메뉴 건너뛰기




Volumn 3, Issue 6, 2012, Pages 743-757

Mechanism of the initiation of mRNA decay: Role of eRF3 family G proteins

Author keywords

[No Author keywords available]

Indexed keywords

CAF1 CCR4 PROTEIN; CHEMOKINE RECEPTOR CCR4; CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN; ERF3 PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; PAN2 PAN3 PROTEIN; POLYADENYLIC ACID BINDING PROTEIN; RNA BINDING PROTEIN; TRISTETRAPROLIN; UNCLASSIFIED DRUG; XRN1 PROTEIN;

EID: 84867622344     PISSN: 17577004     EISSN: 17577012     Source Type: Journal    
DOI: 10.1002/wrna.1133     Document Type: Review
Times cited : (24)

References (84)
  • 1
    • 0025010979 scopus 로고
    • The GTPase superfamily: a conserved switch for diverse cell functions.
    • Bourne HR, Sanders DA, McCormick F. The GTPase superfamily: a conserved switch for diverse cell functions. Nature 1990, 348:125-132.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 2
    • 0026026818 scopus 로고
    • The GTPase superfamily: conserved structure and molecular mechanism.
    • Bourne HR, Sanders DA, McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature 1991, 349:117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 3
    • 0024790320 scopus 로고
    • A human homologue of the yeast GST1 gene codes for a GTP-binding protein and is expressed in a proliferation-dependent manner in mammalian cells.
    • Hoshino S, Miyazawa H, Enomoto T, Hanaoka F, Kikuchi Y, Kikuchi A, Ui M. A human homologue of the yeast GST1 gene codes for a GTP-binding protein and is expressed in a proliferation-dependent manner in mammalian cells. EMBO J 1989, 8:3807-3814.
    • (1989) EMBO J , vol.8 , pp. 3807-3814
    • Hoshino, S.1    Miyazawa, H.2    Enomoto, T.3    Hanaoka, F.4    Kikuchi, Y.5    Kikuchi, A.6    Ui, M.7
  • 4
    • 0032575550 scopus 로고    scopus 로고
    • Molecular cloning of a novel member of the eukaryotic polypeptide chain-releasing factors (eRF). Its identification as eRF3 interacting with eRF1.
    • Hoshino S, Imai M, Mizutani M, Kikuchi Y, Hanaoka F, Ui M, Katada T. Molecular cloning of a novel member of the eukaryotic polypeptide chain-releasing factors (eRF). Its identification as eRF3 interacting with eRF1. J Biol Chem 1998, 273:22254-22259.
    • (1998) J Biol Chem , vol.273 , pp. 22254-22259
    • Hoshino, S.1    Imai, M.2    Mizutani, M.3    Kikuchi, Y.4    Hanaoka, F.5    Ui, M.6    Katada, T.7
  • 5
    • 0032437714 scopus 로고    scopus 로고
    • The product of the mammalian orthologue of the Saccharomyces cerevisiae HBS1 gene is phylogenetically related to eukaryotic release factor 3 (eRF3) but does not carry eRF3-like activity.
    • Wallrapp C, Verrier SB, Zhouravleva G, Philippe H, Philippe M, Gress TM, Jean-Jean O. The product of the mammalian orthologue of the Saccharomyces cerevisiae HBS1 gene is phylogenetically related to eukaryotic release factor 3 (eRF3) but does not carry eRF3-like activity. FEBS Lett 1998, 440:387-392.
    • (1998) FEBS Lett , vol.440 , pp. 387-392
    • Wallrapp, C.1    Verrier, S.B.2    Zhouravleva, G.3    Philippe, H.4    Philippe, M.5    Gress, T.M.6    Jean-Jean, O.7
  • 6
    • 0021262150 scopus 로고
    • Superkiller mutations in Saccharomyces cerevisiae suppress exclusion of M2 double-stranded RNA by L-A -HN and confer cold sensitivity in the presence of M and L-A-HN.
    • Ridley SP, Sommer SS, Wickner RB. Superkiller mutations in Saccharomyces cerevisiae suppress exclusion of M2 double-stranded RNA by L-A -HN and confer cold sensitivity in the presence of M and L-A-HN. Mol Cell Biol 1984, 4:761-770.
    • (1984) Mol Cell Biol , vol.4 , pp. 761-770
    • Ridley, S.P.1    Sommer, S.S.2    Wickner, R.B.3
  • 7
    • 0034616691 scopus 로고    scopus 로고
    • Mouse and human GTPBP2, newly identified members of the GP-1 family of GTPase.
