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Volumn 9, Issue 9, 2010, Pages 1697-1705

CYCLINg through transcription: Posttranslational modifications of P-TEFb regulate transcription elongation

Author keywords

CDK9; Cyclin T; RNA polymerase II; Transcription elongation

Indexed keywords

CYCLIN DEPENDENT KINASE 9; CYCLIN T1; POSITIVE TRANSCRIPTION ELONGATION FACTOR B;

EID: 77953548232     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.9.9.11346     Document Type: Review
Times cited : (58)

References (89)
  • 3
    • 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, et al. NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation. Cell 1999; 97:41-51. (Pubitemid 29165888)
    • (1999) Cell , vol.97 , Issue.1 , 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
  • 4
    • 34447098370 scopus 로고    scopus 로고
    • A Chromatin Landmark and Transcription Initiation at Most Promoters in Human Cells
    • DOI 10.1016/j.cell.2007.05.042, PII S0092867407006812
    • Guenther MG, Levine SS, Boyer LA, Jaenisch R, Young RA. A chromatin landmark and transcription initiation at most promoters in human cells. Cell 2007; 130:77-88. (Pubitemid 47031323)
    • (2007) Cell , vol.130 , Issue.1 , pp. 77-88
    • Guenther, M.G.1    Levine, S.S.2    Boyer, L.A.3    Jaenisch, R.4    Young, R.A.5
  • 6
    • 36549013619 scopus 로고    scopus 로고
    • RNA polymerase stalling at developmental control genes in the Drosophila melanogaster embryo
    • Zeitlinger J, Stark A, Kellis M, Hong JW, Nechaev S, Adelman K, et al. RNA polymerase stalling at developmental control genes in the Drosophila melanogaster embryo. Nat Genet 2007; 39:1512-6.
    • (2007) Nat Genet , vol.39 , pp. 1512-1516
    • Zeitlinger, J.1    Stark, A.2    Kellis, M.3    Hong, J.W.4    Nechaev, S.5    Adelman, K.6
  • 8
    • 0034667949 scopus 로고    scopus 로고
    • High-resolution localization of Drosophila Spt5 and Spt6 at heat shock genes in vivo: Roles in promoter proximal pausing and transcription elongation
    • Andrulis ED, Guzman E, Doring P, Werner J, Lis JT. High-resolution localization of Drosophila Spt5 and Spt6 at heat shock genes in vivo: roles in promoter proximal pausing and transcription elongation. Genes Dev 2000; 14:2635-49.
    • (2000) Genes Dev , vol.14 , pp. 2635-2649
    • Andrulis, E.D.1    Guzman, E.2    Doring, P.3    Werner, J.4    Lis, J.T.5
  • 9
    • 67649648237 scopus 로고    scopus 로고
    • Control of inducible gene expression by signal-dependent transcriptional elongation
    • Hargreaves DC, Horng T, Medzhitov R. Control of inducible gene expression by signal-dependent transcriptional elongation. Cell 2009; 138:129-45.
    • (2009) Cell , vol.138 , pp. 129-145
    • Hargreaves, D.C.1    Horng, T.2    Medzhitov, R.3
  • 11
    • 70449641057 scopus 로고    scopus 로고
    • Progression through the RNA polymerase II CTD cycle
    • Buratowski S. Progression through the RNA polymerase II CTD cycle. Mol Cell 2009; 36:541-6.
    • (2009) Mol Cell , vol.36 , pp. 541-546
    • Buratowski, S.1
  • 12
    • 0032534814 scopus 로고    scopus 로고
    • Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro
    • DOI 10.1093/emboj/17.24.7395
    • Wada T, Takagi T, Yamaguchi Y, Watanabe D, Handa H. Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro. EMBO J 1998; 17:7395-403. (Pubitemid 29002707)
    • (1998) EMBO Journal , vol.17 , Issue.24 , pp. 7395-7403
    • Wada, T.1    Takagi, T.2    Yamaguchi, Y.3    Watanabe, D.4    Handa, H.5
  • 13
    • 30744449491 scopus 로고    scopus 로고
    • P-TEFb-mediated phosphorylation of hSpt5 C-terminal repeats is critical for processive transcription elongation
    • DOI 10.1016/j.molcel.2005.11.024, PII S1097276505018125
    • Yamada T, Yamaguchi Y, Inukai N, Okamoto S, Mura T, Handa H. P-TEFb-mediated phosphorylation of hSpt5 C-terminal repeats is critical for processive transcription elongation. Mol Cell 2006; 21:227-37. (Pubitemid 43099938)
    • (2006) Molecular Cell , vol.21 , Issue.2 , pp. 227-237
    • Yamada, T.1    Yamaguchi, Y.2    Inukai, N.3    Okamoto, S.4    Mura, T.5    Handa, H.6
  • 15
    • 15144348173 scopus 로고    scopus 로고
    • Transcription elongation factor P-TEFb is required for HIV-1 tat transactivation in vitro
    • Zhu Y, Pe'ery T, Peng J, Ramanathan Y, Marshall N, Marshall T, et al. Transcription elongation factor P-TEFb is required for HIV-1 tat transactivation in vitro. Genes Dev 1997; 11:2622-32.
