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Molecular and Cellular Biology
Volumn 35, Issue 2, 2015, Pages 468-478
Cyclin-dependent kinase 12 increases 3' end processing of growth factor-induced c-FOS transcripts
Author keywords

[No Author keywords available]
Indexed keywords

CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR 73; CLEAVAGE STIMULATING FACTOR 64; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE 12; EPIDERMAL GROWTH FACTOR; INITIATION FACTOR 4A; INITIATION FACTOR 4A3; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; NUCLEAR RECEPTOR NR4A3; RNA POLYMERASE II; SERINE ARGININE RICH PROTEIN; UNCLASSIFIED DRUG; CDK12 PROTEIN, HUMAN; PROTEIN C FOS; SIGNAL PEPTIDE;
EID: 84919665147     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01157-14     Document Type: Article
Times cited : (56)
References (84)
  • 1
    • 84871699564 scopus 로고    scopus 로고
    • Promoter-proximal pausing of RNA polymerase II: emerging roles in metazoans
    • Adelman K, Lis JT. 2012. Promoter-proximal pausing of RNA polymerase II: emerging roles in metazoans. Nat Rev Genet 13:720-731. http://dx.doi.org/10.1038/nrg3293.
    • (2012) Nat Rev Genet , vol.13 , pp. 720-731
    • Adelman, K.1    Lis, J.T.2
  • 2
    • 84872412814 scopus 로고    scopus 로고
    • RNA polymerase II transcription: structure and mechanism
    • Liu X, Bushnell DA, Kornberg RD. 2013. RNA polymerase II transcription: structure and mechanism. Biochim Biophys Acta 1829:2-8. http://dx.doi.org/10.1016/j.bbagrm.2012.09.003.
    • (2013) Biochim Biophys Acta , vol.1829 , pp. 2-8
    • Liu, X.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 3
    • 80052447253 scopus 로고    scopus 로고
    • Ending the message: poly(A) signals then and now
    • Proudfoot NJ. 2011. Ending the message: poly(A) signals then and now. Genes Dev 25:1770-1782. http://dx.doi.org/10.1101/gad.17268411.
    • (2011) Genes Dev , vol.25 , pp. 1770-1782
    • Proudfoot, N.J.1
  • 4
    • 2142716979 scopus 로고    scopus 로고
    • The link between mRNA processing and transcription: communication works both ways
    • Zorio DA, Bentley DL. 2004. The link between mRNA processing and transcription: communication works both ways. Exp Cell Res 296:91-97. http://dx.doi.org/10.1016/j.yexcr.2004.03.019.
    • (2004) Exp Cell Res , vol.296 , pp. 91-97
    • Zorio, D.A.1    Bentley, D.L.2
  • 5
    • 70350569286 scopus 로고    scopus 로고
    • Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches
    • Chen M, Manley JL. 2009. Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches. Nat Rev Mol Cell Biol 10:741-754. http://dx.doi.org/10.1038/nrm2777.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 741-754
    • Chen, M.1    Manley, J.L.2
  • 6
    • 84894318075 scopus 로고    scopus 로고
    • Coupling mRNA processing with transcription in time and space
    • Bentley DL. 2014. Coupling mRNA processing with transcription in time and space. Nat Rev Genet 15:163-175. http://dx.doi.org/10.1038/nrg3662.
    • (2014) Nat Rev Genet , vol.15 , pp. 163-175
    • Bentley, D.L.1
  • 7
    • 84874972604 scopus 로고    scopus 로고
    • Coupling pre-mRNA processing to transcription on the RNA factory assembly line
    • Lee KM, Tarn WY. 2013. Coupling pre-mRNA processing to transcription on the RNA factory assembly line. RNA Biol 10:380-390. http://dx.doi.org/10.4161/rna.23697.
    • (2013) RNA Biol , vol.10 , pp. 380-390
    • Lee, K.M.1    Tarn, W.Y.2
  • 8
    • 21644474090 scopus 로고    scopus 로고
    • Role of CDK/cyclin complexes in transcription and RNA splicing
    • Loyer P, Trembley JH, Katona R, Kidd VJ, Lahti JM. 2005. Role of CDK/cyclin complexes in transcription and RNA splicing. Cell Signal 17:1033-1051. http://dx.doi.org/10.1016/j.cellsig.2005.02.005.
    • (2005) Cell Signal , vol.17 , pp. 1033-1051
    • Loyer, P.1    Trembley, J.H.2    Katona, R.3    Kidd, V.J.4    Lahti, J.M.5
  • 9
    • 84879988130 scopus 로고    scopus 로고
    • Pause, play, repeat: CDKs push RNAP II's buttons
    • Sanso M, Fisher RP. 2013. Pause, play, repeat: CDKs push RNAP II's buttons. Transcription 4:146-152. http://dx.doi.org/10.4161/trns.25146.