    • Kudo H, Senju S, Mitsuya H, Nishimura Y. Mouse and human GTPBP2, newly identified members of the GP-1 family of GTPase. Biochem Biophys Res Commun 2000, 272:456-465.
    • (2000) Biochem Biophys Res Commun , vol.272 , pp. 456-465
    • Kudo, H.1    Senju, S.2    Mitsuya, H.3    Nishimura, Y.4
  • 11
    • 33746728252 scopus 로고    scopus 로고
    • Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF3.
    • Hauryliuk V, Zavialov A, Kisselev L, Ehrenberg M. Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF3. Biochimie 2006, 88:747-757.
    • (2006) Biochimie , vol.88 , pp. 747-757
    • Hauryliuk, V.1    Zavialov, A.2    Kisselev, L.3    Ehrenberg, M.4
  • 16
    • 77957935294 scopus 로고    scopus 로고
    • Dom34:Hbs1 promotes subunit dissociation and peptidyl-trna drop-off to initiate no-go decay.
    • Shoemaker CJ, Eyler DE, Green R. Dom34:Hbs1 promotes subunit dissociation and peptidyl-trna drop-off to initiate no-go decay. Science 2010, 330:369-372.
    • (2010) Science , vol.330 , pp. 369-372
    • Shoemaker, C.J.1    Eyler, D.E.2    Green, R.3
  • 17
    • 79955626576 scopus 로고    scopus 로고
    • Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80s ribosomes and stalled elongation complexes.
    • Pisareva VP, Skabkin MA, Hellen CU, Pestova TV, Pisarev AV. Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80s ribosomes and stalled elongation complexes. EMBO J 2011, 30:1804-1817.
    • (2011) EMBO J , vol.30 , pp. 1804-1817
    • Pisareva, V.P.1    Skabkin, M.A.2    Hellen, C.U.3    Pestova, T.V.4    Pisarev, A.V.5
  • 18
    • 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, Imai M, Kobayashi T, Uchida N, Katada T. 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 1999, 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
  • 19
    • 0037184899 scopus 로고    scopus 로고
    • A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in cap/poly(A)-dependent translation.
    • Uchida N, Hoshino S, Imataka H, Sonenberg N, Katada T. A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in cap/poly(A)-dependent translation. J Biol Chem 2002, 277:50286-50292.
    • (2002) J Biol Chem , vol.277 , pp. 50286-50292
    • Uchida, N.1    Hoshino, S.2    Imataka, H.3    Sonenberg, N.4    Katada, T.5
  • 20
    • 0141866883 scopus 로고    scopus 로고
    • Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation.
    • Hosoda N, Kobayashi T, Uchida N, Funakoshi Y, Kikuchi Y, Hoshino S, Katada T. Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation. J Biol Chem 2003, 278:38287-38291.
    • (2003) J Biol Chem , vol.278 , pp. 38287-38291
    • Hosoda, N.1    Kobayashi, T.2    Uchida, N.3    Funakoshi, Y.4    Kikuchi, Y.5    Hoshino, S.6    Katada, T.7
  • 21
    • 36849079370 scopus 로고    scopus 로고
    • Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases.
    • Funakoshi Y, Doi Y, Hosoda N, Uchida N, Osawa M, Shimada I, Tsujimoto M, Suzuki T, Katada T, Hoshino S. Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases. Genes Dev 2007, 21:3135-3148.
    • (2007) Genes Dev , vol.21 , pp. 3135-3148
    • Funakoshi, Y.1    Doi, Y.2    Hosoda, N.3    Uchida, N.4    Osawa, M.5    Shimada, I.6    Tsujimoto, M.7    Suzuki, T.8    Katada, T.9    Hoshino, S.10
  • 23
    • 77956319461 scopus 로고    scopus 로고
    • Molecular basis of eRF3 recognition by the MLLE domain of poly(A)-binding protein.
    • Kozlov G, Gehring K. Molecular basis of eRF3 recognition by the MLLE domain of poly(A)-binding protein. PLoS One 2010, 5:e10169.
    • (2010) PLoS One , vol.5
    • Kozlov, G.1    Gehring, K.2
  • 24
    • 0035801392 scopus 로고    scopus 로고
    • Ski7p G protein interacts with the exosome and the Ski complex for 3′-to-5′ mRNA decay in yeast.