    • (1997) Genes Dev , vol.11 , pp. 2622-2632
    • Zhu, Y.1    Pe'ery, T.2    Peng, J.3    Ramanathan, Y.4    Marshall, N.5    Marshall, T.6
  • 16
    • 0032548918 scopus 로고    scopus 로고
    • A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
    • DOI 10.1016/S0092-8674(00)80939-3
    • Wei P, Garber ME, Fang SM, Fischer WH, Jones KA. A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell 1998; 92:451-62. (Pubitemid 28101109)
    • (1998) Cell , vol.92 , Issue.4 , pp. 451-462
    • Wei, P.1    Garber, M.E.2    Fang, S.-M.3    Fischer, W.H.4    Jones, K.A.5
  • 17
    • 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. Insights into the function of the human P-TEFb component CDK9 in the regulation of chromatin modifications and co-transcriptional mRNA processing. Cell Cycle 2009; 8:3636-42.
    • (2009) Cell Cycle , vol.8 , pp. 3636-3642
    • Pirngruber, J.1    Shchebet, A.2    Johnsen, S.A.3
  • 18
    • 33847070442 scopus 로고    scopus 로고
    • The role of chromatin during transcription
    • Li B, Carey M, Workman JL. The role of chromatin during transcription. Cell 2007; 128:707-19.
    • (2007) Cell , vol.128 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 19
    • 1042289789 scopus 로고    scopus 로고
    • Phosphorylated Positive Transcription Elongation Factor b (P-TEFb) Is Tagged for Inhibition through Association with 7SK snRNA
    • DOI 10.1074/jbc.M310044200
    • Chen R, Yang Z, Zhou Q. Phosphorylated positive transcription elongation factor b (P-TEFb) is tagged for inhibition through association with 7SK snRNA. J Biol Chem 2004; 279:4153-60. (Pubitemid 38199000)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.6 , pp. 4153-4160
    • Chen, R.1    Yang, Z.2    Zhou, Q.3
  • 20
    • 70149112313 scopus 로고    scopus 로고
    • Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation
    • Zippo A, Serafini R, Rocchigiani M, Pennacchini S, Krepelova A, Oliviero S. Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation. Cell 2009; 138:1122-36.
    • (2009) Cell , vol.138 , pp. 1122-1136
    • Zippo, A.1    Serafini, R.2    Rocchigiani, M.3    Pennacchini, S.4    Krepelova, A.5    Oliviero, S.6
  • 21
    • 0034111019 scopus 로고    scopus 로고
    • P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II
    • Price DH. P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II. Mol Cell Biol 2000; 20:2629-34.
    • (2000) Mol Cell Biol , vol.20 , pp. 2629-2634
    • Price, D.H.1
  • 22
    • 0032031706 scopus 로고    scopus 로고
    • Identification of multiple cyclin subunits of human P-TEFb
    • Peng J, Zhu Y, Milton JT, Price DH. Identification of multiple cyclin subunits of human P-TEFb. Genes Dev 1998; 12:755-62.
    • (1998) Genes Dev , vol.12 , pp. 755-762
    • Peng, J.1    Zhu, Y.2    Milton, J.T.3    Price, D.H.4
  • 24
    • 0032533253 scopus 로고    scopus 로고
    • The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein
    • Garber ME, Wei P, KewalRamani VN, Mayall TP, Herrmann CH, Rice AP, et al. The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein. Genes Dev 1998; 12:3512-27.