    • (2013) Transcription , vol.4 , pp. 146-152
    • Sanso, M.1    Fisher, R.P.2
  • 10
    • 84888588009 scopus 로고    scopus 로고
    • The Mediator complex and transcription regulation
    • Poss ZC, Ebmeier CC, Taatjes DJ. 2013. The Mediator complex and transcription regulation. Crit Rev Biochem Mol 48:575-608. http://dx.doi.org/10.3109/10409238.2013.840259.
    • (2013) Crit Rev Biochem Mol , vol.48 , pp. 575-608
    • Poss, Z.C.1    Ebmeier, C.C.2    Taatjes, D.J.3
  • 11
    • 84872175836 scopus 로고    scopus 로고
    • The cell cycle rallies the transcription cycle: Cdc28/Cdk1 is a cell cycle-regulated transcriptional CDK
    • Chymkowitch P, Enserink JM. 2013. The cell cycle rallies the transcription cycle: Cdc28/Cdk1 is a cell cycle-regulated transcriptional CDK. Transcription 4:3-6. http://dx.doi.org/10.4161/trns.22456.
    • (2013) Transcription , vol.4 , pp. 3-6
    • Chymkowitch, P.1    Enserink, J.M.2
  • 12
    • 84872405841 scopus 로고    scopus 로고
    • Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription
    • Heidemann M, Hintermair C, Voss K, Eick D. 2013. Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription. Biochim Biophys Acta 1829:55-62. http://dx.doi.org/10.1016/j.bbagrm.2012.08.013.
    • (2013) Biochim Biophys Acta , vol.1829 , pp. 55-62
    • Heidemann, M.1    Hintermair, C.2    Voss, K.3    Eick, D.4
  • 13
    • 79952255182 scopus 로고    scopus 로고
    • CDK8: a positive regulator of transcription
    • Galbraith MD, Donner AJ, Espinosa JM. 2010. CDK8: a positive regulator of transcription. Transcription 1:4-12. http://dx.doi.org/10.4161/trns.1.1.12373.
    • (2010) Transcription , vol.1 , pp. 4-12
    • Galbraith, M.D.1    Donner, A.J.2    Espinosa, J.M.3
  • 14
    • 0033105827 scopus 로고    scopus 로고
    • Distinct roles for CTD Ser-2 and Ser-5 phosphorylation in the recruitment and allosteric activation of mammalian mRNA capping enzyme
    • Ho CK, Shuman S. 1999. Distinct roles for CTD Ser-2 and Ser-5 phosphorylation in the recruitment and allosteric activation of mammalian mRNA capping enzyme. Mol Cell 3:405-411. http://dx.doi.org/10.1016/S1097-2765(00)80468-2.
    • (1999) Mol Cell , vol.3 , pp. 405-411
    • Ho, C.K.1    Shuman, S.2
  • 15
    • 0031453408 scopus 로고    scopus 로고
    • mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain
    • Cho EJ, Takagi T, Moore CR, Buratowski S. 1997. mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev 11:3319-3326. http://dx.doi.org/10.1101/gad.11.24.3319.
    • (1997) Genes Dev , vol.11 , pp. 3319-3326
    • Cho, E.J.1    Takagi, T.2    Moore, C.R.3    Buratowski, S.4
  • 16
    • 84880475258 scopus 로고    scopus 로고
    • The CDK network: linking cycles of cell division and gene expression
    • Fisher RP. 2012. The CDK network: linking cycles of cell division and gene expression. Genes Cancer 3:731-738. http://dx.doi.org/10.1177/1947601912473308.
    • (2012) Genes Cancer , vol.3 , pp. 731-738
    • Fisher, R.P.1
  • 17
    • 0033515521 scopus 로고    scopus 로고
    • NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation
    • Yamaguchi Y, Takagi T, Wada T, Yano K, Furuya A, Sugimoto S, Hasegawa J, Handa H. 1999. NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation. Cell 97:41-51. http://dx.doi.org/10.1016/S0092-8674(00)80713-8.
    • (1999) Cell , vol.97 , pp. 41-51
    • Yamaguchi, Y.1    Takagi, T.2    Wada, T.3    Yano, K.4    Furuya, A.5    Sugimoto, S.6    Hasegawa, J.7    Handa, H.8
  • 19
    • 70449915963 scopus 로고    scopus 로고
    • Insights into the function of the human P-TEFb component CDK9 in the regulation of chromatin modifications and co-transcriptional mRNA processing
    • Pirngruber J, Shchebet A, Johnsen SA. 2009. Insights into the function of the human P-TEFb component CDK9 in the regulation of chromatin modifications and co-transcriptional mRNA processing. Cell Cycle 8:3636-3642. http://dx.doi.org/10.4161/cc.8.22.9890.
    • (2009) Cell Cycle , vol.8 , pp. 3636-3642
    • Pirngruber, J.1    Shchebet, A.2    Johnsen, S.A.3
  • 20
    • 33746403681 scopus 로고    scopus 로고
    • Controlling the elongation phase of transcription with P-TEFb
    • Peterlin BM, Price DH. 2006. Controlling the elongation phase of transcription with P-TEFb. Mol Cell 23:297-305. http://dx.doi.org/10.1016/j.molcel.2006.06.014.
