burd, C.G.1    Matunis, E.L.2    Dreyfuss, G.3
  • 13
    • 69449095602 scopus 로고    scopus 로고
    • Host shutoff is a conserved phenotype of gammaherpesvirus infection and is orchestrated exclusively from the cytoplasm
    • Covarrubias, S., J. M. Richner, K. Clyde, Y. J. Lee, and B. A. Glaunsinger. 2009. Host shutoff is a conserved phenotype of gammaherpesvirus infection and is orchestrated exclusively from the cytoplasm. J. Virol. 83:9554-9566.
    • (2009) J. Virol. , vol.83 , pp. 9554-9566
    • Covarrubias, S.1    Richner, J.M.2    Clyde, K.3    Lee, Y.J.4    Glaunsinger, B.A.5
  • 14
    • 0032473972 scopus 로고    scopus 로고
    • Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation
    • Craig, A. W., A. Haghighat, A. T. Yu, and N. Sonenberg. 1998. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature 392:520-523.
    • (1998) Nature , vol.392 , pp. 520-523
    • Craig, A.W.1    Haghighat, A.2    Yu, A.T.3    Sonenberg, N.4
  • 15
    • 72849121959 scopus 로고    scopus 로고
    • Herpes simplex virus proteins ICP27 and UL47 associate with polyadenylate-binding protein and control its subcellular distribution
    • Dobrikova, E., M. Shveygert, R. Walters, and M. Gromeier. 2010. Herpes simplex virus proteins ICP27 and UL47 associate with polyadenylate-binding protein and control its subcellular distribution. J. Virol. 84:270-279.
    • (2010) J. Virol. , vol.84 , pp. 270-279
    • Dobrikova, E.1    Shveygert, M.2    Walters, R.3    Gromeier, M.4
  • 16
    • 43249093760 scopus 로고    scopus 로고
    • Posttranscriptional gene regulation by spatial rearrangement of the 3′ untranslated region
    • Eberle, A. B., L. Stalder, H. Mathys, R. Z. Orozco, and O. Muhlemann. 2008. Posttranscriptional gene regulation by spatial rearrangement of the 3′ untranslated region. PLoS Biol. 6:e92.
    • (2008) PLoS Biol. , vol.6
    • Eberle, A.B.1    Stalder, L.2    Mathys, H.3    Orozco, R.Z.4    Muhlemann, O.5
  • 17
    • 0036333951 scopus 로고    scopus 로고
    • mRNA degradation by the virion host shutoff (Vhs) protein of herpes simplex virus: Genetic and biochemical evidence that Vhs is a nuclease
    • Everly, D. N., Jr., P. Feng, I. S. Mian, and G. S. Read. 2002. mRNA degradation by the virion host shutoff (Vhs) protein of herpes simplex virus: genetic and biochemical evidence that Vhs is a nuclease. J. Virol. 76:8560-8571.
