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Volumn 7, Issue 4, 2016, Pages 438-454

The Ccr4-Not complex is a key regulator of eukaryotic gene expression

Author keywords

[No Author keywords available]

Indexed keywords

CCR4 NOT COMPLEX; CHEMOKINE RECEPTOR CCR4; MEMBRANE PROTEIN; MESSENGER RNA; PROTEIN CAF1; PROTEIN NOT1; PROTEIN NOT2; PROTEIN NOT3; PROTEIN NOT4; PROTEIN NOT5; RETINOL BINDING PROTEIN 4; RNA POLYMERASE II; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84974688539     PISSN: 17577004     EISSN: 17577012     Source Type: Journal    
DOI: 10.1002/wrna.1332     Document Type: Review
Times cited : (230)

References (98)
  • 1
    • 4143055666 scopus 로고    scopus 로고
    • The eukaryotic Ccr4-not complex: a regulatory platform integrating mRNA metabolism with cellular signaling pathways?
    • Collart MA, Timmers HT . The eukaryotic Ccr4-not complex: a regulatory platform integrating mRNA metabolism with cellular signaling pathways? Prog Nucleic Acid Res Mol Biol 2004, 77:289–322.
    • (2004) Prog Nucleic Acid Res Mol Biol , vol.77 , pp. 289-322
    • Collart, M.A.1    Timmers, H.T.2
  • 2
    • 0347323165 scopus 로고    scopus 로고
    • The CCR4-NOT complex plays diverse roles in mRNA metabolism
    • Denis CL, Chen J . The CCR4-NOT complex plays diverse roles in mRNA metabolism. Prog Nucleic Acid Res Mol Biol 2003, 73:221–250.
    • (2003) Prog Nucleic Acid Res Mol Biol , vol.73 , pp. 221-250
    • Denis, C.L.1    Chen, J.2
  • 3
    • 0242285769 scopus 로고    scopus 로고
    • Global control of gene expression in yeast by the Ccr4-Not complex
    • Collart MA . Global control of gene expression in yeast by the Ccr4-Not complex. Gene 2003, 313:1–16.
    • (2003) Gene , vol.313 , pp. 1-16
    • Collart, M.A.1
  • 4
    • 84155195139 scopus 로고    scopus 로고
    • The Ccr4--not complex
    • Collart MA, Panasenko OO . The Ccr4--not complex. Gene 2012, 492:42–53.
    • (2012) Gene , vol.492 , pp. 42-53
    • Collart, M.A.1    Panasenko, O.O.2
  • 5
    • 84873247966 scopus 로고    scopus 로고
    • The Not3/5 subunit of the Ccr4-Not complex: a central regulator of gene expression that integrates signals between the cytoplasm and the nucleus in eukaryotic cells
    • Collart MA, Panasenko OO, Nikolaev SI . The Not3/5 subunit of the Ccr4-Not complex: a central regulator of gene expression that integrates signals between the cytoplasm and the nucleus in eukaryotic cells. Cell Signal 2013, 25:743–751.
    • (2013) Cell Signal , vol.25 , pp. 743-751
    • Collart, M.A.1    Panasenko, O.O.2    Nikolaev, S.I.3
  • 6
    • 84862685172 scopus 로고    scopus 로고
    • Ccr4-Not complex: the control freak of eukaryotic cells
    • Miller JE, Reese JC . Ccr4-Not complex: the control freak of eukaryotic cells. Crit Rev Biochem Mol Biol 2012, 47:315–333.
    • (2012) Crit Rev Biochem Mol Biol , vol.47 , pp. 315-333
    • Miller, J.E.1    Reese, J.C.2
  • 7
    • 84892377573 scopus 로고    scopus 로고
    • The cellular roles of Ccr4-NOT in model and pathogenic fungi-implications for fungal virulence
    • Panepinto JC, Heinz E, Traven A . The cellular roles of Ccr4-NOT in model and pathogenic fungi-implications for fungal virulence. Front Genet 2013, 4:302.
    • (2013) Front Genet , vol.4 , pp. 302
    • Panepinto, J.C.1    Heinz, E.2    Traven, A.3
  • 8
    • 84905672506 scopus 로고    scopus 로고
    • Insights into the structure and architecture of the CCR4-NOT complex
    • Xu K, Bai Y, Zhang A, Zhang Q, Bartlam MG . Insights into the structure and architecture of the CCR4-NOT complex. Front Genet 2014, 5:137.
    • (2014) Front Genet , vol.5 , pp. 137
    • Xu, K.1    Bai, Y.2    Zhang, A.3    Zhang, Q.4    Bartlam, M.G.5
  • 9
    • 84905665078 scopus 로고    scopus 로고
    • Novel roles of the multi-functional CCR4-NOT complex in post-transcriptional regulation
    • Inada T, Makino S . Novel roles of the multi-functional CCR4-NOT complex in post-transcriptional regulation. Front Genet 2014, 5:135.
    • (2014) Front Genet , vol.5 , pp. 135
    • Inada, T.1    Makino, S.2
  • 10
    • 84905668594 scopus 로고    scopus 로고
    • The role of the E3 ligase Not4 in cotranslational quality control
    • Panasenko OO . The role of the E3 ligase Not4 in cotranslational quality control. Front Genet 2014, 5:141.