    • (1998) Genes Dev , vol.12 , pp. 3512-3527
    • Garber, M.E.1    Wei, P.2    KewalRamani, V.N.3    Mayall, T.P.4    Herrmann, C.H.5    Rice, A.P.6
  • 28
    • 23744514308 scopus 로고    scopus 로고
    • The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription
    • DOI 10.1016/j.molcel.2005.06.027, PII S1097276505014322
    • Jang MK, Mochizuki K, Zhou M, Jeong HS, Brady JN, Ozato K. The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription. Mol Cell 2005; 19:523-34. (Pubitemid 41140009)
    • (2005) Molecular Cell , vol.19 , Issue.4 , pp. 523-534
    • Moon, K.J.1    Mochizuki, K.2    Zhou, M.3    Jeong, H.-S.4    Brady, J.N.5    Ozato, K.6
  • 29
    • 0036133174 scopus 로고    scopus 로고
    • Interaction between P-TEFb and the C-terminal domain of RNA polymerase II activates transcriptional elongation from sites upstream or downstream of target genes
    • DOI 10.1128/MCB.22.1.321-331.2002
    • Taube R, Lin X, Irwin D, Fujinaga K, Peterlin BM. Interaction between P-TEFb and the C-terminal domain of RNA polymerase II activates transcriptional elongation from sites upstream or downstream of target genes. Mol Cell Biol 2002; 22:321-31. (Pubitemid 33144278)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.1 , pp. 321-331
    • Taube, R.1    Lin, X.2    Irwin, D.3    Fujinaga, K.4    Peterlin, B.M.5
  • 31
    • 46949093191 scopus 로고    scopus 로고
    • The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation
    • Baumli S, Lolli G, Lowe ED, Troiani S, Rusconi L, Bullock AN, et al. The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation. EMBO J 2008; 27:1907-18.
    • (2008) EMBO J , vol.27 , pp. 1907-1918
    • Baumli, S.1    Lolli, G.2    Lowe, E.D.3    Troiani, S.4    Rusconi, L.5    Bullock, A.N.6
  • 32
    • 0033574614 scopus 로고    scopus 로고
    • Mechanisms of cyclin-dependent kinase regulation: Structures of Cdks, their cyclin activators, and Cip and INK4 inhibitors
    • Pavletich NP. Mechanisms of cyclin-dependent kinase regulation: structures of Cdks, their cyclin activators, and Cip and INK4 inhibitors. J Mol Biol 1999; 287:821-8.
    • (1999) J Mol Biol , vol.287 , pp. 821-828
    • Pavletich, N.P.1
  • 33
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan DO. Principles of CDK regulation. Nature 1995; 374:131-4.
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 34
    • 0037468903 scopus 로고    scopus 로고
    • Identification of a novel isoform of Cdk9
    • Shore SM, Byers SA, Maury W, Price DH. Identification of a novel isoform of Cdk9. Gene 2003; 307:175-82.
    • (2003) Gene , vol.307 , pp. 175-182
    • Shore, S.M.1    Byers, S.A.2    Maury, W.3    Price, D.H.4
  • 35
    • 17044433094 scopus 로고    scopus 로고
    • Characterization of Cdk9(55) and differential regulation of two Cdk9 isoforms
    • Shore SM, Byers SA, Dent P, Price DH. Characterization of Cdk9(55) and differential regulation of two Cdk9 isoforms. Gene 2005; 350:51-8.
    • (2005) Gene , vol.350 , pp. 51-58
    • Shore, S.M.1    Byers, S.A.2    Dent, P.3    Price, D.H.4
  • 36
    • 0035022568 scopus 로고    scopus 로고
    • The Cdk9 and cyclin T subunits of TAK/P-TEFb localize to splicing factor-rich nuclear speckle regions
    • Herrmann CH, Mancini MA. The Cdk9 and cyclin T subunits of TAK/P-TEFb localize to splicing factor-rich nuclear speckle regions. J Cell Sci 2001; 114:1491-503.
    • (2001) J Cell Sci , vol.114 , pp. 1491-1503
    • Herrmann, C.H.1    Mancini, M.A.2
  • 37
    • 0035891288 scopus 로고    scopus 로고
    • 7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes
    • Nguyen VT, Kiss T, Michels AA, Bensaude O. 7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes. Nature 2001; 414:322-5.