    • Araki Y, Takahashi S, Kobayashi T, Kajiho H, Hoshino S, Katada T. Ski7p G protein interacts with the exosome and the Ski complex for 3′-to-5′ mRNA decay in yeast. EMBO J 2001, 20:4684-4693.
    • (2001) EMBO J , vol.20 , pp. 4684-4693
    • Araki, Y.1    Takahashi, S.2    Kobayashi, T.3    Kajiho, H.4    Hoshino, S.5    Katada, T.6
  • 25
    • 0033777266 scopus 로고    scopus 로고
    • Function of the ski4p (Csl4p) and Ski7p proteins in 3′-to-5′ degradation of mRNA.
    • van Hoof A, Staples RR, Baker RE, Parker R. Function of the ski4p (Csl4p) and Ski7p proteins in 3′-to-5′ degradation of mRNA. Mol Cell Biol 2000, 20:8230-8243.
    • (2000) Mol Cell Biol , vol.20 , pp. 8230-8243
    • van Hoof, A.1    Staples, R.R.2    Baker, R.E.3    Parker, R.4
  • 26
    • 0027320701 scopus 로고
    • A turnover pathway for both stable and unstable mRNAs in yeast: evidence for a requirement for deadenylation.
    • Decker CJ, Parker R. A turnover pathway for both stable and unstable mRNAs in yeast: evidence for a requirement for deadenylation. Genes Dev 1993, 7:1632-1643.
    • (1993) Genes Dev , vol.7 , pp. 1632-1643
    • Decker, C.J.1    Parker, R.2
  • 27
    • 84856218082 scopus 로고    scopus 로고
    • Nuclear quality control of RNA polymerase II transcripts.
    • Schmid M, Jensen TH. Nuclear quality control of RNA polymerase II transcripts. Wiley Interdiscip Rev RNA 2010, 1:474-485.
    • (2010) Wiley Interdiscip Rev RNA , vol.1 , pp. 474-485
    • Schmid, M.1    Jensen, T.H.2
  • 28
    • 0032824911 scopus 로고    scopus 로고
    • Linking mRNA turnover and translation: assessing the polyribosomal association of mRNA decay factors and degradative intermediates.
    • Mangus DA, Jacobson A. Linking mRNA turnover and translation: assessing the polyribosomal association of mRNA decay factors and degradative intermediates. Methods 1999, 17:28-37.
    • (1999) Methods , vol.17 , pp. 28-37
    • Mangus, D.A.1    Jacobson, A.2
  • 29
    • 0025267840 scopus 로고
    • Identification and comparison of stable and unstable mRNAs in Saccharomyces cerevisiae.
    • Herrick D, Parker R, Jacobson A. Identification and comparison of stable and unstable mRNAs in Saccharomyces cerevisiae. Mol Cell Biol 1990, 10:2269-2284.
    • (1990) Mol Cell Biol , vol.10 , pp. 2269-2284
    • Herrick, D.1    Parker, R.2    Jacobson, A.3
  • 30
    • 0028225993 scopus 로고
    • Differential effects of translational inhibition in cis and in trans on the decay of the unstable yeast MFA2 mRNA.
    • Beelman CA, Parker R. Differential effects of translational inhibition in cis and in trans on the decay of the unstable yeast MFA2 mRNA. J Biol Chem 1994, 269:9687-9692.
    • (1994) J Biol Chem , vol.269 , pp. 9687-9692
    • Beelman, C.A.1    Parker, R.2
  • 31
    • 70249141564 scopus 로고    scopus 로고
    • Co-translational mRNA decay in Saccharomyces cerevisiae.
    • Hu W, Sweet TJ, Chamnongpol S, Baker KE, Coller J. Co-translational mRNA decay in Saccharomyces cerevisiae. Nature 2009, 461:225-229.
    • (2009) Nature , vol.461 , pp. 225-229
    • Hu, W.1    Sweet, T.J.2    Chamnongpol, S.3    Baker, K.E.4    Coller, J.5
  • 33
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies.
    • Sheth U, Parker R. Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 2003, 300:805-808.
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 34
    • 0035830508 scopus 로고    scopus 로고
    • The transcription factor associated ccr4 and caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae.
    • Tucker M, Valencia-Sanchez MA, Staples RR, Chen J, Denis CL, Parker R. The transcription factor associated ccr4 and caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae. Cell 2001, 104:377-386.