    • (2014) Front Genet , vol.5 , pp. 141
    • Panasenko, O.O.1
  • 11
    • 84877801967 scopus 로고
    • RNA decay machines: deadenylation by the Ccr4-not and Pan2-Pan3 complexes
    • Wahle E, Winkler GS . RNA decay machines: deadenylation by the Ccr4-not and Pan2-Pan3 complexes. Biochim Biophys Acta 1829, 2013:561–570.
    • (1829) Biochim Biophys Acta , vol.2013 , pp. 561-570
    • Wahle, E.1    Winkler, G.S.2
  • 12
    • 84905671047 scopus 로고    scopus 로고
    • Deadenylation of mRNA by the CCR4-NOT complex in Drosophila: molecular and developmental aspects
    • Temme C, Simonelig M, Wahle E . Deadenylation of mRNA by the CCR4-NOT complex in Drosophila: molecular and developmental aspects. Front Genet 2014, 5:143.
    • (2014) Front Genet , vol.5 , pp. 143
    • Temme, C.1    Simonelig, M.2    Wahle, E.3
  • 13
    • 84906215359 scopus 로고    scopus 로고
    • Multifunctional roles of the mammalian CCR4-NOT complex in physiological phenomena
    • Shirai YT, Suzuki T, Morita M, Takahashi A, Yamamoto T . Multifunctional roles of the mammalian CCR4-NOT complex in physiological phenomena. Front Genet 2014, 5:286.
    • (2014) Front Genet , vol.5 , pp. 286
    • Shirai, Y.T.1    Suzuki, T.2    Morita, M.3    Takahashi, A.4    Yamamoto, T.5
  • 14
    • 85027916791 scopus 로고    scopus 로고
    • Novel roles of the CCR4-NOT complex
    • Chapat C, Corbo L . Novel roles of the CCR4-NOT complex. WIREs RNA 2014, 5:883–901.
    • (2014) WIREs RNA , vol.5 , pp. 883-901
    • Chapat, C.1    Corbo, L.2
  • 15
    • 84872398471 scopus 로고    scopus 로고
    • The control of elongation by the yeast Ccr4-not complex
    • Reese JC . The control of elongation by the yeast Ccr4-not complex. Biochim Biophys Acta 2013, 1829:127–133.
    • (2013) Biochim Biophys Acta , vol.1829 , pp. 127-133
    • Reese, J.C.1
  • 16
    • 84864383679 scopus 로고    scopus 로고
    • Deadenylation of cytoplasmic mRNA by the mammalian Ccr4-Not complex
    • Doidge R, Mittal S, Aslam A, Winkler GS . Deadenylation of cytoplasmic mRNA by the mammalian Ccr4-Not complex. Biochem Soc Trans 2012, 40:896–901.
    • (2012) Biochem Soc Trans , vol.40 , pp. 896-901
    • Doidge, R.1    Mittal, S.2    Aslam, A.3    Winkler, G.S.4
  • 17
    • 84892401030 scopus 로고    scopus 로고
    • Heterogeneity and complexity within the nuclease module of the Ccr4-Not complex
    • Winkler GS, Balacco DL . Heterogeneity and complexity within the nuclease module of the Ccr4-Not complex. Front Genet 2013, 4:296.
    • (2013) Front Genet , vol.4 , pp. 296
    • Winkler, G.S.1    Balacco, D.L.2
  • 18
    • 84908317412 scopus 로고    scopus 로고
    • The NOT4 RING E3 ligase: a relevant player in co-translational quality control
    • Collart MA . The NOT4 RING E3 ligase: a relevant player in co-translational quality control. ISRN Mol Biol 2013, doi: 10.1155/2013/548359.
    • (2013) ISRN Mol Biol
    • Collart, M.A.1
  • 20
    • 84874586399 scopus 로고    scopus 로고
    • NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT complex that docks onto the NOT1 N-terminal domain
    • Bawankar P, Loh B, Wohlbold L, Schmidt S, Izaurralde E . NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT complex that docks onto the NOT1 N-terminal domain. RNA Biol 2013, 10:228–244.
    • (2013) RNA Biol , vol.10 , pp. 228-244
    • Bawankar, P.1    Loh, B.2    Wohlbold, L.3    Schmidt, S.4    Izaurralde, E.5
  • 21
    • 0034692875 scopus 로고    scopus 로고
    • The essential function of Not1 lies within the Ccr4-Not complex
    • Maillet L, Tu C, Hong YK, Shuster EO, Collart MA . The essential function of Not1 lies within the Ccr4-Not complex. J Mol Biol 2000, 303:131–143.
    • (2000) J Mol Biol , vol.303 , pp. 131-143
    • Maillet, L.1    Tu, C.2    Hong, Y.K.3    Shuster, E.O.4    Collart, M.A.5
  • 22
    • 84930191835 scopus 로고    scopus 로고
    • Architecture of the ubiquitylation module of the yeast Ccr4-Not complex
    • Bhaskar V, Basquin J, Conti E . Architecture of the ubiquitylation module of the yeast Ccr4-Not complex. Structure 2015, 23:921–928.
    • (2015) Structure , vol.23 , pp. 921-928
    • Bhaskar, V.1    Basquin, J.2    Conti, E.3
  • 23
    • 79960366105 scopus 로고    scopus 로고
    • Insights into the structure of the CCR4-NOT complex by electron microscopy
    • Nasertorabi F, Batisse C, Diepholz M, Suck D, Bottcher B . Insights into the structure of the CCR4-NOT complex by electron microscopy. FEBS Lett 2011, 585:2182–2186.