    • (2001) Nature , vol.414 , pp. 322-325
    • Nguyen, V.T.1    Kiss, T.2    Michels, A.A.3    Bensaude, O.4
  • 38
    • 0242361319 scopus 로고    scopus 로고
    • Inhibition of P-TEFb (CDK9/Cyclin T) kinase and RNA polymerase II transcription by the coordinated actions of HEXIM1 and 7SK snRNA
    • Yik JH, Chen R, Nishimura R, Jennings JL, Link AJ, Zhou Q. Inhibition of P-TEFb (CDK9/Cyclin T) kinase and RNA polymerase II transcription by the coordinated actions of HEXIM1 and 7SK snRNA. Mol Cell 2003; 12:971-82.
    • (2003) Mol Cell , vol.12 , pp. 971-982
    • Yik, J.H.1    Chen, R.2    Nishimura, R.3    Jennings, J.L.4    Link, A.J.5    Zhou, Q.6
  • 39
    • 0035891271 scopus 로고    scopus 로고
    • The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription
    • Yang Z, Zhu Q, Luo K, Zhou Q. The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription. Nature 2001; 414:317-22.
    • (2001) Nature , vol.414 , pp. 317-322
    • Yang, Z.1    Zhu, Q.2    Luo, K.3    Zhou, Q.4
  • 40
    • 30644478471 scopus 로고    scopus 로고
    • Regulation of polymerase II transcription by 7SK snRNA: Two distinct RNA elements direct P-TEFb and HEXIM1 binding
    • DOI 10.1128/MCB.26.2.630-642.2006
    • Egloff S, Van Herreweghe E, Kiss T. Regulation of polymerase II transcription by 7SK snRNA: two distinct RNA elements direct P-TEFb and HEXIM1 binding. Mol Cell Biol 2006; 26:630-42. (Pubitemid 43089774)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.2 , pp. 630-642
    • Egloff, S.1    Van Herreweghe, E.2    Kiss, T.3
  • 41
    • 31944446145 scopus 로고    scopus 로고
    • Increased HEXIM1 expression during erythroleukemia and neuroblastoma cell differentiation
    • DOI 10.1002/jcp.20502
    • Turano M, Napolitano G, Dulac C, Majello B, Bensaude O, Lania L. Increased HEXIM1 expression during erythroleukemia and neuroblastoma cell differentiation. J Cell Physiol 2006; 206:603-10. (Pubitemid 43191034)
    • (2006) Journal of Cellular Physiology , vol.206 , Issue.3 , pp. 603-610
    • Turano, M.1    Napolitano, G.2    Dulac, C.3    Majello, B.4    Bensaude, O.5    Lania, L.6
  • 42
    • 33749169192 scopus 로고    scopus 로고
    • Modulation of a P-TEFb functional equilibrium for the global control of cell growth and differentiation
    • DOI 10.1128/MCB.00778-06
    • He N, Pezda AC, Zhou Q. Modulation of a P-TEFb functional equilibrium for the global control of cell growth and differentiation. Mol Cell Biol 2006; 26:7068-76. (Pubitemid 44477686)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.19 , pp. 7068-7076
    • He, N.1    Pezda, A.C.2    Zhou, Q.3
  • 43
    • 51649089956 scopus 로고    scopus 로고
    • RNA-driven cyclin-dependent kinase regulation: When CDK9/cyclin T subunits of P-TEFb meet their ribonucleoprotein partners
    • Michels AA, Bensaude O. RNA-driven cyclin-dependent kinase regulation: when CDK9/cyclin T subunits of P-TEFb meet their ribonucleoprotein partners. Biotechnol J 2008; 3:1022-32.
    • (2008) Biotechnol J , vol.3 , pp. 1022-1032
    • Michels, A.A.1    Bensaude, O.2
  • 44
    • 29244474416 scopus 로고    scopus 로고
    • Interplay between 7SK snRNA and oppositely charged regions in HEXIM1 direct the inhibition of P-TEFb
    • Barboric M, Kohoutek J, Price JP, Blazek D, Price DH, Peterlin BM. Interplay between 7SK snRNA and oppositely charged regions in HEXIM1 direct the inhibition of P-TEFb. EMBO J 2005; 24:4291-303.