    • (2006) Mol Cell , vol.23 , pp. 297-305
    • Peterlin, B.M.1    Price, D.H.2
  • 21
    • 0346095303 scopus 로고    scopus 로고
    • Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element
    • Fujinaga K, Irwin D, Huang Y, Taube R, Kurosu T, Peterlin BM. 2004. Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element. Mol Cell Biol 24:787-795. http://dx.doi.org/10.1128/MCB.24.2.787-795.2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 787-795
    • Fujinaga, K.1    Irwin, D.2    Huang, Y.3    Taube, R.4    Kurosu, T.5    Peterlin, B.M.6
  • 22
    • 0037154967 scopus 로고    scopus 로고
    • Integrating mRNA processing with transcription
    • Proudfoot NJ, Furger A, Dye MJ. 2002. Integrating mRNA processing with transcription. Cell 108:501-512. http://dx.doi.org/10.1016/S0092-8674(02)00617-7.
    • (2002) Cell , vol.108 , pp. 501-512
    • Proudfoot, N.J.1    Furger, A.2    Dye, M.J.3
  • 23
    • 84867160564 scopus 로고    scopus 로고
    • The RNA polymerase II CTD coordinates transcription and RNA processing
    • Hsin JP, Manley JL. 2012. The RNA polymerase II CTD coordinates transcription and RNA processing. Genes Dev 26:2119-2137. http://dx.doi.org/10.1101/gad.200303.112.
    • (2012) Genes Dev , vol.26 , pp. 2119-2137
    • Hsin, J.P.1    Manley, J.L.2
  • 25
    • 84881601434 scopus 로고    scopus 로고
    • Phosphorylation of RNA polymerase II is independent of P-TEFb in the C. elegans germline
    • Bowman EA, Bowman CR, Ahn JH, Kelly WG. 2013. Phosphorylation of RNA polymerase II is independent of P-TEFb in the C. elegans germline. Development 140:3703-3713. http://dx.doi.org/10.1242/dev.095778.
    • (2013) Development , vol.140 , pp. 3703-3713
    • Bowman, E.A.1    Bowman, C.R.2    Ahn, J.H.3    Kelly, W.G.4
  • 26
    • 84868681176 scopus 로고    scopus 로고
    • Interaction of cyclin-dependent kinase 12/CrkRS with cyclin K1 is required for the phosphorylation of the C-terminal domain of RNA polymerase II
    • Cheng SW, Kuzyk MA, Moradian A, Ichu TA, Chang VC, Tien JF, Vollett SE, Griffith M, Marra MA, Morin GB. 2012. Interaction of cyclin-dependent kinase 12/CrkRS with cyclin K1 is required for the phosphorylation of the C-terminal domain of RNA polymerase II. Mol Cell Biol 32:4691-4704. http://dx.doi.org/10.1128/MCB.06267-11.
    • (2012) Mol Cell Biol , vol.32 , pp. 4691-4704
    • Cheng, S.W.1    Kuzyk, M.A.2    Moradian, A.3    Ichu, T.A.4    Chang, V.C.5    Tien, J.F.6    Vollett, S.E.7    Griffith, M.8    Marra, M.A.9    Morin, G.B.10
  • 28
    • 84893936668 scopus 로고    scopus 로고
    • 3' End formation of pre-mRNA and phosphorylation of Ser2 on the RNA polymerase II CTD are reciprocally coupled in human cells
    • Davidson L, Muniz L, West S. 2014. 3' End formation of pre-mRNA and phosphorylation of Ser2 on the RNA polymerase II CTD are reciprocally coupled in human cells. Genes Dev 28:342-356. http://dx.doi.org/10.1101/gad.231274.113.
    • (2014) Genes Dev , vol.28 , pp. 342-356
    • Davidson, L.1    Muniz, L.2    West, S.3
  • 29
    • 0028028266 scopus 로고
    • A polyadenylation factor subunit is the human homolog of the Drosophila suppressor of forked protein
    • Takagaki Y, Manley JL. 1994. A polyadenylation factor subunit is the human homolog of the Drosophila suppressor of forked protein. Nature 372:471-474. http://dx.doi.org/10.1038/372471a0.
    • (1994) Nature , vol.372 , pp. 471-474
    • Takagaki, Y.1    Manley, J.L.2
  • 30
    • 0023511815 scopus 로고
    • Memories of Fos
    • Curran T, Morgan JI. 1987. Memories of Fos. Bioessays 7:255-258. http://dx.doi.org/10.1002/bies.950070606.
    • (1987) Bioessays , vol.7 , pp. 255-258
    • Curran, T.1    Morgan, J.I.2
  • 31
    • 27544468372 scopus 로고    scopus 로고
    • The Fos family of transcription factors and their role in tumourigenesis
    • Milde-Langosch K. 2005. The Fos family of transcription factors and their role in tumourigenesis. Eur J Cancer 41:2449-2461. http://dx.doi.org/10.1016/j.ejca.2005.08.008.