    • (2011) FEBS Lett , vol.585 , pp. 2182-2186
    • Nasertorabi, F.1    Batisse, C.2    Diepholz, M.3    Suck, D.4    Bottcher, B.5
  • 24
    • 0021702006 scopus 로고
    • Identification of new genes involved in the regulation of yeast alcohol dehydrogenase II
    • Denis CL . Identification of new genes involved in the regulation of yeast alcohol dehydrogenase II. Genetics 1984, 108:833–844.
    • (1984) Genetics , vol.108 , pp. 833-844
    • Denis, C.L.1
  • 25
    • 0028268566 scopus 로고
    • NOT1(CDC39), NOT2(CDC36), NOT3, and NOT4 encode a global-negative regulator of transcription that differentially affects TATA-element utilization
    • Collart MA, Struhl K . NOT1(CDC39), NOT2(CDC36), NOT3, and NOT4 encode a global-negative regulator of transcription that differentially affects TATA-element utilization. Genes Dev 1994, 8:525–537.
    • (1994) Genes Dev , vol.8 , pp. 525-537
    • Collart, M.A.1    Struhl, K.2
  • 26
    • 0027394010 scopus 로고
    • CDC39, an essential nuclear protein that negatively regulates transcription and differentially affects the constitutive and inducible HIS3 promoters
    • Collart MA, Struhl K . CDC39, an essential nuclear protein that negatively regulates transcription and differentially affects the constitutive and inducible HIS3 promoters. EMBO J 1993, 12:177–186.
    • (1993) EMBO J , vol.12 , pp. 177-186
    • Collart, M.A.1    Struhl, K.2
  • 27
    • 0032545665 scopus 로고    scopus 로고
    • Characterization of NOT5 that encodes a new component of the Not protein complex
    • Oberholzer U, Collart MA . Characterization of NOT5 that encodes a new component of the Not protein complex. Gene 1998, 207:61–69.
    • (1998) Gene , vol.207 , pp. 61-69
    • Oberholzer, U.1    Collart, M.A.2
  • 28
    • 0029025449 scopus 로고
    • Identification of a mouse protein whose homolog in Saccharomyces cerevisiae is a component of the CCR4 transcriptional regulatory complex
    • Draper MP, Salvadore C, Denis CL . Identification of a mouse protein whose homolog in Saccharomyces cerevisiae is a component of the CCR4 transcriptional regulatory complex. Mol Cell Biol 1995, 15:3487–3495.
    • (1995) Mol Cell Biol , vol.15 , pp. 3487-3495
    • Draper, M.P.1    Salvadore, C.2    Denis, C.L.3
  • 29
    • 0035824883 scopus 로고    scopus 로고
    • Purification and characterization of the 1.0 MDa CCR4-NOT complex identifies two novel components of the complex
    • Chen J, Rappsilber J, Chiang YC, Russell P, Mann M, Denis CL . Purification and characterization of the 1.0 MDa CCR4-NOT complex identifies two novel components of the complex. J Mol Biol 2001, 314:683–694.
    • (2001) J Mol Biol , vol.314 , pp. 683-694
    • Chen, J.1    Rappsilber, J.2    Chiang, Y.C.3    Russell, P.4    Mann, M.5    Denis, C.L.6
  • 30
    • 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
  • 31
    • 0032374047 scopus 로고    scopus 로고
    • Human carbon catabolite repressor protein (CCR4)-associative factor 1: cloning, expression and characterization of its interaction with the B-cell translocation protein BTG1
    • Bogdan JA, Adams-Burton C, Pedicord DL, Sukovich DA, Benfield PA, Corjay MH, Stoltenborg JK, Dicker IB . Human carbon catabolite repressor protein (CCR4)-associative factor 1: cloning, expression and characterization of its interaction with the B-cell translocation protein BTG1. Biochem J 1998, 336(Pt 2):471–481.
    • (1998) Biochem J , vol.336 , pp. 471-481
    • Bogdan, J.A.1    Adams-Burton, C.2    Pedicord, D.L.3    Sukovich, D.A.4    Benfield, P.A.5    Corjay, M.H.6    Stoltenborg, J.K.7    Dicker, I.B.8
  • 33
    • 0041669422 scopus 로고    scopus 로고
    • BTG2 antiproliferative protein interacts with the human CCR4 complex existing in vivo in three cell-cycle-regulated forms
    • Morel AP, Sentis S, Bianchin C, Le Romancer M, Jonard L, Rostan MC, Rimokh R, Corbo L . BTG2 antiproliferative protein interacts with the human CCR4 complex existing in vivo in three cell-cycle-regulated forms. J Cell Sci 2003, 116:2929–2936.
    • (2003) J Cell Sci , vol.116 , pp. 2929-2936
    • Morel, A.P.1    Sentis, S.2    Bianchin, C.3    Le Romancer, M.4    Jonard, L.5    Rostan, M.C.6    Rimokh, R.7    Corbo, L.8
  • 34
    • 66849136862 scopus 로고    scopus 로고
    • Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome
    • Dimitrova LN, Kuroha K, Tatematsu T, Inada T . Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome. J Biol Chem 2009, 284:10343–10352.
    • (2009) J Biol Chem , vol.284 , pp. 10343-10352
    • Dimitrova, L.N.1    Kuroha, K.2    Tatematsu, T.3    Inada, T.4
  • 35
    • 84856026751 scopus 로고    scopus 로고
    • Presence of Not5 and ubiquitinated Rps7A in polysome fractions depends upon the Not4 E3 ligase
    • Panasenko OO, Collart MA . Presence of Not5 and ubiquitinated Rps7A in polysome fractions depends upon the Not4 E3 ligase. Mol Microbiol 2012, 83:640–653.