    • (2002) J. Virol. , vol.76 , pp. 8560-8571
    • Everly Jr., D.N.1    Feng, P.2    Mian, I.S.3    Read, G.S.4
  • 18
    • 36049016095 scopus 로고    scopus 로고
    • Human TOB, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation
    • Ezzeddine, N., T. C. Chang, W. Zhu, A. Yamashita, C. Y. Chen, Z. Zhong, Y. Yamashita, D. Zheng, and A. B. Shyu. 2007. Human TOB, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation. Mol. Cell. Biol. 27:7791-7801.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7791-7801
    • Ezzeddine, N.1    Chang, T.C.2    Zhu, W.3    Yamashita, A.4    Chen, C.Y.5    Zhong, Z.6    Yamashita, Y.7    Zheng, D.8    Shyu, A.B.9
  • 21
    • 19944389569 scopus 로고    scopus 로고
    • The exonuclease and host shutoff functions of the SOX protein of Kaposi's sarcoma-associated herpesvirus are genetically separable
    • DOI 10.1128/JVI.79.12.7396-7401.2005
    • Glaunsinger, B., L. Chavez, and D. Ganem. 2005. The exonuclease and host shutoff functions of the SOX protein of Kaposi's sarcoma-associated herpesvirus are genetically separable. J. Virol. 79:7396-7401. (Pubitemid 40756776)
    • (2005) Journal of Virology , vol.79 , Issue.12 , pp. 7396-7401
    • Glaunsinger, B.1    Chavez, L.2    Ganem, D.3
  • 22
    • 1642271607 scopus 로고    scopus 로고
    • Lytic KSHV infection inhibits host gene expression by accelerating global mRNA turnover
    • DOI 10.1016/S1097-2765(04)00091-7, PII S1097276504000917
    • Glaunsinger, B., and D. Ganem. 2004. Lytic KSHV infection inhibits host gene expression by accelerating global mRNA turnover. Mol. Cell 13:713-723. (Pubitemid 38368128)
    • (2004) Molecular Cell , vol.13 , Issue.5 , pp. 713-723
    • Glaunsinger, B.1    Ganem, D.2
  • 23
    • 85011940617 scopus 로고    scopus 로고
    • How tails define the ending: Divergent roles for polyadenylation in RNA stability and gene expression
    • Glaunsinger, B. A., and Y. J. Lee. 2010. How tails define the ending: divergent roles for polyadenylation in RNA stability and gene expression. RNA Biol. 7:13-17.
    • (2010) RNA Biol. , vol.7 , pp. 13-17
    • Glaunsinger, B.A.1    Lee, Y.J.2
  • 24
    • 0036298692 scopus 로고    scopus 로고
    • Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization
    • Groft, C. M., and S. K. Burley. 2002. Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization. Mol. Cell 9:1273-1283.
    • (2002) Mol. Cell , vol.9 , pp. 1273-1283
    • Groft, C.M.1    Burley, S.K.2
  • 25
    • 55549116341 scopus 로고    scopus 로고
    • Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN
    • Harb, M., M. M. Becker, D. Vitour, C. H. Baron, P. Vende, S. C. Brown, S. Bolte, S. T. Arold, and D. Poncet. 2008. Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN. J. Virol. 82:11283-11293.
    • (2008) J. Virol. , vol.82 , pp. 11283-11293
    • Harb, M.1    Becker, M.M.2    Vitour, D.3    Baron, C.H.4    Vende, P.5    Brown, S.C.6    Bolte, S.7    Arold, S.T.8    Poncet, D.9
  • 27
    • 0035807308 scopus 로고    scopus 로고
    • Quality control of mRNA 3′-end processing is linked to the nuclear exosome
    • Hilleren, P., T. McCarthy, M. Rosbash, R. Parker, and T. H. Jensen. 2001. Quality control of mRNA 3′-end processing is linked to the nuclear exosome. Nature 413:538-542.
    • (2001) Nature , vol.413 , pp. 538-542
    • Hilleren, P.1    McCarthy, T.2    Rosbash, M.3    Parker, R.4    Jensen, T.H.5
  • 28
    • 0035047844 scopus 로고    scopus 로고
    • Defects in the mRNA export factors Rat7p, Gle1p, Mex67p, and Rat8p cause hyperadenylation during 3′-end formation of nascent transcripts
    • DOI 10.1017/S1355838201010147
    • Hilleren, P., and R. Parker. 2001. Defects in the mRNA export factors Rat7p, Gle1p, Mex67p, and Rat8p cause hyperadenylation during 3′-end formation of nascent transcripts. RNA 7:753-764. (Pubitemid 32405872)
    • (2001) RNA , vol.7 , Issue.5 , pp. 753-764
    • Hilleren, P.1    Parker, R.2
  • 29
    • 0033546405 scopus 로고    scopus 로고
    • The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein
    • Hoshino, S., M. Imai, T. Kobayashi, N. Uchida, and T. Katada. 1999. The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein. J. Biol. Chem. 274:16677-16680.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16677-16680
    • Hoshino, S.1    Imai, M.2    Kobayashi, T.3    Uchida, N.4    Katada, T.5
  • 30
    • 33645824089 scopus 로고    scopus 로고
    • Evidence that poly(A) binding protein C1 binds nuclear pre-mRNA poly(A) tails
    • Hosoda, N., F. Lejeune, and L. E. Maquat. 2006. Evidence that poly(A) binding protein C1 binds nuclear pre-mRNA poly(A) tails. Mol. Cell. Biol. 26:3085-3097.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3085-3097
    • Hosoda, N.1    Lejeune, F.2    Maquat, L.E.3
  • 31
    • 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., A. Gradi, and N. Sonenberg. 1998. 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) EMBO J. , vol.17 , pp. 7480-7489
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 32
    • 34547623918 scopus 로고    scopus 로고
    • Quality control of eukaryotic mRNA: Safeguarding cells from abnormal mRNA function
    • Isken, O., and L. E. Maquat. 2007. Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function. Genes Dev. 21:1833-1856.