    • (2005) Eur J Cancer , vol.41 , pp. 2449-2461
    • Milde-Langosch, K.1
  • 32
    • 0026544430 scopus 로고
    • The human 64-Kda polyadenylylation factor contains a ribonucleoprotein-type RNAbinding domain and unusual auxiliary motifs
    • Takagaki Y, Macdonald CC, Shenk T, Manley JL. 1992. The human 64-Kda polyadenylylation factor contains a ribonucleoprotein-type RNAbinding domain and unusual auxiliary motifs. Proc Natl Acad Sci U S A 89:1403-1407. http://dx.doi.org/10.1073/pnas.89.4.1403.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 1403-1407
    • Takagaki, Y.1    Macdonald, C.C.2    Shenk, T.3    Manley, J.L.4
  • 33
    • 33845902048 scopus 로고    scopus 로고
    • Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease
    • Mandel CR, Kaneko S, Zhang HL, Gebauer D, Vethantham V, Manley JL, Tong L. 2006. Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease. Nature 444:953-956. http://dx.doi.org/10.1038/nature05363.
    • (2006) Nature , vol.444 , pp. 953-956
    • Mandel, C.R.1    Kaneko, S.2    Zhang, H.L.3    Gebauer, D.4    Vethantham, V.5    Manley, J.L.6    Tong, L.7
  • 34
    • 84873676209 scopus 로고    scopus 로고
    • CTD serine-2 plays a critical role in splicing and termination factor recruitment to RNA polymerase II in vivo
    • Gu B, Eick D, Bensaude O. 2013. CTD serine-2 plays a critical role in splicing and termination factor recruitment to RNA polymerase II in vivo. Nucleic Acids Res 41:1591-1603. http://dx.doi.org/10.1093/nar/gks1327.
    • (2013) Nucleic Acids Res , vol.41 , pp. 1591-1603
    • Gu, B.1    Eick, D.2    Bensaude, O.3
  • 35
    • 33847661809 scopus 로고    scopus 로고
    • Protocol for the fast chromatin immunoprecipitation (ChIP) method
    • Nelson JD, Denisenko O, Bomsztyk K. 2006. Protocol for the fast chromatin immunoprecipitation (ChIP) method. Nat Protoc 1:179-185. http://dx.doi.org/10.1038/nprot.2006.27.
    • (2006) Nat Protoc , vol.1 , pp. 179-185
    • Nelson, J.D.1    Denisenko, O.2    Bomsztyk, K.3
  • 36
    • 39849085276 scopus 로고    scopus 로고
    • RNA immunoprecipitation for determining RNA-protein associations in vivo
    • Gilbert C, Svejstrup JQ. 2006. RNA immunoprecipitation for determining RNA-protein associations in vivo. Curr Protoc Mol Biol Chapter 27: Unit 27.4. http://dx.doi.org/10.1002/0471142727.mb2704s75.
    • (2006) Curr Protoc Mol Biol Chapter 27: Unit 27.4
    • Gilbert, C.1    Svejstrup, J.Q.2
  • 37
    • 84867760525 scopus 로고    scopus 로고
    • Bromodomain and extra-terminal (BET) bromodomain inhibition activate transcription via transient release of positive transcription elongation factor b (P-TEFb) from 7SK small nuclear ribonucleoprotein
    • Bartholomeeusen K, Xiang Y, Fujinaga K, Peterlin BM. 2012. Bromodomain and extra-terminal (BET) bromodomain inhibition activate transcription via transient release of positive transcription elongation factor b (P-TEFb) from 7SK small nuclear ribonucleoprotein. J Biol Chem 287:36609-36616. http://dx.doi.org/10.1074/jbc.M112.410746.
    • (2012) J Biol Chem , vol.287 , pp. 36609-36616
    • Bartholomeeusen, K.1    Xiang, Y.2    Fujinaga, K.3    Peterlin, B.M.4
  • 39
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (+/- 10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser KR, Baker P, Burlingame AL. 1999. Role of accurate mass measurement (+/- 10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Anal Chem 71:2871-2882. http://dx.doi.org/10.1021/ac9810516.
    • (1999) Anal Chem , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3
  • 40
    • 0036826885 scopus 로고    scopus 로고
    • 5' Exon interactions within the human spliceosome establish a framework for exon Junction complex structure and assembly
    • Reichert VL, Le Hir H, Jurica MS, Moore MJ. 2002. 5' Exon interactions within the human spliceosome establish a framework for exon Junction complex structure and assembly. Genes Dev 16:2778-2791. http://dx.doi.org/10.1101/gad.1030602.
    • (2002) Genes Dev , vol.16 , pp. 2778-2791
    • Reichert, V.L.1    Le Hir, H.2    Jurica, M.S.3    Moore, M.J.4
  • 41
    • 0029894931 scopus 로고    scopus 로고
    • Identification of proteins that interact with exon sequences, splice sites, and the branchpoint sequence during each stage of spliceosome assembly
    • Chiara MD, Gozani O, Bennett M, Champion-Arnaud P, Palandjian L, Reed R. 1996. Identification of proteins that interact with exon sequences, splice sites, and the branchpoint sequence during each stage of spliceosome assembly. Mol Cell Biol 16:3317-3326.