    • (2005) EMBO J , vol.24 , pp. 4291-4303
    • Barboric, M.1    Kohoutek, J.2    Price, J.P.3    Blazek, D.4    Price, D.H.5    Peterlin, B.M.6
  • 45
    • 29244459405 scopus 로고    scopus 로고
    • Oligomerization of HEXIM1 via 7SK snRNA and coiled-coil region directs the inhibition of P-TEFb
    • Blazek D, Barboric M, Kohoutek J, Oven I, Peterlin BM. Oligomerization of HEXIM1 via 7SK snRNA and coiled-coil region directs the inhibition of P-TEFb. Nucleic Acids Res 2005; 33:7000-10.
    • (2005) Nucleic Acids Res , vol.33 , pp. 7000-7010
    • Blazek, D.1    Barboric, M.2    Kohoutek, J.3    Oven, I.4    Peterlin, B.M.5
  • 46
    • 23344437022 scopus 로고    scopus 로고
    • Analysis of the large inactive P-TEFb complex indicates that it contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb molecules containing Cdk9 phosphorylated at threonine 186
    • Li Q, Price JP, Byers SA, Cheng D, Peng J, Price DH. Analysis of the large inactive P-TEFb complex indicates that it contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb molecules containing Cdk9 phosphorylated at threonine 186. J Biol Chem 2005; 280:28819-26.
    • (2005) J Biol Chem , vol.280 , pp. 28819-28826
    • Li, Q.1    Price, J.P.2    Byers, S.A.3    Cheng, D.4    Peng, J.5    Price, D.H.6
  • 49
    • 56749096290 scopus 로고    scopus 로고
    • Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4
    • Lin YJ, Umehara T, Inoue M, Saito K, Kigawa T, Jang MK, et al. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4. Protein Sci 2008; 17:2174-9.
    • (2008) Protein Sci , vol.17 , pp. 2174-2179
    • Lin, Y.J.1    Umehara, T.2    Inoue, M.3    Saito, K.4    Kigawa, T.5    Jang, M.K.6
  • 50
    • 34250357662 scopus 로고    scopus 로고
    • The double bromodomain-containing chromatin adaptor Brd4 and transcriptional regulation
    • Wu SY, Chiang CM. The double bromodomain-containing chromatin adaptor Brd4 and transcriptional regulation. J Biol Chem 2007; 282:13141-5.
    • (2007) J Biol Chem , vol.282 , pp. 13141-13145
    • Wu, S.Y.1    Chiang, C.M.2
  • 52
    • 23744467035 scopus 로고    scopus 로고
    • Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4
    • DOI 10.1016/j.molcel.2005.06.029, PII S1097276505014310
    • Yang Z, Yik JH, Chen R, He N, Jang MK, Ozato K, Zhou Q. Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4. Mol Cell 2005; 19:535-45. (Pubitemid 41140010)
    • (2005) Molecular Cell , vol.19 , Issue.4 , pp. 535-545
    • Yang, Z.1    Yik, J.H.N.2    Chen, R.3    He, N.4    Moon, K.J.5    Ozato, K.6    Zhou, Q.7
  • 53
    • 42049095157 scopus 로고    scopus 로고
    • The bromodomain protein Brd4 stimulates G1 gene transcription and promotes progression to S phase
    • Mochizuki K, Nishiyama A, Jang MK, Dey A, Ghosh A, Tamura T, et al. The bromodomain protein Brd4 stimulates G1 gene transcription and promotes progression to S phase. J Biol Chem 2008; 283:9040-8.
    • (2008) J Biol Chem , vol.283 , pp. 9040-9048
    • Mochizuki, K.1    Nishiyama, A.2    Jang, M.K.3    Dey, A.4    Ghosh, A.5    Tamura, T.6
  • 54
    • 38549113034 scopus 로고    scopus 로고
    • 1 gene expression and cell cycle progression
    • 1 gene expression and cell cycle progression. Mol Cell Biol 2008; 28:967-76.
    • (2008) Mol Cell Biol , vol.28 , pp. 967-976
    • Yang, Z.1    He, N.2    Zhou, Q.3
  • 56
    • 73949087197 scopus 로고    scopus 로고
    • Brd4 Marks Select Genes on Mitotic Chromatin and Directs Post-mitotic Transcription
    • Dey A, Nishiyama A, Karpova T, McNally J, Ozato K. Brd4 Marks Select Genes on Mitotic Chromatin and Directs Post-mitotic Transcription. Mol Biol Cell 2009.