    • (2007) Genes Dev. , vol.21 , pp. 1833-1856
    • Isken, O.1    Maquat, L.E.2
  • 33
    • 40949148553 scopus 로고    scopus 로고
    • Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways
    • Ivanov, P. V., N. H. Gehring, J. B. Kunz, M. W. Hentze, and A. E. Kulozik. 2008. Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways. EMBO J. 27:736-747.
    • (2008) EMBO J. , vol.27 , pp. 736-747
    • Ivanov, P.V.1    Gehring, N.H.2    Kunz, J.B.3    Hentze, M.W.4    Kulozik, A.E.5
  • 34
    • 0035022577 scopus 로고    scopus 로고
    • A block to mRNA nuclear export in S. cerevisiae leads to hyperadenylation of transcripts that accumulate at the site of transcription
    • Jensen, T. H., K. Patricio, T. McCarthy, and M. Rosbash. 2001. A block to mRNA nuclear export in S. cerevisiae leads to hyperadenylation of transcripts that accumulate at the site of transcription. Mol. Cell 7:887-898.
    • (2001) Mol. Cell , vol.7 , pp. 887-898
    • Jensen, T.H.1    Patricio, K.2    McCarthy, T.3    Rosbash, M.4
  • 35
    • 0029019122 scopus 로고
    • Mutational analysis of the herpes simplex virus virion host shutoff protein: Evidence that vhs functions in the absence of other viral proteins
    • Jones, F. E., C. A. Smibert, and J. R. Smiley. 1995. Mutational analysis of the herpes simplex virus virion host shutoff protein: evidence that vhs functions in the absence of other viral proteins. J. Virol. 69:4863-4871.
    • (1995) J. Virol. , vol.69 , pp. 4863-4871
    • Jones, F.E.1    Smibert, C.A.2    Smiley, J.R.3
  • 36
    • 70350768988 scopus 로고    scopus 로고
    • A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein
    • Kamitani, W., C. Huang, K. Narayanan, K. G. Lokugamage, and S. Makino. 2009. A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein. Nat. Struct. Mol. Biol. 16:1134-1140.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1134-1140
    • Kamitani, W.1    Huang, C.2    Narayanan, K.3    Lokugamage, K.G.4    Makino, S.5
  • 37
    • 33748046163 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus nsp1 protein suppresses host gene expression by promoting host mRNA degradation
    • Kamitani, W., K. Narayanan, C. Huang, K. Lokugamage, T. Ikegami, N. Ito, H. Kubo, and S. Makino. 2006. Severe acute respiratory syndrome coronavirus nsp1 protein suppresses host gene expression by promoting host mRNA degradation. Proc. Natl. Acad. Sci. U. S. A. 103:12885-12890.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 12885-12890
    • Kamitani, W.1    Narayanan, K.2    Huang, C.3    Lokugamage, K.4    Ikegami, T.5    Ito, N.6    Kubo, H.7    Makino, S.8
  • 38
    • 0041312652 scopus 로고    scopus 로고
    • Stimulation of poly(A) polymerase through a direct interaction with the nuclear poly(A) binding protein allosterically regulated by RNA
    • DOI 10.1093/emboj/cdg347
    • Kerwitz, Y., U. Kuhn, H. Lilie, A. Knoth, T. Scheuermann, H. Friedrich, E. Schwarz, and E. Wahle. 2003. Stimulation of poly(A) polymerase through a direct interaction with the nuclear poly(A) binding protein allosterically regulated by RNA. EMBO J. 22:3705-3714. (Pubitemid 36898347)