    • (1996) Mol Cell Biol , vol.16 , pp. 3317-3326
    • Chiara, M.D.1    Gozani, O.2    Bennett, M.3    Champion-Arnaud, P.4    Palandjian, L.5    Reed, R.6
  • 42
    • 84870802818 scopus 로고    scopus 로고
    • Intimate liaison with SR proteins brings exon junction complexes to unexpected places
    • Muhlemann O. 2012. Intimate liaison with SR proteins brings exon junction complexes to unexpected places. Nat Struct Mol Biol 19:1209-1211. http://dx.doi.org/10.1038/nsmb.2454.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 1209-1211
    • Muhlemann, O.1
  • 43
    • 84869090905 scopus 로고    scopus 로고
    • The cellular EJC interactome reveals higher-order mRNP structure and an EJC-SR protein nexus
    • Singh G, Kucukural A, Cenik C, Leszyk JD, Shaffer SA, Weng Z, Moore MJ. 2012. The cellular EJC interactome reveals higher-order mRNP structure and an EJC-SR protein nexus. Cell 151:750-764. http://dx.doi.org/10.1016/j.cell.2012.10.007.
    • (2012) Cell , vol.151 , pp. 750-764
    • Singh, G.1    Kucukural, A.2    Cenik, C.3    Leszyk, J.D.4    Shaffer, S.A.5    Weng, Z.6    Moore, M.J.7
  • 44
    • 39149089317 scopus 로고    scopus 로고
    • Structural insights into the exon junction complex
    • Le Hir H, Andersen GR. 2008. Structural insights into the exon junction complex. Curr Opin Struc. Biol 18:112-119. http://dx.doi.org/10.1016/j.sbi.2007.11.002.
    • (2008) Curr Opin Struc. Biol , vol.18 , pp. 112-119
    • Le Hir, H.1    Andersen, G.R.2
  • 45
    • 34547927647 scopus 로고    scopus 로고
    • Introns play an essential role in splicing-dependent formation of the exon junction complex
    • Ideue T, Sasaki YT, Hagiwara M, Hirose T. 2007. Introns play an essential role in splicing-dependent formation of the exon junction complex. Genes Dev 21:1993-1998. http://dx.doi.org/10.1101/gad.1557907.
    • (2007) Genes Dev , vol.21 , pp. 1993-1998
    • Ideue, T.1    Sasaki, Y.T.2    Hagiwara, M.3    Hirose, T.4
  • 46
    • 85011942476 scopus 로고    scopus 로고
    • Assembly, disassembly and recycling: the dynamics of exon junction complexes
    • Bono F, Gehring NH. 2011. Assembly, disassembly and recycling: the dynamics of exon junction complexes. RNA Biol 8:24-29. http://dx.doi.org/10.4161/rna.8.1.13618.
    • (2011) RNA Biol , vol.8 , pp. 24-29
    • Bono, F.1    Gehring, N.H.2
  • 47
    • 1342325392 scopus 로고    scopus 로고
    • A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex
    • Kataoka N, Dreyfuss G. 2004. A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex. J Biol Chem 279:7009-7013.
    • (2004) J Biol Chem , vol.279 , pp. 7009-7013
    • Kataoka, N.1    Dreyfuss, G.2
  • 48
    • 0942268832 scopus 로고    scopus 로고
    • Splicing enhances translation in mammalian cells: an additional function of the exon junction complex
    • Nott A, Le Hir H, Moore MJ. 2004. Splicing enhances translation in mammalian cells: an additional function of the exon junction complex. Genes Dev 18:210-222. http://dx.doi.org/10.1101/gad.1163204.
    • (2004) Genes Dev , vol.18 , pp. 210-222
    • Nott, A.1    Le Hir, H.2    Moore, M.J.3
  • 49
    • 0141706348 scopus 로고    scopus 로고
    • Exon junction complexes mediate the enhancing effect of splicing on mRNA expression
    • Wiegand HL, Lu S, Cullen BR. 2003. Exon junction complexes mediate the enhancing effect of splicing on mRNA expression. Proc Natl Acad Sci U S A 100:11327-11332. http://dx.doi.org/10.1073/pnas.1934877100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 11327-11332
    • Wiegand, H.L.1    Lu, S.2    Cullen, B.R.3
  • 50
    • 34247197937 scopus 로고    scopus 로고
    • The nonsense-mediated decay RNA surveillance pathway
    • Chang YF, Imam JS, Wilkinson MF. 2007. The nonsense-mediated decay RNA surveillance pathway. Annu Rev Biochem 76:51-74. http://dx.doi.org/10.1146/annurev.biochem.76.050106.093909.
    • (2007) Annu Rev Biochem , vol.76 , pp. 51-74
    • Chang, Y.F.1    Imam, J.S.2    Wilkinson, M.F.3
  • 51
    • 0037175374 scopus 로고    scopus 로고
    • REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export
    • Gatfield D, Izaurralde E. 2002. REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export. J Cell Biol 159:579-588. http://dx.doi.org/10.1083/jcb.200207128.