    • (2001) Cell , vol.104 , pp. 377-386
    • Tucker, M.1    Valencia-Sanchez, M.A.2    Staples, R.R.3    Chen, J.4    Denis, C.L.5    Parker, R.6
  • 36
    • 79956117132 scopus 로고    scopus 로고
    • Lsm1-7-pat1 complex: a link between 3′ and 5′-ends in mRNA decay?
    • Tharun S. Lsm1-7-pat1 complex: a link between 3′ and 5′-ends in mRNA decay? RNA Biol 2009, 6:228-232.
    • (2009) RNA Biol , vol.6 , pp. 228-232
    • Tharun, S.1
  • 37
    • 8544231439 scopus 로고    scopus 로고
    • The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay.
    • Kobayashi T, Funakoshi Y, Hoshino S, Katada T. The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay. J Biol Chem 2004, 279:45693-45700.
    • (2004) J Biol Chem , vol.279 , pp. 45693-45700
    • Kobayashi, T.1    Funakoshi, Y.2    Hoshino, S.3    Katada, T.4
  • 38
    • 0033251605 scopus 로고    scopus 로고
    • Novel function of the eukaryotic polypeptide-chain releasing factor 3 (eRF3/GSPT) in the mRNA degradation pathway.
    • Hoshino S, Hosoda N, Araki Y, Kobayashi T, Uchida N, Funakoshi Y, Katada T. Novel function of the eukaryotic polypeptide-chain releasing factor 3 (eRF3/GSPT) in the mRNA degradation pathway. Biochemistry (Mosc) 1999, 64:1367-1372.
    • (1999) Biochemistry (Mosc) , vol.64 , pp. 1367-1372
    • Hoshino, S.1    Hosoda, N.2    Araki, Y.3    Kobayashi, T.4    Uchida, N.5    Funakoshi, Y.6    Katada, T.7
  • 39
    • 0347093310 scopus 로고    scopus 로고
    • Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein.
    • Uchida N, Hoshino S, Katada T. Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein. J Biol Chem 2004, 279:1383-1391.
    • (2004) J Biol Chem , vol.279 , pp. 1383-1391
    • Uchida, N.1    Hoshino, S.2    Katada, T.3
  • 40
    • 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, Mangus DA, Chang TC, Palermino JM, Shyu AB, Gehring K. Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein. J Biol Chem 2007, 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
  • 41
    • 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, Chang TC, Zhu W, Yamashita A, Chen CY, Zhong Z, Yamashita Y, Zheng D, Shyu AB. Human tob, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation. Mol Cell Biol 2007, 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
  • 42
    • 14244256765 scopus 로고    scopus 로고
    • Interaction of anti-proliferative protein tob with poly(A)-binding protein and inducible poly(A)-binding protein: implication of tob in translational control.
    • Okochi K, Suzuki T, Inoue J, Matsuda S, Yamamoto T. Interaction of anti-proliferative protein tob with poly(A)-binding protein and inducible poly(A)-binding protein: implication of tob in translational control. Genes Cells 2005, 10:151-163.
    • (2005) Genes Cells , vol.10 , pp. 151-163
    • Okochi, K.1    Suzuki, T.2    Inoue, J.3    Matsuda, S.4    Yamamoto, T.5
  • 43
    • 77956259603 scopus 로고    scopus 로고
    • Quantitative characterization of tob interactions provides the thermodynamic basis for translation termination-coupled deadenylase regulation.
    • Ruan L, Osawa M, Hosoda N, Imai S, Machiyama A, Katada T, Hoshino S, Shimada I. Quantitative characterization of tob interactions provides the thermodynamic basis for translation termination-coupled deadenylase regulation. J Biol Chem 2010, 285:27624-27631.
    • (2010) J Biol Chem , vol.285 , pp. 27624-27631
    • Ruan, L.1    Osawa, M.2    Hosoda, N.3    Imai, S.4    Machiyama, A.5    Katada, T.6    Hoshino, S.7    Shimada, I.8
  • 44
    • 33745806590 scopus 로고    scopus 로고
    • Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae.
    • Keeling KM, Salas-Marco J, Osherovich LZ, Bedwell DM. Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae. Mol Cell Biol 2006, 26:5237-5248.
    • (2006) Mol Cell Biol , vol.26 , pp. 5237-5248
    • Keeling, K.M.1    Salas-Marco, J.2    Osherovich, L.Z.3    Bedwell, D.M.4
  • 46
    • 13944274507 scopus 로고    scopus 로고
    • Smaug recruits the CCR4/POP2/NOT deadenylase complex to trigger maternal transcript localization in the early Drosophila embryo.