    • (2012) Mol Microbiol , vol.83 , pp. 640-653
    • Panasenko, O.O.1    Collart, M.A.2
  • 36
    • 34250374824 scopus 로고    scopus 로고
    • Analysis of P-body assembly in Saccharomyces cerevisiae
    • Teixeira D, Parker R . Analysis of P-body assembly in Saccharomyces cerevisiae . Mol Biol Cell 2007, 18:2274–2287.
    • (2007) Mol Biol Cell , vol.18 , pp. 2274-2287
    • Teixeira, D.1    Parker, R.2
  • 37
    • 52049101404 scopus 로고    scopus 로고
    • Regulators of cellular levels of histone acetylation in Saccharomyces cerevisiae
    • Peng W, Togawa C, Zhang K, Kurdistani SK . Regulators of cellular levels of histone acetylation in Saccharomyces cerevisiae . Genetics 2008, 179:277–289.
    • (2008) Genetics , vol.179 , pp. 277-289
    • Peng, W.1    Togawa, C.2    Zhang, K.3    Kurdistani, S.K.4
  • 38
    • 34249855658 scopus 로고    scopus 로고
    • Regulation of histone H3K4 tri-methylation and PAF complex recruitment by the Ccr4-Not complex
    • Mulder KW, Brenkman AB, Inagaki A, van den Broek NJ, Timmers HT . Regulation of histone H3K4 tri-methylation and PAF complex recruitment by the Ccr4-Not complex. Nucleic Acids Res 2007, 35:2428–2439.
    • (2007) Nucleic Acids Res , vol.35 , pp. 2428-2439
    • Mulder, K.W.1    Brenkman, A.B.2    Inagaki, A.3    van den Broek, N.J.4    Timmers, H.T.5
  • 40
    • 65249123408 scopus 로고    scopus 로고
    • Polyubiquitination of the demethylase Jhd2 controls histone methylation and gene expression
    • Mersman DP, Du HN, Fingerman IM, South PF, Briggs SD . Polyubiquitination of the demethylase Jhd2 controls histone methylation and gene expression. Genes Dev 2009, 23:951–962.
    • (2009) Genes Dev , vol.23 , pp. 951-962
    • Mersman, D.P.1    Du, H.N.2    Fingerman, I.M.3    South, P.F.4    Briggs, S.D.5
  • 44
    • 79952609007 scopus 로고    scopus 로고
    • The multifunctional Ccr4-Not complex directly promotes transcription elongation
    • Kruk JA, Dutta A, Fu J, Gilmour DS, Reese JC . The multifunctional Ccr4-Not complex directly promotes transcription elongation. Genes Dev 2011, 25:581–593.
    • (2011) Genes Dev , vol.25 , pp. 581-593
    • Kruk, J.A.1    Dutta, A.2    Fu, J.3    Gilmour, D.S.4    Reese, J.C.5
  • 45
    • 64349096829 scopus 로고    scopus 로고
    • A genome-wide RNAi screen identifies a new transcriptional module required for self-renewal
    • Hu G, Kim J, Xu Q, Leng Y, Orkin SH, Elledge SJ . A genome-wide RNAi screen identifies a new transcriptional module required for self-renewal. Genes Dev 2009, 23:837–848.
    • (2009) Genes Dev , vol.23 , pp. 837-848
    • Hu, G.1    Kim, J.2    Xu, Q.3    Leng, Y.4    Orkin, S.H.5    Elledge, S.J.6
  • 46
    • 84870674014 scopus 로고    scopus 로고
    • CNOT3 is a modifier of PRPF31 mutations in retinitis pigmentosa with incomplete penetrance
    • Venturini G, Rose AM, Shah AZ, Bhattacharya SS, Rivolta C . CNOT3 is a modifier of PRPF31 mutations in retinitis pigmentosa with incomplete penetrance. PLoS Genet 2012, 8:e1003040.
    • (2012) PLoS Genet , vol.8
    • Venturini, G.1    Rose, A.M.2    Shah, A.Z.3    Bhattacharya, S.S.4    Rivolta, C.5
  • 47
    • 1642483755 scopus 로고    scopus 로고
    • Repression of promoter activity by CNOT2, a subunit of the transcription regulatory Ccr4-not complex
    • Zwartjes CG, Jayne S, van den Berg DL, Timmers HT . Repression of promoter activity by CNOT2, a subunit of the transcription regulatory Ccr4-not complex. J Biol Chem 2004, 279:10848–10854.
    • (2004) J Biol Chem , vol.279 , pp. 10848-10854
    • Zwartjes, C.G.1    Jayne, S.2    van den Berg, D.L.3    Timmers, H.T.4
  • 48
    • 0032538977 scopus 로고    scopus 로고
    • Association of distinct yeast Not2 functional domains with components of Gcn5 histone acetylase and Ccr4 transcriptional regulatory complexes
    • Benson JD, Benson M, Howley PM, Struhl K . Association of distinct yeast Not2 functional domains with components of Gcn5 histone acetylase and Ccr4 transcriptional regulatory complexes. EMBO J 1998, 17:6714–6722.