    • (2002) J Cell Biol , vol.159 , pp. 579-588
    • Gatfield, D.1    Izaurralde, E.2
  • 52
    • 84878582352 scopus 로고    scopus 로고
    • Regulation of splicing by SR proteins and SR protein-specific kinases
    • Zhou Z, Fu XD. 2013. Regulation of splicing by SR proteins and SR protein-specific kinases. Chromosoma 122:191-207. http://dx.doi.org/10.1007/s00412-013-0407-z.
    • (2013) Chromosoma , vol.122 , pp. 191-207
    • Zhou, Z.1    Fu, X.D.2
  • 53
    • 0027137934 scopus 로고
    • Specific interactions between proteins implicated in splice site selection and regulated alternative splicing
    • Wu JY, Maniatis T. 1993. Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. Cell 75:1061-1070. http://dx.doi.org/10.1016/0092-8674(93)90316-I.
    • (1993) Cell , vol.75 , pp. 1061-1070
    • Wu, J.Y.1    Maniatis, T.2
  • 54
    • 76349090199 scopus 로고    scopus 로고
    • CDK8 is a positive regulator of transcriptional elongation within the serum response network
    • Donner AJ, Ebmeier CC, Taatjes DJ, Espinosa JM. 2010. CDK8 is a positive regulator of transcriptional elongation within the serum response network. Nat Struct Mol Biol 17:194-201. http://dx.doi.org/10.1038/nsmb.1752.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 194-201
    • Donner, A.J.1    Ebmeier, C.C.2    Taatjes, D.J.3    Espinosa, J.M.4
  • 56
    • 0037469729 scopus 로고    scopus 로고
    • Epidermal growth factor induces c-fos and c-jun mRNA via Raf-1/MEK1/ERK-dependent and -independent pathways in bovine luteal cells
    • Chen DB, Davis JS. 2003. Epidermal growth factor induces c-fos and c-jun mRNA via Raf-1/MEK1/ERK-dependent and -independent pathways in bovine luteal cells. Mol Cell Endocrinol 200:141-154. http://dx.doi.org/10.1016/S0303-7207(02)00379-9.
    • (2003) Mol Cell Endocrinol , vol.200 , pp. 141-154
    • Chen, D.B.1    Davis, J.S.2
  • 57
    • 64749099643 scopus 로고    scopus 로고
    • SR protein family members display diverse activities in the formation of nascent and mature mRNPs in vivo
    • Sapra AK, Anko ML, Grishina I, Lorenz M, Pabis M, Poser I, Rollins J, Weiland EM, Neugebauer KM. 2009. SR protein family members display diverse activities in the formation of nascent and mature mRNPs in vivo. Mol Cell 34:179-190. http://dx.doi.org/10.1016/j.molcel.2009.02.031.
    • (2009) Mol Cell , vol.34 , pp. 179-190
    • Sapra, A.K.1    Anko, M.L.2    Grishina, I.3    Lorenz, M.4    Pabis, M.5    Poser, I.6    Rollins, J.7    Weiland, E.M.8    Neugebauer, K.M.9
  • 58
    • 66249134562 scopus 로고    scopus 로고
    • The hierarchy of exon-junction complex assembly by the spliceosome explains key features of mammalian nonsense-mediated mRNA decay
    • Gehring NH, Lamprinaki S, Hentze MW, Kulozik AE. 2009. The hierarchy of exon-junction complex assembly by the spliceosome explains key features of mammalian nonsense-mediated mRNA decay. PLoS Biol 7:e1000120. http://dx.doi.org/10.1371/journal.pbio.1000120.
    • (2009) PLoS Biol , vol.7 , pp. e1000120
    • Gehring, N.H.1    Lamprinaki, S.2    Hentze, M.W.3    Kulozik, A.E.4
  • 59
    • 41949135532 scopus 로고    scopus 로고
    • EJCs at the heart of translational control
    • Le Hir H, Seraphin B. 2008. EJCs at the heart of translational control. Cell 133:213-216. http://dx.doi.org/10.1016/j.cell.2008.04.002.
    • (2008) Cell , vol.133 , pp. 213-216
    • Le Hir, H.1    Seraphin, B.2
  • 61
    • 0025695149 scopus 로고
    • A multisubunit factor, CstF, is required for polyadenylation of mammalian pre-mRNAs
    • Takagaki Y, Manley JL, MacDonald CC, Wilusz J, Shenk T. 1990. A multisubunit factor, CstF, is required for polyadenylation of mammalian pre-mRNAs. Genes Dev 4:2112-2120. http://dx.doi.org/10.1101/gad.4.12a.2112.
    • (1990) Genes Dev , vol.4 , pp. 2112-2120
    • Takagaki, Y.1    Manley, J.L.2    MacDonald, C.C.3    Wilusz, J.4    Shenk, T.5
  • 62
    • 0030784958 scopus 로고    scopus 로고
    • Mechanism and regulation of mRNA polyadenylation
    • Colgan DF, Manley JL. 1997. Mechanism and regulation of mRNA polyadenylation. Genes Dev 11:2755-2766. http://dx.doi.org/10.1101/gad.11.21.2755.