    • Semotok JL, Cooperstock RL, Pinder BD, Vari HK, Lipshitz HD, Smibert CA. Smaug recruits the CCR4/POP2/NOT deadenylase complex to trigger maternal transcript localization in the early Drosophila embryo. Curr Biol 2005, 15:284-294.
    • (2005) Curr Biol , vol.15 , pp. 284-294
    • Semotok, J.L.1    Cooperstock, R.L.2    Pinder, B.D.3    Vari, H.K.4    Lipshitz, H.D.5    Smibert, C.A.6
  • 47
    • 33846954393 scopus 로고    scopus 로고
    • PUF protein-mediated deadenylation is catalyzed by Ccr4p.
    • Goldstrohm AC, Seay DJ, Hook BA, Wickens M. PUF protein-mediated deadenylation is catalyzed by Ccr4p. J Biol Chem 2007, 282:109-114.
    • (2007) J Biol Chem , vol.282 , pp. 109-114
    • Goldstrohm, A.C.1    Seay, D.J.2    Hook, B.A.3    Wickens, M.4
  • 48
    • 33646875518 scopus 로고    scopus 로고
    • CUG-BP binds to RNA substrates and recruits PARN deadenylase.
    • Moraes KC, Wilusz CJ, Wilusz J. CUG-BP binds to RNA substrates and recruits PARN deadenylase. RNA 2006, 12:1084-1091.
    • (2006) RNA , vol.12 , pp. 1084-1091
    • Moraes, K.C.1    Wilusz, C.J.2    Wilusz, J.3
  • 49
    • 2942612333 scopus 로고    scopus 로고
    • A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery.
    • Gherzi R, Lee KY, Briata P, Wegmuller D, Moroni C, Karin M, Chen CY. A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery. Mol Cell 2004, 14:571-583.
    • (2004) Mol Cell , vol.14 , pp. 571-583
    • Gherzi, R.1    Lee, K.Y.2    Briata, P.3    Wegmuller, D.4    Moroni, C.5    Karin, M.6    Chen, C.Y.7
  • 50
    • 77956261147 scopus 로고    scopus 로고
    • MAPKAP kinase 2 blocks tristetraprolin-directed mRNA decay by inhibiting CAF1 deadenylase recruitment.
    • Marchese FP, Aubareda A, Tudor C, Saklatvala J, Clark AR, Dean JL. MAPKAP kinase 2 blocks tristetraprolin-directed mRNA decay by inhibiting CAF1 deadenylase recruitment. J Biol Chem 2010, 285:27590-27600.
    • (2010) J Biol Chem , vol.285 , pp. 27590-27600
    • Marchese, F.P.1    Aubareda, A.2    Tudor, C.3    Saklatvala, J.4    Clark, A.R.5    Dean, J.L.6
  • 51
    • 78751504841 scopus 로고    scopus 로고
    • Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment.
    • Clement SL, Scheckel C, Stoecklin G, Lykke-Andersen J. Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment. Mol Cell Biol 2011, 31:256-266.
    • (2011) Mol Cell Biol , vol.31 , pp. 256-266
    • Clement, S.L.1    Scheckel, C.2    Stoecklin, G.3    Lykke-Andersen, J.4
  • 52
    • 78751477191 scopus 로고    scopus 로고
    • Gene silencing by micrornas: contributions of translational repression and mRNA decay.
    • Huntzinger E, Izaurralde E. Gene silencing by micrornas: contributions of translational repression and mRNA decay. Nat Rev Genet 2011, 12:99-110.
    • (2011) Nat Rev Genet , vol.12 , pp. 99-110
    • Huntzinger, E.1    Izaurralde, E.2
  • 53
    • 79955046372 scopus 로고    scopus 로고
    • The poly(rC)-binding protein αcp2 is a noncanonical factor inX. Laevis cytoplasmic polyadenylation.
    • Vishnu MR, Sumaroka M, Klein PS, Liebhaber SA. The poly(rC)-binding protein αcp2 is a noncanonical factor inX. Laevis cytoplasmic polyadenylation. RNA 2011, 17:944-956.
    • (2011) RNA , vol.17 , pp. 944-956
    • Vishnu, M.R.1    Sumaroka, M.2    Klein, P.S.3    Liebhaber, S.A.4
  • 54
    • 0742323558 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: splicing, translation and mRNP dynamics.