    • (1998) EMBO J , vol.17 , pp. 6714-6722
    • Benson, J.D.1    Benson, M.2    Howley, P.M.3    Struhl, K.4
  • 49
    • 33746295893 scopus 로고    scopus 로고
    • Human Ccr4-Not complex is a ligand-dependent repressor of nuclear receptor-mediated transcription
    • Winkler GS, Mulder KW, Bardwell VJ, Kalkhoven E, Timmers HT . Human Ccr4-Not complex is a ligand-dependent repressor of nuclear receptor-mediated transcription. EMBO J 2006, 25:3089–3099.
    • (2006) EMBO J , vol.25 , pp. 3089-3099
    • Winkler, G.S.1    Mulder, K.W.2    Bardwell, V.J.3    Kalkhoven, E.4    Timmers, H.T.5
  • 50
    • 3042606545 scopus 로고    scopus 로고
    • c-Myb protein interacts with Rcd-1, a component of the CCR4 transcription mediator complex
    • Haas M, Siegert M, Schurmann A, Sodeik B, Wolfes H . c-Myb protein interacts with Rcd-1, a component of the CCR4 transcription mediator complex. Biochemistry 2004, 43:8152–8159.
    • (2004) Biochemistry , vol.43 , pp. 8152-8159
    • Haas, M.1    Siegert, M.2    Schurmann, A.3    Sodeik, B.4    Wolfes, H.5
  • 51
    • 84864560759 scopus 로고    scopus 로고
    • Proteolytic degradation of the Yap1 transcription factor is regulated by subcellular localization and the E3 ubiquitin ligase Not4
    • Gulshan K, Thommandru B, Moye-Rowley WS . Proteolytic degradation of the Yap1 transcription factor is regulated by subcellular localization and the E3 ubiquitin ligase Not4. J Biol Chem 2012, 287:26796–26805.
    • (2012) J Biol Chem , vol.287 , pp. 26796-26805
    • Gulshan, K.1    Thommandru, B.2    Moye-Rowley, W.S.3
  • 52
    • 84928730920 scopus 로고    scopus 로고
    • Protein degradation of RNA polymerase II-association factor 1(PAF1) is controlled by CNOT4 and 26S proteasome
    • Sun HY, Kim N, Hwang CS, Yoo JY . Protein degradation of RNA polymerase II-association factor 1(PAF1) is controlled by CNOT4 and 26S proteasome. PLoS One 2015, 10:e0125599.
    • (2015) PLoS One , vol.10
    • Sun, H.Y.1    Kim, N.2    Hwang, C.S.3    Yoo, J.Y.4
  • 53
    • 19944399062 scopus 로고    scopus 로고
    • The Ccr4-Not complex independently controls both Msn2-dependent transcriptional activation--via a newly identified Glc7/Bud14 type I protein phosphatase module--and TFIID promoter distribution
    • Lenssen E, James N, Pedruzzi I, Dubouloz F, Cameroni E, Bisig R, Maillet L, Werner M, Roosen J, Petrovic K, et al. The Ccr4-Not complex independently controls both Msn2-dependent transcriptional activation--via a newly identified Glc7/Bud14 type I protein phosphatase module--and TFIID promoter distribution. Mol Cell Biol 2005, 25:488–498.
    • (2005) Mol Cell Biol , vol.25 , pp. 488-498
    • Lenssen, E.1    James, N.2    Pedruzzi, I.3    Dubouloz, F.4    Cameroni, E.5    Bisig, R.6    Maillet, L.7    Werner, M.8    Roosen, J.9    Petrovic, K.10
  • 54
    • 35048897014 scopus 로고    scopus 로고
    • A SAGA-independent function of SPT3 mediates transcriptional deregulation in a mutant of the Ccr4-not complex in Saccharomyces cerevisiae
    • James N, Landrieux E, Collart MA . A SAGA-independent function of SPT3 mediates transcriptional deregulation in a mutant of the Ccr4-not complex in Saccharomyces cerevisiae . Genetics 2007, 177:123–135.
    • (2007) Genetics , vol.177 , pp. 123-135
    • James, N.1    Landrieux, E.2    Collart, M.A.3
  • 55
    • 43349106039 scopus 로고    scopus 로고
    • Genome wide expression analysis of the CCR4-NOT complex indicates that it consists of three modules with the NOT module controlling SAGA-responsive genes
    • Cui Y, Ramnarain DB, Chiang YC, Ding LH, McMahon JS, Denis CL . Genome wide expression analysis of the CCR4-NOT complex indicates that it consists of three modules with the NOT module controlling SAGA-responsive genes. Mol Genet Genomics 2008, 279:323–337.
    • (2008) Mol Genet Genomics , vol.279 , pp. 323-337
    • Cui, Y.1    Ramnarain, D.B.2    Chiang, Y.C.3    Ding, L.H.4    McMahon, J.S.5    Denis, C.L.6
  • 56
    • 0034971991 scopus 로고    scopus 로고
    • Genetic evidence supports a role for the yeast CCR4-NOT complex in transcriptional elongation
    • Denis CL, Chiang YC, Cui Y, Chen J . Genetic evidence supports a role for the yeast CCR4-NOT complex in transcriptional elongation. Genetics 2001, 158:627–634.