    • (1997) Genes Dev , vol.11 , pp. 2755-2766
    • Colgan, D.F.1    Manley, J.L.2
  • 63
    • 84869228761 scopus 로고    scopus 로고
    • Transcriptome-wide analyses of CstF64-RNA interactions in global regulation of mRNA alternative polyadenylation
    • Yao C, Biesinger J, Wan J, Weng L, Xing Y, Xie X, Shi Y. 2012. Transcriptome-wide analyses of CstF64-RNA interactions in global regulation of mRNA alternative polyadenylation. Proc Natl Acad Sci U S A 109:18773-18778. http://dx.doi.org/10.1073/pnas.1211101109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 18773-18778
    • Yao, C.1    Biesinger, J.2    Wan, J.3    Weng, L.4    Xing, Y.5    Xie, X.6    Shi, Y.7
  • 64
    • 84887290020 scopus 로고    scopus 로고
    • The human nuclear poly(a)-binding protein promotes RNA hyperadenylation and decay
    • Bresson SM, Conrad NK. 2013. The human nuclear poly(a)-binding protein promotes RNA hyperadenylation and decay. PLoS Genet 9:e1003893. http://dx.doi.org/10.1371/journal.pgen.1003893.
    • (2013) PLoS Genet , vol.9 , pp. e1003893
    • Bresson, S.M.1    Conrad, N.K.2
  • 65
    • 60149090021 scopus 로고    scopus 로고
    • The many pathways of RNA degradation
    • Houseley J, Tollervey D. 2009. The many pathways of RNA degradation. Cell 136:763-776. http://dx.doi.org/10.1016/j.cell.2009.01.019.
    • (2009) Cell , vol.136 , pp. 763-776
    • Houseley, J.1    Tollervey, D.2
  • 66
    • 0029973094 scopus 로고    scopus 로고
    • Interrelationships of the pathways of mRNA decay and translation in eukaryotic cells
    • Jacobson A, Peltz SW. 1996. Interrelationships of the pathways of mRNA decay and translation in eukaryotic cells. Annu Rev Biochem 65:693-739. http://dx.doi.org/10.1146/annurev.bi.65.070196.003401.
    • (1996) Annu Rev Biochem , vol.65 , pp. 693-739
    • Jacobson, A.1    Peltz, S.W.2
  • 67
    • 0035878112 scopus 로고    scopus 로고
    • Capping, splicing, and 3' processing are independently stimulated by RNA polymerase II: different functions for different segments of the CTD
    • Fong N, Bentley DL. 2001. Capping, splicing, and 3' processing are independently stimulated by RNA polymerase II: different functions for different segments of the CTD. Genes Dev 15:1783-1795. http://dx.doi.org/10.1101/gad.889101.
    • (2001) Genes Dev , vol.15 , pp. 1783-1795
    • Fong, N.1    Bentley, D.L.2
  • 68
    • 80053413109 scopus 로고    scopus 로고
    • Transcriptional activity regulates alternative cleavage and polyadenylation
    • Ji Z, Luo W, Li W, Hoque M, Pan Z, Zhao Y, Tian B. 2011. Transcriptional activity regulates alternative cleavage and polyadenylation. Mol Syst Biol 7:534. http://dx.doi.org/10.1038/msb.2011.69.
    • (2011) Mol Syst Biol , vol.7 , pp. 534
    • Ji, Z.1    Luo, W.2    Li, W.3    Hoque, M.4    Pan, Z.5    Zhao, Y.6    Tian, B.7
  • 69
    • 61449254471 scopus 로고    scopus 로고
    • Specific combinations of SR proteins associate with single premessenger RNAs in vivo and contribute different functions
    • Bjork P, Jin S, Zhao J, Singh OP, Persson JO, Hellman U, Wieslander L. 2009. Specific combinations of SR proteins associate with single premessenger RNAs in vivo and contribute different functions. J Cell Biol 184:555-568. http://dx.doi.org/10.1083/jcb.200806156.
    • (2009) J Cell Biol , vol.184 , pp. 555-568
    • Bjork, P.1    Jin, S.2    Zhao, J.3    Singh, O.P.4    Persson, J.O.5    Hellman, U.6    Wieslander, L.7
  • 70
    • 84900508949 scopus 로고    scopus 로고
    • Function and control of RNA polymerase II C-terminal domain phosphorylation in vertebrate transcription and RNA processing
    • Hsin JP, Xiang K, Manley JL. 2014. Function and control of RNA polymerase II C-terminal domain phosphorylation in vertebrate transcription and RNA processing. Mol Cell Biol 34:2488-2498. http://dx.doi.org/10.1128/MCB.00181-14.