    • (2003) EMBO Journal , vol.22 , Issue.14 , pp. 3705-3714
    • Kerwitz, Y.1    Kuhn, U.2    Lilie, H.3    Knoth, A.4    Scheuermann, T.5    Friedrich, H.6    Schwarz, E.7    Wahle, E.8
  • 40
    • 69249151288 scopus 로고    scopus 로고
    • Poly(A) tail length is controlled by the nuclear poly(A)-binding protein regulating the interaction between poly(A) polymerase and the cleavage and polyadenylation specificity factor
    • Kuhn, U., M. Gundel, A. Knoth, Y. Kerwitz, S. Rudel, and E. Wahle. 2009. Poly(A) tail length is controlled by the nuclear poly(A)-binding protein regulating the interaction between poly(A) polymerase and the cleavage and polyadenylation specificity factor. J. Biol. Chem. 284:22803-22814.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22803-22814
    • Kuhn, U.1    Gundel, M.2    Knoth, A.3    Kerwitz, Y.4    Rudel, S.5    Wahle, E.6
  • 41
    • 0038063499 scopus 로고    scopus 로고
    • Xenopus poly(A) binding protein: Functional domains in RNA binding and protein-protein interaction
    • Kuhn, U., and T. Pieler. 1996. Xenopus poly(A) binding protein: functional domains in RNA binding and protein-protein interaction. J. Mol. Biol. 256:20-30.
    • (1996) J. Mol. Biol. , vol.256 , pp. 20-30
    • Kuhn, U.1    Pieler, T.2
  • 42
    • 2442482777 scopus 로고    scopus 로고
    • Structure and function of poly(A) binding proteins
    • Kuhn, U., and E. Wahle. 2004. Structure and function of poly(A) binding proteins. Biochim. Biophys. Acta 1678:67-84.
    • (2004) Biochim. Biophys. Acta , vol.1678 , pp. 67-84
    • Kuhn, U.1    Wahle, E.2
  • 43
    • 20444368818 scopus 로고    scopus 로고
    • RNA degradation by the exosome is promoted by a nuclear polyadenylation complex
    • DOI 10.1016/j.cell.2005.04.029, PII S0092867405004423
    • LaCava, J., J. Houseley, C. Saveanu, E. Petfalski, E. Thompson, A. Jacquier, and D. Tollervey. 2005. RNA degradation by the exosome is promoted by a nuclear polyadenylation complex. Cell 121:713-724. (Pubitemid 40797594)
    • (2005) Cell , vol.121 , Issue.5 , pp. 713-724
    • LaCava, J.1    Houseley, J.2    Saveanu, C.3    Petfalski, E.4    Thompson, E.5    Jacquier, A.6    Tollervey, D.7
  • 44
    • 69449096380 scopus 로고    scopus 로고
    • Polyadenylation-assisted RNA degradation processes in plants
    • Lange, H., F. M. Sement, J. Canaday, and D. Gagliardi. 2009. Polyadenylation-assisted RNA degradation processes in plants. Trends Plant Sci. 14:497-504.
    • (2009) Trends Plant Sci. , vol.14 , pp. 497-504
    • Lange, H.1    Sement, F.M.2    Canaday, J.3    Gagliardi, D.4
  • 45
    • 66249138088 scopus 로고    scopus 로고
    • Aberrant herpesvirus-induced polyadenylation correlates with cellular messenger RNA destruction
    • Lee, Y. J., and B. A. Glaunsinger. 2009. Aberrant herpesvirus-induced polyadenylation correlates with cellular messenger RNA destruction. PLoS Biol. 7:e1000107.
