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Volumn 5, Issue 6, 2010, Pages

Caffeine prevents transcription inhibition and P-TEFb/ 7SK dissociation following UV-induced DNA damage

Author keywords

[No Author keywords available]

Indexed keywords

ATM PROTEIN; ATR PROTEIN; CAFFEINE; DNA DEPENDENT PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; POSITIVE TRANSCRIPTION ELONGATION FACTOR B; RNA POLYMERASE II; SMALL NUCLEAR RIBONUCLEOPROTEIN; DNA DIRECTED DNA POLYMERASE ALPHA;

EID: 77955285489     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0011245     Document Type: Article
Times cited : (11)

References (36)
  • 1
    • 0034641753 scopus 로고    scopus 로고
    • UV-induced inhibition of transcription involves repression of transcription initiation and phosphorylation of RNA polymerase II
    • Rockx DA, Mason R, vanHoffen A, Barton MC, Citterio E, et al. (2000) UV-induced inhibition of transcription involves repression of transcription initiation and phosphorylation of RNA polymerase II. Proc Natl Acad Sci U S A 97: 10503-10508.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10503-10508
    • Rockx, D.A.1    Mason, R.2    Vanhoffen, A.3    Barton, M.C.4    Citterio, E.5
  • 2
    • 0141916811 scopus 로고    scopus 로고
    • Cell cycle arrest and apoptosis provoked by UV radiation-induced DNA damage are transcriptionally highly divergent responses
    • Gentile M, Latonen L, Laiho M (2003) Cell cycle arrest and apoptosis provoked by UV radiation-induced DNA damage are transcriptionally highly divergent responses. Nucleic Acids Res 31: 4779-4790.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4779-4790
    • Gentile, M.1    Latonen, L.2    Laiho, M.3
  • 3
    • 33646589650 scopus 로고    scopus 로고
    • Cockayne syndrome B protein regulates the transcriptional program after UV irradiation
    • Proietti-De-Santis L, Drane P, Egly JM (2006) Cockayne syndrome B protein regulates the transcriptional program after UV irradiation. Embo J 25: 1915-1923.
    • (2006) Embo J , vol.25 , pp. 1915-1923
    • Proietti-De-Santis, L.1    Drane, P.2    Egly, J.M.3
  • 4
    • 0035807072 scopus 로고    scopus 로고
    • Ultraviolet radiation alters the phosphorylation of RNA polymerase II large subunit and accelerates its proteasome-dependent degradation
    • Luo Z, Zheng J, Lu Y, Bregman DB (2001) Ultraviolet radiation alters the phosphorylation of RNA polymerase II large subunit and accelerates its proteasome-dependent degradation. Mutat Res 486: 259-274.
    • (2001) Mutat Res , vol.486 , pp. 259-274
    • Luo, Z.1    Zheng, J.2    Lu, Y.3    Bregman, D.B.4
  • 5
    • 20444428382 scopus 로고    scopus 로고
    • Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest
    • Somesh BP, Reid J, Liu WF, Sogaard TM, et al. (2005) Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest. Cell 121: 913-923.
    • (2005) Cell , vol.121 , pp. 913-923
    • Somesh, B.P.1    Reid, J.2    Liu, W.F.3    Sogaard, T.M.4
  • 6
    • 33751090746 scopus 로고    scopus 로고
    • Phosphorylation and functions of the RNA polymerase II CTD
    • Phatnani HP, Greenleaf AL (2006) Phosphorylation and functions of the RNA polymerase II CTD. Genes Dev 20: 2922-2936.
    • (2006) Genes Dev , vol.20 , pp. 2922-2936
    • Phatnani, H.P.1    Greenleaf, A.L.2
  • 7
    • 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.
    • (2006) Mol Cell , vol.23 , pp. 297-305
    • Peterlin, B.M.1    Price, D.H.2
  • 8
    • 71049193792 scopus 로고    scopus 로고
    • P-TEFb- the final frontier
    • Kohoutek J (2009) P-TEFb- the final frontier. Cell Div 4: 19.
    • (2009) Cell Div , vol.4 , pp. 19
    • Kohoutek, J.1
  • 10