    • Maquat LE. Nonsense-mediated mRNA decay: splicing, translation and mRNP dynamics. Nat Rev Mol Cell Biol 2004, 5:89-99.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 89-99
    • Maquat, L.E.1
  • 55
    • 74549134095 scopus 로고    scopus 로고
    • How and where are nonsense mRNAs degraded in mammalian cells?
    • Muhlemann O, Lykke-Andersen J. How and where are nonsense mRNAs degraded in mammalian cells? RNA Biol 2010, 7:28-32.
    • (2010) RNA Biol , vol.7 , pp. 28-32
    • Muhlemann, O.1    Lykke-Andersen, J.2
  • 57
    • 32044435368 scopus 로고    scopus 로고
    • Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA decay.
    • Kashima I, Yamashita A, Izumi N, Kataoka N, Morishita R, Hoshino S, Ohno M, Dreyfuss G, Ohno S. Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA decay. Genes Dev 2006, 20:355-367.
    • (2006) Genes Dev , vol.20 , pp. 355-367
    • Kashima, I.1    Yamashita, A.2    Izumi, N.3    Kataoka, N.4    Morishita, R.5    Hoshino, S.6    Ohno, M.7    Dreyfuss, G.8    Ohno, S.9
  • 58
    • 78049447110 scopus 로고    scopus 로고
    • Smg6 interacts with the exon junction complex via two conserved EJC-binding motifs (EBMs) required for nonsense-mediated mRNA decay.
    • Kashima I, Jonas S, Jayachandran U, Buchwald G, Conti E, Lupas AN, Izaurralde E. Smg6 interacts with the exon junction complex via two conserved EJC-binding motifs (EBMs) required for nonsense-mediated mRNA decay. Genes Dev 2010, 24:2440-2450.
    • (2010) Genes Dev , vol.24 , pp. 2440-2450
    • Kashima, I.1    Jonas, S.2    Jayachandran, U.3    Buchwald, G.4    Conti, E.5    Lupas, A.N.6    Izaurralde, E.7
  • 60
    • 0027932513 scopus 로고
    • Premature translational termination triggers mRNA decapping.
    • Muhlrad D, Parker R. Premature translational termination triggers mRNA decapping. Nature 1994, 370:578-581.
    • (1994) Nature , vol.370 , pp. 578-581
    • Muhlrad, D.1    Parker, R.2
  • 61
    • 0037762554 scopus 로고    scopus 로고
    • An nmd pathway in yeast involving accelerated deadenylation and exosome-mediated 3′->5′ degradation.
    • Mitchell P, Tollervey D. An nmd pathway in yeast involving accelerated deadenylation and exosome-mediated 3′->5′ degradation. Mol Cell 2003, 11:1405-1413.
    • (2003) Mol Cell , vol.11 , pp. 1405-1413
    • Mitchell, P.1    Tollervey, D.2
  • 62
    • 0141819096 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities.
    • Lejeune F, Li X, Maquat LE. Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Mol Cell 2003, 12:675-687.
    • (2003) Mol Cell , vol.12 , pp. 675-687
    • Lejeune, F.1    Li, X.2    Maquat, L.E.3
  • 63
    • 0038112021 scopus 로고    scopus 로고
    • Rapid deadenylation triggered by a nonsense codon precedes decay of the RNA body in a mammalian cytoplasmic nonsense-mediated decay pathway.
    • Chen CY, Shyu AB. Rapid deadenylation triggered by a nonsense codon precedes decay of the RNA body in a mammalian cytoplasmic nonsense-mediated decay pathway. Mol Cell Biol 2003, 23:4805-4813.
    • (2003) Mol Cell Biol , vol.23 , pp. 4805-4813
    • Chen, C.Y.1    Shyu, A.B.2
  • 65
    • 0038402506 scopus 로고    scopus 로고
    • Computational modeling and experimental analysis of nonsense-mediated decay in yeast.
    • Cao D, Parker R. Computational modeling and experimental analysis of nonsense-mediated decay in yeast. Cell 2003, 113:533-545.
    • (2003) Cell , vol.113 , pp. 533-545
    • Cao, D.1    Parker, R.2
  • 66
    • 33744994837 scopus 로고    scopus 로고
    • EJC-independent degradation of nonsense immunoglobulin-mu mRNA depends on 3′ UTR length.