    • (2009) PLoS Biol. , vol.7
    • Lee, Y.J.1    Glaunsinger, B.A.2
  • 46
    • 0036889142 scopus 로고    scopus 로고
    • Interactions between mRNA export commitment, 3′-end quality control, and nuclear degradation
    • Libri, D., K. Dower, J. Boulay, R. Thomsen, M. Rosbash, and T. H. Jensen. 2002. Interactions between mRNA export commitment, 3′-end quality control, and nuclear degradation. Mol. Cell. Biol. 22:8254-8266.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8254-8266
    • Libri, D.1    Dower, K.2    Boulay, J.3    Thomsen, R.4    Rosbash, M.5    Jensen, T.H.6
  • 47
    • 0025912305 scopus 로고
    • Purification and characterization of poly(A) polymerase from Saccharomyces cerevisiae
    • Lingner, J., I. Radtke, E. Wahle, and W. Keller. 1991. Purification and characterization of poly(A) polymerase from Saccharomyces cerevisiae. J. Biol. Chem. 266:8741-8746.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8741-8746
    • Lingner, J.1    Radtke, I.2    Wahle, E.3    Keller, W.4
  • 48
    • 58149147440 scopus 로고    scopus 로고
    • Expression of poly(A)-binding protein is upregulated during recovery from heat shock in HeLa cells
    • Ma, S., R. B. Bhattacharjee, and J. Bag. 2009. Expression of poly(A)-binding protein is upregulated during recovery from heat shock in HeLa cells. FEBS J. 276:552-570.
    • (2009) FEBS J. , vol.276 , pp. 552-570
    • Ma, S.1    Bhattacharjee, R.B.2    Bag, J.3
  • 49
    • 0038487811 scopus 로고    scopus 로고
    • Poly(A)-binding proteins: Multifunctional scaffolds for the post-transcriptional control of gene expression
    • Mangus, D. A., M. C. Evans, and A. Jacobson. 2003. Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol. 4:223.
    • (2003) Genome Biol. , vol.4 , pp. 223
    • Mangus, D.A.1    Evans, M.C.2    Jacobson, A.3
  • 50
    • 0029797247 scopus 로고    scopus 로고
    • The hnRNP C proteins contain a nuclear retention sequence that can override nuclear export signals
    • Nakielny, S., and G. Dreyfuss. 1996. The hnRNP C proteins contain a nuclear retention sequence that can override nuclear export signals. J. Cell Biol. 134:1365-1373.
    • (1996) J. Cell Biol. , vol.134 , pp. 1365-1373
    • Nakielny, S.1    Dreyfuss, G.2
  • 51
    • 0025038919 scopus 로고
    • The Xenopus laevis poly(A) binding protein is composed of multiple functionally independent RNA binding domains
    • Nietfeld, W., H. Mentzel, and T. Pieler. 1990. The Xenopus laevis poly(A) binding protein is composed of multiple functionally independent RNA binding domains. EMBO J. 9:3699-3705. (Pubitemid 20337402)
    • (1990) EMBO Journal , vol.9 , Issue.11 , pp. 3699-3705
    • Nietfeld, W.1    Mentzel, H.2    Pieler, T.3
  • 52
    • 70349306459 scopus 로고    scopus 로고
    • Assembly of an export-competent mRNP is needed for efficient release of the 3′-end processing complex after polyadenylation
    • Qu, X., S. Lykke-Andersen, T. Nasser, C. Saguez, E. Bertrand, T. H. Jensen, and C. Moore. 2009. Assembly of an export-competent mRNP is needed for efficient release of the 3′-end processing complex after polyadenylation. Mol. Cell. Biol. 29:5327-5338.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5327-5338
    • Qu, X.1    Lykke-Andersen, S.2    Nasser, T.3    Saguez, C.4    Bertrand, E.5    Jensen, T.H.6    Moore, C.7
  • 53
    • 66049162655 scopus 로고    scopus 로고
    • Execution of nonsense-mediated mRNA decay: What defines a substrate?
    • Rebbapragada, I., and J. Lykke-Andersen. 2009. Execution of nonsense-mediated mRNA decay: what defines a substrate? Curr. Opin. Cell Biol. 21:394-402.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 394-402
    • Rebbapragada, I.1    Lykke-Andersen, J.2
  • 55
    • 77952702091 scopus 로고    scopus 로고
    • Evidence for translational regulation by the herpes simplex virus virion host shutoff protein
    • Saffran, H. A., G. S. Read, and J. R. Smiley. 2010. Evidence for translational regulation by the herpes simplex virus virion host shutoff protein. J. Virol. 84:6041-6049.