    • (2009) Mol Biol Cell
    • Dey, A.1    Nishiyama, A.2    Karpova, T.3    McNally, J.4    Ozato, K.5
  • 57
    • 73649124584 scopus 로고    scopus 로고
    • Structures of the dual bromodomains of the P-TEFb activating protein Brd4 at atomic resolution
    • Vollmuth F, Blankenfeldt W, Geyer M. Structures of the dual bromodomains of the P-TEFb activating protein Brd4 at atomic resolution. J Biol Chem 2009.
    • (2009) J Biol Chem
    • Vollmuth, F.1    Blankenfeldt, W.2    Geyer, M.3
  • 58
    • 0032127436 scopus 로고    scopus 로고
    • Transcription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stages
    • Zhou Q, Chen D, Pierstorff E, Luo K. Transcription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stages. EMBO J 1998; 17:3681-91.
    • (1998) EMBO J , vol.17 , pp. 3681-3691
    • Zhou, Q.1    Chen, D.2    Pierstorff, E.3    Luo, K.4
  • 59
    • 0033817555 scopus 로고    scopus 로고
    • CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA
    • Garber ME, Mayall TP, Suess EM, Meisenhelder J, Thompson NE, Jones KA. CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA. Mol Cell Biol 2000; 20:6958-69.
    • (2000) Mol Cell Biol , vol.20 , pp. 6958-6969
    • Garber, M.E.1    Mayall, T.P.2    Suess, E.M.3    Meisenhelder, J.4    Thompson, N.E.5    Jones, K.A.6
  • 60
    • 36048945927 scopus 로고    scopus 로고
    • HMBA releases P-TEFb from HEXIM1 and 7SK snRNA via PI3K/Akt and activates HIV transcription
    • Contreras X, Barboric M, Lenasi T, Peterlin BM. HMBA releases P-TEFb from HEXIM1 and 7SK snRNA via PI3K/Akt and activates HIV transcription. PLoS Pathog 2007; 3:1459-69.
    • (2007) PLoS Pathog , vol.3 , pp. 1459-1469
    • Contreras, X.1    Barboric, M.2    Lenasi, T.3    Peterlin, B.M.4
  • 61
    • 44149117974 scopus 로고    scopus 로고
    • PP2B and PP1alpha cooperatively disrupt 7SK snRNP to release P-TEFb for transcription in response to Ca2+ signaling
    • Chen R, Liu M, Li H, Xue Y, Ramey WN, He N, et al. PP2B and PP1alpha cooperatively disrupt 7SK snRNP to release P-TEFb for transcription in response to Ca2+ signaling. Genes Dev 2008; 22:1356-68.
    • (2008) Genes Dev , vol.22 , pp. 1356-1368
    • Chen, R.1    Liu, M.2    Li, H.3    Xue, Y.4    Ramey, W.N.5    He, N.6
  • 62
    • 33646463585 scopus 로고    scopus 로고
    • Tax interacts with P-TEFb in a novel manner to stimulate human T-lymphotropic virus type 1 transcription
    • Zhou M, Lu H, Park H, Wilson-Chiru J, Linton R, Brady JN. Tax interacts with P-TEFb in a novel manner to stimulate human T-lymphotropic virus type 1 transcription. J Virol 2006; 80:4781-91.
    • (2006) J Virol , vol.80 , pp. 4781-4791
    • Zhou, M.1    Lu, H.2    Park, H.3    Wilson-Chiru, J.4    Linton, R.5    Brady, J.N.6
  • 63
    • 0032751695 scopus 로고    scopus 로고
    • Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases
    • Cheng A, Ross KE, Kaldis P, Solomon MJ. Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases. Genes Dev 1999; 13:2946-57.
    • (1999) Genes Dev , vol.13 , pp. 2946-2957
    • Cheng, A.1    Ross, K.E.2    Kaldis, P.3    Solomon, M.J.4
  • 64
    • 0034602268 scopus 로고    scopus 로고
    • Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2Calpha and beta2 isoforms
    • Cheng A, Kaldis P, Solomon MJ. Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2Calpha and beta2 isoforms. J Biol Chem 2000; 275:34744-9.