    • (2001) Genetics , vol.158 , pp. 627-634
    • Denis, C.L.1    Chiang, Y.C.2    Cui, Y.3    Chen, J.4
  • 58
    • 84912098443 scopus 로고    scopus 로고
    • The Rpb4/7 module of RNA polymerase II is required for carbon catabolite repressor protein 4-negative on TATA (Ccr4-Not) complex to promote elongation
    • Babbarwal V, Fu J, Reese JC . The Rpb4/7 module of RNA polymerase II is required for carbon catabolite repressor protein 4-negative on TATA (Ccr4-Not) complex to promote elongation. J Biol Chem 2014, 289:33125–33130.
    • (2014) J Biol Chem , vol.289 , pp. 33125-33130
    • Babbarwal, V.1    Fu, J.2    Reese, J.C.3
  • 60
    • 0034006399 scopus 로고    scopus 로고
    • Transcription elongation factor SII
    • Wind M, Reines D . Transcription elongation factor SII. Bioessays 2000, 22:327–336.
    • (2000) Bioessays , vol.22 , pp. 327-336
    • Wind, M.1    Reines, D.2
  • 62
    • 0036889142 scopus 로고    scopus 로고
    • Interactions between mRNA export commitment, 3′-end quality control, and nuclear degradation
    • Libri D, Dower K, Boulay J, Thomsen R, Rosbash M, Jensen TH . Interactions between mRNA export commitment, 3′-end quality control, and nuclear degradation. Mol Cell Biol 2002, 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
  • 64
    • 69449094660 scopus 로고    scopus 로고
    • The CCR4-NOT complex physically and functionally interacts with TRAMP and the nuclear exosome
    • Azzouz N, Panasenko OO, Colau G, Collart MA . The CCR4-NOT complex physically and functionally interacts with TRAMP and the nuclear exosome. PLoS One 2009, 4:e6760.
    • (2009) PLoS One , vol.4
    • Azzouz, N.1    Panasenko, O.O.2    Colau, G.3    Collart, M.A.4
  • 65
    • 80053199328 scopus 로고    scopus 로고
    • Implication of Ccr4-Not complex function in mRNA quality control in Saccharomyces cerevisiae
    • Assenholt J, Mouaikel J, Saguez C, Rougemaille M, Libri D, Jensen TH . Implication of Ccr4-Not complex function in mRNA quality control in Saccharomyces cerevisiae . RNA 2011, 17:1788–1794.
    • (2011) RNA , vol.17 , pp. 1788-1794
    • Assenholt, J.1    Mouaikel, J.2    Saguez, C.3    Rougemaille, M.4    Libri, D.5    Jensen, T.H.6
  • 66
    • 84865658810 scopus 로고    scopus 로고
    • P-bodies and stress granules: possible roles in the control of translation and mRNA degradation
    • Decker CJ, Parker R . P-bodies and stress granules: possible roles in the control of translation and mRNA degradation. Cold Spring Harb Perspect Biol 2012, 4:a012286.
    • (2012) Cold Spring Harb Perspect Biol , vol.4 , pp. 012286
    • Decker, C.J.1    Parker, R.2
  • 68
    • 84858210854 scopus 로고    scopus 로고
    • HSP90 and the R2TP co-chaperone complex: building multi-protein machineries essential for cell growth and gene expression
    • Boulon S, Bertrand E, Pradet-Balade B . HSP90 and the R2TP co-chaperone complex: building multi-protein machineries essential for cell growth and gene expression. RNA Biol 2012, 9:148–154.
    • (2012) RNA Biol , vol.9 , pp. 148-154
    • Boulon, S.1    Bertrand, E.2    Pradet-Balade, B.3
  • 69
    • 79953150421 scopus 로고    scopus 로고
    • Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29
    • Panasenko OO, Collart MA . Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29. Mol Cell Biol 2011, 31:1610–1623.
    • (2011) Mol Cell Biol , vol.31 , pp. 1610-1623
    • Panasenko, O.O.1    Collart, M.A.2
  • 70
    • 33846008044 scopus 로고    scopus 로고
    • The yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EGD) complex
    • Panasenko O, Landrieux E, Feuermann M, Finka A, Paquet N, Collart MA . The yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EGD) complex. J Biol Chem 2006, 281:31389–31398.
    • (2006) J Biol Chem , vol.281 , pp. 31389-31398
    • Panasenko, O.1    Landrieux, E.2    Feuermann, M.3    Finka, A.4    Paquet, N.5    Collart, M.A.6
  • 71
    • 84898429935 scopus 로고    scopus 로고
    • The Not4 E3 ligase and CCR4 deadenylase play distinct roles in protein quality control
    • Halter D, Collart MA, Panasenko OO . The Not4 E3 ligase and CCR4 deadenylase play distinct roles in protein quality control. PLoS One 2014, 9:e86218.
    • (2014) PLoS One , vol.9
    • Halter, D.1    Collart, M.A.2    Panasenko, O.O.3
  • 72
    • 77957169824 scopus 로고    scopus 로고
    • Role of a ribosome-associated E3 ubiquitin ligase in protein quality control
    • Bengtson MH, Joazeiro CA . Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature 2010, 467:470–473.
    • (2010) Nature , vol.467 , pp. 470-473
    • Bengtson, M.H.1    Joazeiro, C.A.2
  • 73
    • 84948573230 scopus 로고    scopus 로고
    • Not4-dependent translational repression is important for cellular protein homeostasis in yeast
    • Preissler S, Reuther J, Koch M, Scior A, Bruderek M, Frickey T, Deuerling E . Not4-dependent translational repression is important for cellular protein homeostasis in yeast. EMBO J 2015, 34:1905–1924.