    • (2010) J. Virol. , vol.84 , pp. 6041-6049
    • Saffran, H.A.1    Read, G.S.2    Smiley, J.R.3
  • 57
    • 77950439778 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus ORF57 protein binds and protects a nuclear noncoding RNA from cellular RNA decay pathways
    • Sahin, B. B., D. Patel, and N. K. Conrad. 2010. Kaposi's sarcoma-associated herpesvirus ORF57 protein binds and protects a nuclear noncoding RNA from cellular RNA decay pathways. PLoS Pathog. 6:e1000799.
    • (2010) PLoS Pathog. , vol.6
    • Sahin, B.B.1    Patel, D.2    Conrad, N.K.3
  • 58
    • 0022178431 scopus 로고
    • Degradation of cellular mRNAs induced by a virion-associated factor during herpes simplex virus infection of Vero cells
    • Schek, N., and S. L. Bachenheimer. 1985. Degradation of cellular mRNAs induced by a virion-associated factor during herpes simplex virus infection of Vero cells. J. Virol. 55:601-610.
    • (1985) J. Virol. , vol.55 , pp. 601-610
    • Schek, N.1    Bachenheimer, S.L.2
  • 60
    • 34548359334 scopus 로고    scopus 로고
    • Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein
    • Siddiqui, N., D. A. Mangus, T. C. Chang, J. M. Palermino, A. B. Shyu, and K. Gehring. 2007. Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein. J. Biol. Chem. 282:25067-25075.
    • (2007) J. Biol. Chem. , vol.282 , pp. 25067-25075
    • Siddiqui, N.1    Mangus, D.A.2    Chang, T.C.3    Palermino, J.M.4    Shyu, A.B.5    Gehring, K.6
  • 61
    • 34548294617 scopus 로고    scopus 로고
    • Communication with the exon-junction complex and activation of nonsense-mediated decay by human Upf proteins occur in the cytoplasm
    • Singh, G., S. Jakob, M. G. Kleedehn, and J. Lykke-Andersen. 2007. Communication with the exon-junction complex and activation of nonsense-mediated decay by human Upf proteins occur in the cytoplasm. Mol. Cell 27:780-792.
    • (2007) Mol. Cell , vol.27 , pp. 780-792
    • Singh, G.1    Jakob, S.2    Kleedehn, M.G.3    Lykke-Andersen, J.4
  • 62
    • 43249084802 scopus 로고    scopus 로고
    • A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay
    • Singh, G., I. Rebbapragada, and J. Lykke-Andersen. 2008. A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay. PLoS Biol. 6:e111.
    • (2008) PLoS Biol. , vol.6
    • Singh, G.1    Rebbapragada, I.2    Lykke-Andersen, J.3
  • 63
    • 1642480256 scopus 로고    scopus 로고
    • Human PABP binds AU-rich RNA via RNA-binding domains 3 and 4
    • Sladic, R. T., C. A. Lagnado, C. J. Bagley, and G. J. Goodall. 2004. Human PABP binds AU-rich RNA via RNA-binding domains 3 and 4. Eur. J. Biochem. 271:450-457.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 450-457
    • Sladic, R.T.1    Lagnado, C.A.2    Bagley, C.J.3    Goodall, G.J.4
  • 64
    • 0346373732 scopus 로고    scopus 로고
    • Herpes Simplex Virus Virion Host Shutoff Protein: Immune Evasion Mediated by a Viral RNase?
    • DOI 10.1128/JVI.78.3.1063-1068.2004
    • Smiley, J. R. 2004. Herpes simplex virus virion host shutoff protein: immune evasion mediated by a viral RNase? J. Virol. 78:1063-1068. (Pubitemid 38095816)
    • (2004) Journal of Virology , vol.78 , Issue.3 , pp. 1063-1068
    • Smiley, J.R.1
  • 65
    • 76549132190 scopus 로고    scopus 로고
    • Poly(A)-binding protein (PABP): A common viral target
    • Smith, R. W., and N. K. Gray. 2010. Poly(A)-binding protein (PABP): a common viral target. Biochem. J. 426:1-12.