    • (2000) J Biol Chem , vol.275 , pp. 34744-34749
    • Cheng, A.1    Kaldis, P.2    Solomon, M.J.3
  • 66
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • DOI 10.1038/nsb0896-696
    • Russo AA, Jeffrey PD, Pavletich NP. Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat Struct Biol 1996; 3:696-700. (Pubitemid 26260060)
    • (1996) Nature Structural Biology , vol.3 , Issue.8 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 67
    • 57749098792 scopus 로고    scopus 로고
    • Phosphatase PPM1A regulates phosphorylation of Thr-186 in the Cdk9 T-loop
    • Wang Y, Dow EC, Liang YY, Ramakrishnan R, Liu H, Sung TL, et al. Phosphatase PPM1A regulates phosphorylation of Thr-186 in the Cdk9 T-loop. J Biol Chem 2008; 283:33578-84.
    • (2008) J Biol Chem , vol.283 , pp. 33578-33584
    • Wang, Y.1    Dow, E.C.2    Liang, Y.Y.3    Ramakrishnan, R.4    Liu, H.5    Sung, T.L.6
  • 68
    • 0031016629 scopus 로고    scopus 로고
    • Dual phosphorylation of the T-loop in cdk7: Its role in controlling cyclin H binding and CAK activity
    • DOI 10.1093/emboj/16.2.343
    • Martinez AM, Afshar M, Martin F, Cavadore JC, Labbe JC, Doree M. Dual phosphorylation of the T-loop in cdk7: its role in controlling cyclin H binding and CAK activity. EMBO J 1997; 16:343-54. (Pubitemid 27049391)
    • (1997) EMBO Journal , vol.16 , Issue.2 , pp. 343-354
    • Martinez, A.-M.1    Afshar, M.2    Martin, F.3    Cavadore, J.-C.4    Labbe, J.-C.5    Doree, M.6
  • 70
    • 0035976987 scopus 로고    scopus 로고
    • TFIIH inhibits CDK9 phosphorylation during human immunodeficiency virus type 1 transcription
    • Zhou M, Nekhai S, Bharucha DC, Kumar A, Ge H, Price DH, et al. TFIIH inhibits CDK9 phosphorylation during human immunodeficiency virus type 1 transcription. J Biol Chem 2001; 276:44633-40.
    • (2001) J Biol Chem , vol.276 , pp. 44633-44640
    • Zhou, M.1    Nekhai, S.2    Bharucha, D.C.3    Kumar, A.4    Ge, H.5    Price, D.H.6
  • 71
    • 0033867973 scopus 로고    scopus 로고
    • Relief of two built-In autoinhibitory mechanisms in P-TEFb is required for assembly of a multicomponent transcription elongation complex at the human immunodeficiency virus type 1 promoter
    • Fong YW, Zhou Q. Relief of two built-In autoinhibitory mechanisms in P-TEFb is required for assembly of a multicomponent transcription elongation complex at the human immunodeficiency virus type 1 promoter. Mol Cell Biol 2000; 20:5897-907.
    • (2000) Mol Cell Biol , vol.20 , pp. 5897-5907
    • Fong, Y.W.1    Zhou, Q.2
  • 72
    • 0026713875 scopus 로고
    • Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15
    • Gu Y, Rosenblatt J, Morgan DO. Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15. EMBO J 1992; 11:3995-4005.
    • (1992) EMBO J , vol.11 , pp. 3995-4005
    • Gu, Y.1    Rosenblatt, J.2    Morgan, D.O.3
  • 73
    • 0026027660 scopus 로고
    • 2/M transitions of the cell cycle: Identification of major phosphorylation sites
    • 2/M transitions of the cell cycle: identification of major phosphorylation sites. EMBO J 1991; 10:305-16.
    • (1991) EMBO J , vol.10 , pp. 305-316
    • Krek, W.1    Nigg, E.A.2
  • 74
    • 58149487612 scopus 로고    scopus 로고
    • Bromodomain protein Brd4 regulates human immunodeficiency virus transcription through phosphorylation of CDK9 at threonine 29
    • Zhou M, Huang K, Jung KJ, Cho WK, Klase Z, Kashanchi F, et al. Bromodomain protein Brd4 regulates human immunodeficiency virus transcription through phosphorylation of CDK9 at threonine 29. J Virol 2009; 83:1036-44.