    • 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 (2008) RNA-driven cyclin-dependent kinase regulation: when CDK9/cyclin T subunits of P-TEFb meet their ribonucleoprotein partners. Biotechnol J 3: 1022-1032.
    • (2008) Biotechnol J , vol.3 , pp. 1022-1032
    • Michels, A.A.1    Bensaude, O.2
  • 11
    • 68249128223 scopus 로고    scopus 로고
    • CDK9 directs H2B monoubiquitination and controls replication-dependent histone mRNA 39-end processing
    • Pirngruber J, Shchebet A, Schreiber L, Shema E, Minsky N, et al. (2009) CDK9 directs H2B monoubiquitination and controls replication-dependent histone mRNA 39-end processing. EMBO Rep 10: 894-900.
    • (2009) EMBO Rep , vol.10 , pp. 894-900
    • Pirngruber, J.1    Shchebet, A.2    Schreiber, L.3    Shema, E.4    Minsky, N.5
  • 12
    • 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 (2001) The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription. Nature 414: 317-322.
    • (2001) Nature , vol.414 , pp. 317-322
    • Yang, Z.1    Zhu, Q.2    Luo, K.3    Zhou, Q.4
  • 13
    • 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 (2001) 7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes. Nature 414: 322-325.
    • (2001) Nature , vol.414 , pp. 322-325
    • Nguyen, V.T.1    Kiss, T.2    Michels, A.A.3    Bensaude, O.4
  • 14
    • 3342967685 scopus 로고    scopus 로고
    • Binding of the 7SK snRNA turns the HEXIM1 protein into a P-TEFb (CDK9/cyclin T) inhibitor
    • Michels AA, Fraldi A, Li Q, Adamson TE, Bonnet F, et al. (2004) Binding of the 7SK snRNA turns the HEXIM1 protein into a P-TEFb (CDK9/cyclin T) inhibitor. Embo J 23: 2608-2619.
    • (2004) Embo J , vol.23 , pp. 2608-2619
    • Michels, A.A.1    Fraldi, A.2    Li, Q.3    Adamson, T.E.4    Bonnet, F.5
  • 15
    • 34447321025 scopus 로고    scopus 로고
    • Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme
    • Jeronimo C, Forget D, Bouchard A, Li Q, et al. (2007) Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme. Mol Cell 27: 262-74.
    • (2007) Mol Cell , vol.27 , pp. 262-274
    • Jeronimo, C.1    Forget, D.2    Bouchard, A.3    Li, Q.4
  • 16
    • 42449086866 scopus 로고    scopus 로고
    • LARP7 is a stable component of the 7SK snRNP while P-TEFb, HEXIM1 and hnRNP A1 are reversibly associated
    • Krueger BJ, Jeronimo C, Roy BB, Bouchard A, Barrandon C, et al. (2008) LARP7 is a stable component of the 7SK snRNP while P-TEFb, HEXIM1 and hnRNP A1 are reversibly associated. Nucleic Acids Res 36: 2219-2229.
    • (2008) Nucleic Acids Res , vol.36 , pp. 2219-2229
    • Krueger, B.J.1    Jeronimo, C.2    Roy, B.B.3    Bouchard, A.4    Barrandon, C.5
  • 17
    • 40649100262 scopus 로고    scopus 로고
    • A La-related protein modulates 7SK snRNP integrity to suppress P-TEFb-dependent transcriptional elongation and tumorigenesis
    • He N, Jahchan NS, Hong E, Li Q, Bayfield MA, et al. (2008) A La-related protein modulates 7SK snRNP integrity to suppress P-TEFb-dependent transcriptional elongation and tumorigenesis. Mol Cell 29: 588-599.
    • (2008) Mol Cell , vol.29 , pp. 588-599
    • He, N.1    Jahchan, N.S.2    Hong, E.3    Li, Q.4    Bayfield, M.A.5
  • 18
    • 65949092198 scopus 로고    scopus 로고
    • Camptothecin releases P-TEFb from the inactive 7SK snRNP complex
    • Amente S, Gargano B, Napolitano G, Lania L, Majello B (2009) Camptothecin releases P-TEFb from the inactive 7SK snRNP complex. Cell Cycle 8: 1249-1255.
    • (2009) Cell Cycle , vol.8 , pp. 1249-1255
    • Amente, S.1    Gargano, B.2    Napolitano, G.3    Lania, L.4    Majello, B.5
  • 19
    • 34548016988 scopus 로고    scopus 로고
    • Inhibition of HIV-1 replication by P-TEFb inhibitors DRB, seliciclib and flavopiridol correlates with release of free P-TEFb from the large, inactive form of the complex