    • (2010) Biochem. J. , vol.426 , pp. 1-12
    • Smith, R.W.1    Gray, N.K.2
  • 66
    • 0034122512 scopus 로고    scopus 로고
    • Host protein interactions with the 3′ end of bovine coronavirus RNA and the requirement of the poly(A) tail for coronavirus defective genome replication
    • Spagnolo, J. F., and B. G. Hogue. 2000. Host protein interactions with the 3′ end of bovine coronavirus RNA and the requirement of the poly(A) tail for coronavirus defective genome replication. J. Virol. 74:5053-5065.
    • (2000) J. Virol. , vol.74 , pp. 5053-5065
    • Spagnolo, J.F.1    Hogue, B.G.2
  • 67
    • 0023182175 scopus 로고
    • Effects of herpes simplex virus on mRNA stability
    • Strom, T., and N. Frenkel. 1987. Effects of herpes simplex virus on mRNA stability. J. Virol. 61:2198-2207. (Pubitemid 17088933)
    • (1987) Journal of Virology , vol.61 , Issue.7 , pp. 2198-2207
    • Strom, T.1    Frenkel, N.2
  • 69
    • 0028895435 scopus 로고
    • Poly(A) tail length control is caused by termination of processive synthesis
    • Wahle, E. 1995. Poly(A) tail length control is caused by termination of processive synthesis. J. Biol. Chem. 270:2800-2808.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2800-2808
    • Wahle, E.1
  • 70
    • 0027400410 scopus 로고
    • Mammalian poly(A)-binding protein II. Physical properties and binding to polynucleotides
    • Wahle, E., A. Lustig, P. Jeno, and P. Maurer. 1993. Mammalian poly(A)-binding protein II. Physical properties and binding to polynucleotides. J. Biol. Chem. 268:2937-2945.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2937-2945
    • Wahle, E.1    Lustig, A.2    Jeno, P.3    Maurer, P.4
  • 71
    • 0033066673 scopus 로고    scopus 로고
    • An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro
    • Wang, Z., N. Day, P. Trifillis, and M. Kiledjian. 1999. An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro. Mol. Cell. Biol. 19:4552-4560.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4552-4560
    • Wang, Z.1    Day, N.2    Trifillis, P.3    Kiledjian, M.4
  • 72
    • 0032112017 scopus 로고    scopus 로고
    • Circularization of mRNA by eukaryotic translation initiation factors
    • Wells, S. E., P. E. Hillner, R. D. Vale, and A. B. Sachs. 1998. Circularization of mRNA by eukaryotic translation initiation factors. Mol. Cell 2:135-140.
    • (1998) Mol. Cell , vol.2 , pp. 135-140
    • Wells, S.E.1    Hillner, P.E.2    Vale, R.D.3    Sachs, A.B.4
  • 73
    • 0030041959 scopus 로고    scopus 로고
    • Overexpression of poly(A) binding protein prevents maturation-specific deadenylation and translational inactivation in Xenopus oocytes
    • Wormington, M., A. M. Searfoss, and C. A. Hurney. 1996. Overexpression of poly(A) binding protein prevents maturation-specific deadenylation and translational inactivation in Xenopus oocytes. EMBO J. 15:900-909.
    • (1996) EMBO J. , vol.15 , pp. 900-909
    • Wormington, M.1    Searfoss, A.M.2    Hurney, C.A.3
  • 75
    • 0028881020 scopus 로고
    • iPABP, an inducible poly(A)-binding protein detected in activated human T cells
    • Yang, H., C. S. Duckett, and T. Lindsten. 1995. iPABP, an inducible poly(A)-binding protein detected in activated human T cells. Mol. Cell. Biol. 15:6770-6776.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6770-6776
    • Yang, H.1    Duckett, C.S.2    Lindsten, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.