    • Buhler M, Steiner S, Mohn F, Paillusson A, Muhlemann O. EJC-independent degradation of nonsense immunoglobulin-mu mRNA depends on 3′ UTR length. Nat Struct Mol Biol 2006, 13:462-464.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 462-464
    • Buhler, M.1    Steiner, S.2    Mohn, F.3    Paillusson, A.4    Muhlemann, O.5
  • 67
    • 40949148553 scopus 로고    scopus 로고
    • Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways.
    • Ivanov PV, Gehring NH, Kunz JB, Hentze MW, Kulozik AE. Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways. EMBO J 2008, 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
  • 68
    • 33947609704 scopus 로고    scopus 로고
    • A conserved role for cytoplasmic poly(A)-binding protein 1 (PABPC1) in nonsense-mediated mRNA decay.
    • Behm-Ansmant I, Gatfield D, Rehwinkel J, Hilgers V, Izaurralde E. A conserved role for cytoplasmic poly(A)-binding protein 1 (PABPC1) in nonsense-mediated mRNA decay. EMBO J 2007, 26:1591-1601.
    • (2007) EMBO J , vol.26 , pp. 1591-1601
    • Behm-Ansmant, I.1    Gatfield, D.2    Rehwinkel, J.3    Hilgers, V.4    Izaurralde, E.5
  • 69
    • 40449131535 scopus 로고    scopus 로고
    • Proximity of the poly(A)-binding protein to a premature termination codon inhibits mammalian nonsense-mediated mRNA decay.
    • Silva AL, Ribeiro P, Inacio A, Liebhaber SA, Romao L. Proximity of the poly(A)-binding protein to a premature termination codon inhibits mammalian nonsense-mediated mRNA decay. RNA 2008, 14:563-576.
    • (2008) RNA , vol.14 , pp. 563-576
    • Silva, A.L.1    Ribeiro, P.2    Inacio, A.3    Liebhaber, S.A.4    Romao, L.5
  • 70
    • 8544253956 scopus 로고    scopus 로고
    • A faux 3′-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay.
    • Amrani N, Ganesan R, Kervestin S, Mangus DA, Ghosh S, Jacobson A. A faux 3′-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay. Nature 2004, 432:112-118.
    • (2004) Nature , vol.432 , pp. 112-118
    • Amrani, N.1    Ganesan, R.2    Kervestin, S.3    Mangus, D.A.4    Ghosh, S.5    Jacobson, A.6
  • 71
    • 0032880399 scopus 로고    scopus 로고
    • Aberrant mRNAs with extended 3′ UTRs are substrates for rapid degradation by mRNA surveillance.
    • Muhlrad D, Parker R. Aberrant mRNAs with extended 3′ UTRs are substrates for rapid degradation by mRNA surveillance. RNA 1999, 5:1299-1307.
    • (1999) RNA , vol.5 , pp. 1299-1307
    • Muhlrad, D.1    Parker, R.2
  • 72
    • 43249093760 scopus 로고    scopus 로고
    • Posttranscriptional gene regulation by spatial rearrangement of the 3′ untranslated region.
    • Eberle AB, Stalder L, Mathys H, Orozco RZ, Muhlemann O. Posttranscriptional gene regulation by spatial rearrangement of the 3′ untranslated region. PLoS Biol 2008, 6:e92.
    • (2008) PLoS Biol , vol.6
    • Eberle, A.B.1    Stalder, L.2    Mathys, H.3    Orozco, R.Z.4    Muhlemann, O.5
  • 73
    • 43249084802 scopus 로고    scopus 로고
    • A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay.
    • Singh G, Rebbapragada I, Lykke-Andersen J. A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay. PLoS Biol 2008, 6:e111.
    • (2008) PLoS Biol , vol.6
    • Singh, G.1    Rebbapragada, I.2    Lykke-Andersen, J.3
  • 74
    • 84862776849 scopus 로고    scopus 로고
    • Testing the faux-UTR model for NMD: Analysis of Upf1p and Pab1p competition for binding to eRF3/Sup35p.
    • Kervestin S, Li C, Buckingham R, Jacobson A. Testing the faux-UTR model for NMD: Analysis of Upf1p and Pab1p competition for binding to eRF3/Sup35p. Biochimie 2012, 94:1560-1571.
    • (2012) Biochimie , vol.94 , pp. 1560-1571
    • Kervestin, S.1    Li, C.2    Buckingham, R.3    Jacobson, A.4
  • 75
    • 38149035044 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in yeast does not require PAB1 or a poly(A) tail.