    • Biglione S, Byers SA, Price JP, Nguyen VT, et al. (2007) Inhibition of HIV-1 replication by P-TEFb inhibitors DRB, seliciclib and flavopiridol correlates with release of free P-TEFb from the large, inactive form of the complex. Retrovirology 2007: 4: 47.
    • (2007) Retrovirology , vol.2007 , Issue.4 , pp. 47
    • Biglione, S.1    Byers, S.A.2    Price, J.P.3    Nguyen, V.T.4
  • 20
    • 34249900227 scopus 로고    scopus 로고
    • Pivotal role of cardiac lineage protein-1 (CLP-1) in transcriptional elongation factor P-TEFb complex formation in cardiac hypertrophy
    • Espinoza-Derout J, Wagner M, Shahmiri K, Mascareno E, Chaqour B, et al. (2007) Pivotal role of cardiac lineage protein-1 (CLP-1) in transcriptional elongation factor P-TEFb complex formation in cardiac hypertrophy. Cardiovasc Res 75: 129-138.
    • (2007) Cardiovasc Res , vol.75 , pp. 129-138
    • Espinoza-Derout, J.1    Wagner, M.2    Shahmiri, K.3    Mascareno, E.4    Chaqour, B.5
  • 21
    • 36048945927 scopus 로고    scopus 로고
    • HMBA releases PTEFb from HEXIM1 and 7SK snRNA via PI3K/Akt and activates HIV transcription
    • Contreras X, Barboric M, Lenasi T, Peterlin BM (2007) HMBA releases PTEFb from HEXIM1 and 7SK snRNA via PI3K/Akt and activates HIV transcription. PLoS Pathog 3: 1459-1469.
    • (2007) PLoS Pathog , vol.3 , pp. 1459-1469
    • Contreras, X.1    Barboric, M.2    Lenasi, T.3    Peterlin, B.M.4
  • 22
    • 38649118240 scopus 로고    scopus 로고
    • Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced transcriptional repression
    • Shimada M, Niida H, Zineldeen DH, Tagami H, Tanaka M, et al. (2008) Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced transcriptional repression. Cell 132: 221-232.
    • (2008) Cell , vol.132 , pp. 221-232
    • Shimada, M.1    Niida, H.2    Zineldeen, D.H.3    Tagami, H.4    Tanaka, M.5
  • 23
    • 29144494151 scopus 로고    scopus 로고
    • The cell cycle: A new entry in the field of Ca2+ signaling
    • Santella L, Ercolano E, Nusco GA (2005) The cell cycle: a new entry in the field of Ca2+ signaling. Cell Mol Life Sci 62: 2405-2413.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2405-2413
    • Santella, L.1    Ercolano, E.2    Nusco, G.A.3
  • 24
    • 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, et al. (2008) PP2B and PP1alpha cooperatively disrupt 7SK snRNP to release P-TEFb for transcription in response to Ca2+ signaling. Genes Dev 22: 1356-1368.
    • (2008) Genes Dev , vol.22 , pp. 1356-1368
    • Chen, R.1    Liu, M.2    Li, H.3    Xue, Y.4    Ramey, W.N.5
  • 25
    • 65549147264 scopus 로고    scopus 로고
    • DNA damage regulates alternative splicing through inhibition of RNA polymerase II elongation
    • Munoz MJ, Perez Santangelo MS, Paronetto MP, de la Mata M, Pelisch F, et al. (2009) DNA damage regulates alternative splicing through inhibition of RNA polymerase II elongation. Cell 137: 708-720.
    • (2009) Cell , vol.137 , pp. 708-720
    • Munoz, M.J.1    Perez Santangelo, M.S.2    Paronetto, M.P.3    de la Mata, M.4    Pelisch, F.5
  • 26
    • 33749169192 scopus 로고    scopus 로고
    • Modulation of a P-TEFb functional equilibrium for the global control of cell growth and differentiation
    • He N, Pezda AC, Zhou Q (2006) Modulation of a P-TEFb functional equilibrium for the global control of cell growth and differentiation. Mol Cell Biol 26: 7068-7076.
    • (2006) Mol Cell Biol , vol.26 , pp. 7068-7076
    • He, N.1    Pezda, A.C.2    Zhou, Q.3
  • 27
    • 34248187995 scopus 로고    scopus 로고
    • Activation of P-TEFb induces p21 leading to cell cycle arrest
    • Napolitano G, Varrone F, Majello B, Lania L (2007) Activation of P-TEFb induces p21 leading to cell cycle arrest. Cell Cycle 6: 1126-1129.