    • (2015) EMBO J , vol.34 , pp. 1905-1924
    • Preissler, S.1    Reuther, J.2    Koch, M.3    Scior, A.4    Bruderek, M.5    Frickey, T.6    Deuerling, E.7
  • 74
    • 77956503398 scopus 로고    scopus 로고
    • Translational repression by deadenylases
    • Cooke A, Prigge A, Wickens M . Translational repression by deadenylases. J Biol Chem 2010, 285:28506–28513.
    • (2010) J Biol Chem , vol.285 , pp. 28506-28513
    • Cooke, A.1    Prigge, A.2    Wickens, M.3
  • 75
    • 33748754298 scopus 로고    scopus 로고
    • Rapid ATP-dependent deadenylation of nanos mRNA in a cell-free system from Drosophila embryos
    • Jeske M, Meyer S, Temme C, Freudenreich D, Wahle E . Rapid ATP-dependent deadenylation of nanos mRNA in a cell-free system from Drosophila embryos. J Biol Chem 2006, 281:25124–25133.
    • (2006) J Biol Chem , vol.281 , pp. 25124-25133
    • Jeske, M.1    Meyer, S.2    Temme, C.3    Freudenreich, D.4    Wahle, E.5
  • 76
    • 34447503943 scopus 로고    scopus 로고
    • Two yeast PUF proteins negatively regulate a single mRNA
    • Hook BA, Goldstrohm AC, Seay DJ, Wickens M . Two yeast PUF proteins negatively regulate a single mRNA. J Biol Chem 2007, 282:15430–15438.
    • (2007) J Biol Chem , vol.282 , pp. 15430-15438
    • Hook, B.A.1    Goldstrohm, A.C.2    Seay, D.J.3    Wickens, M.4
  • 77
    • 84931057948 scopus 로고    scopus 로고
    • Xenopus CAF1 requires NOT1-mediated interaction with 4E-T to repress translation in vivo
    • Waghray S, Williams C, Coon JJ, Wickens M . Xenopus CAF1 requires NOT1-mediated interaction with 4E-T to repress translation in vivo. RNA 2015, 21:1335–1345.
    • (2015) RNA , vol.21 , pp. 1335-1345
    • Waghray, S.1    Williams, C.2    Coon, J.J.3    Wickens, M.4
  • 78
    • 84930757315 scopus 로고    scopus 로고
    • The eIF4E-binding protein 4E-T is a component of the mRNA decay machinery that bridges the 5′ and 3′ termini of target mRNAs
    • Nishimura T, Padamsi Z, Fakim H, Milette S, Dunham WH, Gingras AC, Fabian MR . The eIF4E-binding protein 4E-T is a component of the mRNA decay machinery that bridges the 5′ and 3′ termini of target mRNAs. Cell Rep 2015, 11:1425–1436.
    • (2015) Cell Rep , vol.11 , pp. 1425-1436
    • Nishimura, T.1    Padamsi, Z.2    Fakim, H.3    Milette, S.4    Dunham, W.H.5    Gingras, A.C.6    Fabian, M.R.7
  • 79
    • 84945584585 scopus 로고    scopus 로고
    • Structure of a human 4E-T/DDX6/CNOT1 complex reveals the different interplay of DDX6-binding proteins with the CCR4-NOT complex
    • Ozgur S, Basquin J, Kamenska A, Filipowicz W, Standart N, Conti E . Structure of a human 4E-T/DDX6/CNOT1 complex reveals the different interplay of DDX6-binding proteins with the CCR4-NOT complex. Cell Rep 2015, 13:703–711.
    • (2015) Cell Rep , vol.13 , pp. 703-711
    • Ozgur, S.1    Basquin, J.2    Kamenska, A.3    Filipowicz, W.4    Standart, N.5    Conti, E.6
  • 82
    • 84906874947 scopus 로고    scopus 로고
    • Human DDX6 effects miRNA-mediated gene silencing via direct binding to CNOT1
    • Rouya C, Siddiqui N, Morita M, Duchaine TF, Fabian MR, Sonenberg N . Human DDX6 effects miRNA-mediated gene silencing via direct binding to CNOT1. RNA 2014, 20:1398–1409.
    • (2014) RNA , vol.20 , pp. 1398-1409
    • Rouya, C.1    Siddiqui, N.2    Morita, M.3    Duchaine, T.F.4    Fabian, M.R.5    Sonenberg, N.6
  • 83
    • 25144482816 scopus 로고    scopus 로고
    • General translational repression by activators of mRNA decapping
    • Coller J, Parker R . General translational repression by activators of mRNA decapping. Cell 2005, 122:875–886.
    • (2005) Cell , vol.122 , pp. 875-886
    • Coller, J.1    Parker, R.2
  • 84
    • 84863688029 scopus 로고    scopus 로고
    • The DEAD-box protein Dhh1 promotes decapping by slowing ribosome movement
    • Sweet T, Kovalak C, Coller J . The DEAD-box protein Dhh1 promotes decapping by slowing ribosome movement. PLoS Biol 2012, 10:e1001342.
    • (2012) PLoS Biol , vol.10
    • Sweet, T.1    Kovalak, C.2    Coller, J.3
  • 85
    • 0037169544 scopus 로고    scopus 로고
    • Interaction between Not1p, a component of the Ccr4-not complex, a global regulator of transcription, and Dhh1p, a putative RNA helicase
    • Maillet L, Collart MA . Interaction between Not1p, a component of the Ccr4-not complex, a global regulator of transcription, and Dhh1p, a putative RNA helicase. J Biol Chem 2002, 277:2835–2842.