    • Meaux S, van Hoof A, Baker KE. Nonsense-mediated mRNA decay in yeast does not require PAB1 or a poly(A) tail. Mol Cell 2008, 29:134-140.
    • (2008) Mol Cell , vol.29 , pp. 134-140
    • Meaux, S.1    van Hoof, A.2    Baker, K.E.3
  • 76
    • 0036237537 scopus 로고    scopus 로고
    • Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [psi(+)] propagation.
    • Cosson B, Couturier A, Chabelskaya S, Kiktev D, Inge-Vechtomov S, Philippe M, Zhouravleva G. Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [psi(+)] propagation. Mol Cell Biol 2002, 22:3301-3315.
    • (2002) Mol Cell Biol , vol.22 , pp. 3301-3315
    • Cosson, B.1    Couturier, A.2    Chabelskaya, S.3    Kiktev, D.4    Inge-Vechtomov, S.5    Philippe, M.6    Zhouravleva, G.7
  • 78
    • 0037155584 scopus 로고    scopus 로고
    • Exosome-mediated recognition and degradation of mRNAs lacking a termination codon.
    • van Hoof A, Frischmeyer PA, Dietz HC, Parker R. Exosome-mediated recognition and degradation of mRNAs lacking a termination codon. Science 2002, 295:2262-2264.
    • (2002) Science , vol.295 , pp. 2262-2264
    • van Hoof, A.1    Frischmeyer, P.A.2    Dietz, H.C.3    Parker, R.4
  • 79
    • 0036715205 scopus 로고    scopus 로고
    • Non-stop decay-a new mRNA surveillance pathway.
    • Vasudevan S, Peltz SW, Wilusz CJ. Non-stop decay-a new mRNA surveillance pathway. Bioessays 2002, 24:785-788.
    • (2002) Bioessays , vol.24 , pp. 785-788
    • Vasudevan, S.1    Peltz, S.W.2    Wilusz, C.J.3
  • 80
    • 84867618518 scopus 로고    scopus 로고
    • Degradation of mRNAs that lack a stop codon: a decade of nonstop progress.
    • Klauer AA, van Hoof A. Degradation of mRNAs that lack a stop codon: a decade of nonstop progress. Wiley Interdiscip Rev RNA 2012.
    • (2012) Wiley Interdiscip Rev RNA
    • Klauer, A.A.1    van Hoof, A.2
  • 81
    • 58149178746 scopus 로고    scopus 로고
    • Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components.
    • Atkinson GC, Baldauf SL, Hauryliuk V. Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components. BMC Evol Biol 2008, 8:290.
    • (2008) BMC Evol Biol , vol.8 , pp. 290
    • Atkinson, G.C.1    Baldauf, S.L.2    Hauryliuk, V.3
  • 82
    • 84861456756 scopus 로고    scopus 로고
    • Dom34:Hbs1 plays a general role in quality-control systems by dissociation of a stalled ribosome at the 3′ end of aberrant mRNA.
    • Tsuboi T, Kuroha K, Kudo K, Makino S, Inoue E, Kashima I, Inada T. Dom34:Hbs1 plays a general role in quality-control systems by dissociation of a stalled ribosome at the 3′ end of aberrant mRNA. Mol Cell 2012, 46:518-529.
    • (2012) Mol Cell , vol.46 , pp. 518-529
    • Tsuboi, T.1    Kuroha, K.2    Kudo, K.3    Makino, S.4    Inoue, E.5    Kashima, I.6    Inada, T.7
  • 83
    • 33645277360 scopus 로고    scopus 로고
    • Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation.
    • Doma MK, Parker R. Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature 2006, 440:561-564.
    • (2006) Nature , vol.440 , pp. 561-564
    • Doma, M.K.1    Parker, R.2
  • 84
    • 80051673745 scopus 로고    scopus 로고
    • Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs.
    • Woo KC, Kim TD, Lee KH, Kim DY, Kim S, Lee HR, Kang HJ, Chung SJ, Senju S, Nishimura Y, et al. Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs. FASEB J 2011, 25:2757-2769.
    • (2011) FASEB J , vol.25 , pp. 2757-2769
    • Woo, K.C.1    Kim, T.D.2    Lee, K.H.3    Kim, D.Y.4    Kim, S.5    Lee, H.R.6    Kang, H.J.7    Chung, S.J.8    Senju, S.9    Nishimura, Y.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.