    • (2009) J Virol , vol.83 , pp. 1036-1044
    • Zhou, M.1    Huang, K.2    Jung, K.J.3    Cho, W.K.4    Klase, Z.5    Kashanchi, F.6
  • 75
    • 0035167511 scopus 로고    scopus 로고
    • Interaction between cyclin T1 and SCF(SKP2) targets CDK9 for ubiquitination and degradation by the proteasome
    • Kiernan RE, Emiliani S, Nakayama K, Castro A, Labbe JC, Lorca T, et al. Interaction between cyclin T1 and SCF(SKP2) targets CDK9 for ubiquitination and degradation by the proteasome. Mol Cell Biol 2001; 21:7956-70.
    • (2001) Mol Cell Biol , vol.21 , pp. 7956-7970
    • Kiernan, R.E.1    Emiliani, S.2    Nakayama, K.3    Castro, A.4    Labbe, J.C.5    Lorca, T.6
  • 76
    • 23844509792 scopus 로고    scopus 로고
    • Ubiquitylation of Cdk9 by Skp2 facilitates optimal Tat transactivation
    • Barboric M, Zhang F, Besenicar M, Plemenitas A, Peterlin BM. Ubiquitylation of Cdk9 by Skp2 facilitates optimal Tat transactivation. J Virol 2005; 79:11135-41.
    • (2005) J Virol , vol.79 , pp. 11135-11141
    • Barboric, M.1    Zhang, F.2    Besenicar, M.3    Plemenitas, A.4    Peterlin, B.M.5
  • 77
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers S, Wells R, Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 1986; 234:364-8.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 78
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M, Rogers SW. PEST sequences and regulation by proteolysis. Trends Biochem Sci 1996; 21:267-71.
    • (1996) Trends Biochem Sci , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 80
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 2009; 325:834-40.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6
  • 81
    • 67349221027 scopus 로고    scopus 로고
    • Acetylation of cyclin T1 regulates the equilibrium between active and inactive P-TEFb in cells
    • Cho S, Schroeder S, Kaehlcke K, Kwon HS, Pedal A, Herker E, et al. Acetylation of cyclin T1 regulates the equilibrium between active and inactive P-TEFb in cells. EMBO J 2009; 28:1407-17.
    • (2009) EMBO J , vol.28 , pp. 1407-1417
    • Cho, S.1    Schroeder, S.2    Kaehlcke, K.3    Kwon, H.S.4    Pedal, A.5    Herker, E.6
  • 84
    • 34347346076 scopus 로고    scopus 로고
    • Regulation of P-TEFb elongation complex activity by CDK9 acetylation
    • Fu J, Yoon HG, Qin J, Wong J. Regulation of P-TEFb elongation complex activity by CDK9 acetylation. Mol Cell Biol 2007; 27:4641-51.
    • (2007) Mol Cell Biol , vol.27 , pp. 4641-4651
    • Fu, J.1    Yoon, H.G.2    Qin, J.3    Wong, J.4
  • 85
    • 41149145576 scopus 로고    scopus 로고
    • Acetylation of conserved lysines in the catalytic core of cyclindependent kinase 9 inhibits kinase activity and regulates transcription
    • Sabo A, Lusic M, Cereseto A, Giacca M. Acetylation of conserved lysines in the catalytic core of cyclindependent kinase 9 inhibits kinase activity and regulates transcription. Mol Cell Biol 2008; 28:2201-12.
    • (2008) Mol Cell Biol , vol.28 , pp. 2201-2212
    • Sabo, A.1    Lusic, M.2    Cereseto, A.3    Giacca, M.4
  • 86
    • 0020446736 scopus 로고
    • Coiled-coils in alpha-helix-containing proteins: Analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins
    • Parry DA. Coiled-coils in alpha-helix-containing proteins: analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins. Biosci Rep 1982; 2:1017-24.
    • (1982) Biosci Rep , vol.2 , pp. 1017-1024
    • Parry, D.A.1
  • 87
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, Van Dyke M, Stock J. Predicting coiled coils from protein sequences. Science 1991; 252:1162-4.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 88
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled-coil structures
    • Lupas A. Prediction and analysis of coiled-coil structures. Methods Enzymol 1996; 266:513-25.
    • (1996) Methods Enzymol , vol.266 , pp. 513-525
    • Lupas, A.1


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