    • (2002) J Biol Chem , vol.277 , pp. 2835-2842
    • Maillet, L.1    Collart, M.A.2
  • 86
    • 80955125826 scopus 로고    scopus 로고
    • The role of the CNOT1 subunit of the CCR4-NOT complex in mRNA deadenylation and cell viability
    • Ito K, Takahashi A, Morita M, Suzuki T, Yamamoto T . The role of the CNOT1 subunit of the CCR4-NOT complex in mRNA deadenylation and cell viability. Protein Cell 2011, 2:755–763.
    • (2011) Protein Cell , vol.2 , pp. 755-763
    • Ito, K.1    Takahashi, A.2    Morita, M.3    Suzuki, T.4    Yamamoto, T.5
  • 87
    • 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
  • 88
    • 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
  • 89
    • 73949116438 scopus 로고    scopus 로고
    • The mammalian anti-proliferative BTG/Tob protein family
    • Winkler GS . The mammalian anti-proliferative BTG/Tob protein family. J Cell Physiol 2010, 222:66–72.
    • (2010) J Cell Physiol , vol.222 , pp. 66-72
    • Winkler, G.S.1
  • 90
    • 84885356907 scopus 로고    scopus 로고
    • The SMG5-SMG7 heterodimer directly recruits the CCR4-NOT deadenylase complex to mRNAs containing nonsense codons via interaction with POP2
    • Loh B, Jonas S, Izaurralde E . The SMG5-SMG7 heterodimer directly recruits the CCR4-NOT deadenylase complex to mRNAs containing nonsense codons via interaction with POP2. Genes Dev 2013, 27:2125–2138.
    • (2013) Genes Dev , vol.27 , pp. 2125-2138
    • Loh, B.1    Jonas, S.2    Izaurralde, E.3
  • 92
    • 84898869373 scopus 로고    scopus 로고
    • Structural basis for the Nanos-mediated recruitment of the CCR4-NOT complex and translational repression
    • Bhandari D, Raisch T, Weichenrieder O, Jonas S, Izaurralde E . Structural basis for the Nanos-mediated recruitment of the CCR4-NOT complex and translational repression. Genes Dev 2014, 28:888–901.
    • (2014) Genes Dev , vol.28 , pp. 888-901
    • Bhandari, D.1    Raisch, T.2    Weichenrieder, O.3    Jonas, S.4    Izaurralde, E.5
  • 93
    • 84870956288 scopus 로고    scopus 로고
    • The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex
    • Doidge R, Mittal S, Aslam A, Winkler GS . The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex. PLoS One 2012, 7:e51331.
    • (2012) PLoS One , vol.7
    • Doidge, R.1    Mittal, S.2    Aslam, A.3    Winkler, G.S.4
  • 94
    • 84925003798 scopus 로고    scopus 로고
    • The long unfinished march towards understanding microRNA-mediated repression
    • Filipowicz W, Sonenberg N . The long unfinished march towards understanding microRNA-mediated repression. RNA 2015, 21:519–524.
    • (2015) RNA , vol.21 , pp. 519-524
    • Filipowicz, W.1    Sonenberg, N.2
  • 95
    • 16344395154 scopus 로고    scopus 로고
    • The yeast EDC1 mRNA undergoes deadenylation-independent decapping stimulated by Not2p, Not4p, and Not5p
    • Muhlrad D, Parker R . The yeast EDC1 mRNA undergoes deadenylation-independent decapping stimulated by Not2p, Not4p, and Not5p. EMBO J 2005, 24:1033–1045.
    • (2005) EMBO J , vol.24 , pp. 1033-1045
    • Muhlrad, D.1    Parker, R.2
  • 96
    • 84957812425 scopus 로고    scopus 로고
    • Ccr4-Not is at the core of the eukaryotic gene expression circuitry
    • Villanyi Z, Collart MA . Ccr4-Not is at the core of the eukaryotic gene expression circuitry. Biochem Soc Trans 2015, 43:1253–1258.
    • (2015) Biochem Soc Trans , vol.43 , pp. 1253-1258
    • Villanyi, Z.1    Collart, M.A.2
  • 97
    • 29144508551 scopus 로고    scopus 로고
    • The RNA polymerase II subunit Rpb4p mediates decay of a specific class of mRNAs
    • Lotan R, Bar-On VG, Harel-Sharvit L, Duek L, Melamed D, Choder M . The RNA polymerase II subunit Rpb4p mediates decay of a specific class of mRNAs. Genes Dev 2005, 19:3004–3016.
    • (2005) Genes Dev , vol.19 , pp. 3004-3016
    • Lotan, R.1    Bar-On, V.G.2    Harel-Sharvit, L.3    Duek, L.4    Melamed, D.5    Choder, M.6
  • 98
    • 84901388832 scopus 로고    scopus 로고
    • Gene expression as a circular process: cross-talk between transcription and mRNA degradation in eukaryotes; International University of Andalusia (UNIA) Baeza, Spain
    • Collart MA, Reese JC . Gene expression as a circular process: cross-talk between transcription and mRNA degradation in eukaryotes; International University of Andalusia (UNIA) Baeza, Spain. RNA Biol 2014, 11:320–323.
    • (2014) RNA Biol , vol.11 , pp. 320-323
    • Collart, M.A.1    Reese, J.C.2


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