    • (2014) Mol Cell Biol , vol.34 , pp. 2488-2498
    • Hsin, J.P.1    Xiang, K.2    Manley, J.L.3
  • 71
    • 0033920260 scopus 로고    scopus 로고
    • Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription
    • Zhou M, Halanski MA, Radonovich MF, Kashanchi F, Peng J, Price DH, Brady JN. 2000. Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription. Mol Cell Biol 20:5077-5086. http://dx.doi.org/10.1128/MCB.20.14.5077-5086.2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 5077-5086
    • Zhou, M.1    Halanski, M.A.2    Radonovich, M.F.3    Kashanchi, F.4    Peng, J.5    Price, D.H.6    Brady, J.N.7
  • 72
    • 84865419994 scopus 로고    scopus 로고
    • The super elongation complex (SEC) family in transcriptional control
    • Luo Z, Lin C, Shilatifard A. 2012. The super elongation complex (SEC) family in transcriptional control. Nat Rev Mol Cell Biol 13:543-547. http://dx.doi.org/10.1038/nrm3417.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 543-547
    • Luo, Z.1    Lin, C.2    Shilatifard, A.3
  • 73
    • 1542334001 scopus 로고    scopus 로고
    • Phosphorylation of serine 2 within the RNA polymerase II C-terminal domain couples transcription and 3' end processing
    • Ahn SH, Kim M, Buratowski S. 2004. Phosphorylation of serine 2 within the RNA polymerase II C-terminal domain couples transcription and 3' end processing. Mol Cell 13:67-76. http://dx.doi.org/10.1016/S1097-2765(03)00492-1.
    • (2004) Mol Cell , vol.13 , pp. 67-76
    • Ahn, S.H.1    Kim, M.2    Buratowski, S.3
  • 74
    • 1542290655 scopus 로고    scopus 로고
    • Transitions in RNA polymerase II elongation complexes at the 3' ends of genes
    • Kim M, Ahn SH, Krogan NJ, Greenblatt JF, Buratowski S. 2004. Transitions in RNA polymerase II elongation complexes at the 3' ends of genes. EMBO J 23:354-364. http://dx.doi.org/10.1038/sj.emboj.7600053.
    • (2004) EMBO J , vol.23 , pp. 354-364
    • Kim, M.1    Ahn, S.H.2    Krogan, N.J.3    Greenblatt, J.F.4    Buratowski, S.5
  • 75
    • 84857751341 scopus 로고    scopus 로고
    • An active role for splicing in 3'-end formation
    • Martinson HG. 2011. An active role for splicing in 3'-end formation. Wiley Interdiscip Rev RNA 2:459-470. http://dx.doi.org/10.1002/wrna.68.
    • (2011) Wiley Interdiscip Rev RNA , vol.2 , pp. 459-470
    • Martinson, H.G.1
  • 78
    • 0031834340 scopus 로고    scopus 로고
    • Human cyclin K, a novel RNA polymerase II-associated cyclin possessing both carboxy-terminal domain kinase and Cdk-activating kinase activity
    • Edwards MC, Wong C, Elledge SJ. 1998. Human cyclin K, a novel RNA polymerase II-associated cyclin possessing both carboxy-terminal domain kinase and Cdk-activating kinase activity. Mol Cell Biol 18:4291-4300.
    • (1998) Mol Cell Biol , vol.18 , pp. 4291-4300
    • Edwards, M.C.1    Wong, C.2    Elledge, S.J.3
  • 79
    • 84903973520 scopus 로고    scopus 로고
    • A distinct expression pattern of cyclin k in Mammalian testes suggests a functional role in spermatogenesis
    • Xiang X, Deng L, Zhang J, Zhang X, Lei T, Luan G, Yang C, Xiao ZX, Li Q, Li Q. 2014. A distinct expression pattern of cyclin k in Mammalian testes suggests a functional role in spermatogenesis. PLoS One 9:e101539. http://dx.doi.org/10.1371/journal.pone.0101539.
    • (2014) PLoS One , vol.9 , pp. e101539
    • Xiang, X.1    Deng, L.2    Zhang, J.3    Zhang, X.4    Lei, T.5    Luan, G.6    Yang, C.7    Xiao, Z.X.8    Li, Q.9    Li, Q.10
  • 82
    • 79954552505 scopus 로고    scopus 로고
    • The super elongation complex (SEC) and MLL in development and disease
    • Smith E, Lin C, Shilatifard A. 2011. The super elongation complex (SEC) and MLL in development and disease. Genes Dev 25:661-672. http://dx.doi.org/10.1101/gad.2015411.
    • (2011) Genes Dev , vol.25 , pp. 661-672
    • Smith, E.1    Lin, C.2    Shilatifard, A.3
  • 83
    • 0036648452 scopus 로고    scopus 로고
    • Amplification and expression of genes from the 17q11 approximately q12 amplicon in breast cancer cells
    • Luoh SW. 2002. Amplification and expression of genes from the 17q11 approximately q12 amplicon in breast cancer cells. Cancer Genet Cytogenet 136:43-47. http://dx.doi.org/10.1016/S0165-4608(01)00657-4.
    • (2002) Cancer Genet Cytogenet , vol.136 , pp. 43-47
    • Luoh, S.W.1

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