    • (2007) Cell Cycle , vol.6 , pp. 1126-1129
    • Napolitano, G.1    Varrone, F.2    Majello, B.3    Lania, L.4
  • 28
    • 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, et al. (2008) Phosphatase PPM1A regulates phosphorylation of Thr-186 in the Cdk9 T-loop. J Biol Chem 283: 33578-33584.
    • (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
  • 29
    • 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, et al. (2008) The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation. Embo J 27: 1907-1918.
    • (2008) Embo J , vol.27 , pp. 1907-1918
    • Baumli, S.1    Lolli, G.2    Lowe, E.D.3    Troiani, S.4    Rusconi, L.5
  • 30
    • 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, et al. (2009) Acetylation of cyclin T1 regulates the equilibrium between active and inactive P-TEFb in cells. Embo J 28: 1407-1417.
    • (2009) Embo J , vol.28 , pp. 1407-1417
    • Cho, S.1    Schroeder, S.2    Kaehlcke, K.3    Kwon, H.S.4    Pedal, A.5
  • 31
    • 34547821418 scopus 로고    scopus 로고
    • Dynamic remodelling of human 7SK snRNP controls the nuclear level of active P-TEFb
    • Van Herreweghe E, Egloff S, Goiffon I, Jady BE, Froment C, et al. (2007) Dynamic remodelling of human 7SK snRNP controls the nuclear level of active P-TEFb. Embo J 26: 3570-3580.
    • (2007) Embo J , vol.26 , pp. 3570-3580
    • van Herreweghe, E.1    Egloff, S.2    Goiffon, I.3    Jady, B.E.4    Froment, C.5
  • 32
    • 35148867404 scopus 로고    scopus 로고
    • The transcription-dependent dissociation of P-TEFb-HEXIM1-7SK RNA relies upon formation of hnRNP-7SK RNA complexes
    • Barrandon C, Bonnet F, Nguyen VT, Labas V, Bensaude O (2007) The transcription-dependent dissociation of P-TEFb-HEXIM1-7SK RNA relies upon formation of hnRNP-7SK RNA complexes. Mol Cell Biol 27: 6996-7006.
    • (2007) Mol Cell Biol , vol.27 , pp. 6996-7006
    • Barrandon, C.1    Bonnet, F.2    Nguyen, V.T.3    Labas, V.4    Bensaude, O.5
  • 33
    • 67650409769 scopus 로고    scopus 로고
    • Screen for DNA-damage-responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells
    • Tjeertes JV, Miller KM, Jackson SP (2009) Screen for DNA-damage-responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells. Embo J 28: 1878-1889.
    • (2009) Embo J , vol.28 , pp. 1878-1889
    • Tjeertes, J.V.1    Miller, K.M.2    Jackson, S.P.3
  • 34
    • 66049098191 scopus 로고    scopus 로고
    • 7SK snRNP/ P-TEFb couples transcription elongation with alternative splicing and is essential for vertebrate development
    • Barboric M, Lenasi T, Chen H, Johansen EB, Guo S, et al. (2009) 7SK snRNP/ P-TEFb couples transcription elongation with alternative splicing and is essential for vertebrate development. Proc Natl Acad Sci U S A 106: 7798-7803.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7798-7803
    • Barboric, M.1    Lenasi, T.2    Chen, H.3    Johansen, E.B.4    Guo, S.5
  • 35
    • 33646076438 scopus 로고    scopus 로고
    • Stepwise RNP assembly at the site of H/ACA RNA transcription in human cells
    • Darzacq X, Kittur N, Roy S, Shav-Tal Y, Singer RH, et al. (2006) Stepwise RNP assembly at the site of H/ACA RNA transcription in human cells. J Cell Biol 173: 207-218.
    • (2006) J Cell Biol , vol.173 , pp. 207-218
    • Darzacq, X.1    Kittur, N.2    Roy, S.3    Shav-Tal, Y.4    Singer, R.H.5
  • 36
    • 34548232360 scopus 로고    scopus 로고
    • P-TEFb is a crucial co-factor for Myc transactivation
    • Gargano B, Amente S, Majello B, Lania L (2007) P-TEFb is a crucial co-factor for Myc transactivation. Cell Cycle 6: 2031-2037.
    • (2007) Cell Cycle , vol.6 , pp. 2031-2037
    • Gargano, B.1    Amente, S.2    Majello, B.3    Lania, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.