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Volumn 6, Issue 4, 2011, Pages

Protein phosphatase-1 activates CDK9 by dephosphorylating ser175

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE 7; CYCLIN DEPENDENT KINASE 9; FLAVOPIRIDOL; OKADAIC ACID; PHOSPHOPEPTIDE; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOPROTEIN PHOSPHATASE 2A; RNA POLYMERASE II; SERINE; THREONINE; CDK9 PROTEIN, HUMAN;

EID: 79955382495     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0018985     Document Type: Article
Times cited : (38)

References (41)
  • 1
    • 34848881569 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional regulation of HIV-1 gene expression: role of cellular factors for Tat and Rev
    • Nekhai S, Jeang KT, (2006) Transcriptional and post-transcriptional regulation of HIV-1 gene expression: role of cellular factors for Tat and Rev. Future Microbiol 1: 417-426.
    • (2006) Future Microbiol , vol.1 , pp. 417-426
    • Nekhai, S.1    Jeang, K.T.2
  • 2
    • 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
  • 3
    • 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
  • 4
    • 0038111978 scopus 로고    scopus 로고
    • MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a transcription-dependent manner
    • Michels AA, Nguyen VT, Fraldi A, Labas V, Edwards M, et al. (2003) MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a transcription-dependent manner. Mol Cell Biol 23: 4859-4869.
    • (2003) Mol Cell Biol , vol.23 , pp. 4859-4869
    • Michels, A.A.1    Nguyen, V.T.2    Fraldi, A.3    Labas, V.4    Edwards, M.5
  • 5
    • 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, et al. (2003) Inhibition of P-TEFb (CDK9/Cyclin T) kinase and RNA polymerase II transcription by the coordinated actions of HEXIM1 and 7SK snRNA. Mol Cell 12: 971-982.
    • (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
  • 6
    • 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
  • 7
    • 44649135099 scopus 로고    scopus 로고
    • The La-related protein LARP7 is a component of the 7SK ribonucleoprotein and affects transcription of cellular and viral polymerase II genes
    • Markert A, Grimm M, Martinez J, Wiesner J, Meyerhans A, et al. (2008) The La-related protein LARP7 is a component of the 7SK ribonucleoprotein and affects transcription of cellular and viral polymerase II genes. EMBO Rep 9: 569-575.
    • (2008) EMBO Rep , vol.9 , pp. 569-575
    • Markert, A.1    Grimm, M.2    Martinez, J.3    Wiesner, J.4    Meyerhans, A.5
  • 8
    • 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
  • 9
    • 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
  • 10
    • 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, Chua G, 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: 262-274.
    • (2007) Mol Cell , vol.27 , pp. 262-274
    • Jeronimo, C.1    Forget, D.2    Bouchard, A.3    Li, Q.4    Chua, G.5
  • 11
    • 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, et al. (2005) 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 280: 28819-28826.
    • (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
  • 12
    • 1042289789 scopus 로고    scopus 로고
    • Phosphorylated positive transcription elongation factor b (P-TEFb) is tagged for inhibition through association with 7SK snRNA
    • Chen R, Yang Z, Zhou Q, (2004) Phosphorylated positive transcription elongation factor b (P-TEFb) is tagged for inhibition through association with 7SK snRNA. J Biol Chem 279: 4153-4160.
    • (2004) J Biol Chem , vol.279 , pp. 4153-4160
    • Chen, R.1    Yang, Z.2    Zhou, Q.3
  • 13
    • 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, et al. (2006) Tax interacts with P-TEFb in a novel manner to stimulate human T-lymphotropic virus type 1 transcription. J Virol 80: 4781-4791.
    • (2006) J Virol , vol.80 , pp. 4781-4791
    • Zhou, M.1    Lu, H.2    Park, H.3    Wilson-Chiru, J.4    Linton, R.5
  • 14
    • 34250641183 scopus 로고    scopus 로고
    • Regulation of two key nuclear enzymatic activities by the 7SK small nuclear RNA
    • He WJ, Chen R, Yang Z, Zhou Q, (2006) Regulation of two key nuclear enzymatic activities by the 7SK small nuclear RNA. Cold Spring Harb Symp Quant Biol 71: 301-311.
    • (2006) Cold Spring Harb Symp Quant Biol , vol.71 , pp. 301-311
    • He, W.J.1    Chen, R.2    Yang, Z.3    Zhou, Q.4
  • 15
    • 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, et al. (2000) CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA. Mol Cell Biol 20: 6958-6969.
    • (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
  • 16
    • 0035853736 scopus 로고    scopus 로고
    • Positive transcription elongation factor B phosphorylates hSPT5 and RNA polymerase II carboxyl-terminal domain independently of cyclin-dependent kinase-activating kinase
    • Kim JB, Sharp PA, (2001) Positive transcription elongation factor B phosphorylates hSPT5 and RNA polymerase II carboxyl-terminal domain independently of cyclin-dependent kinase-activating kinase. J Biol Chem 276: 12317-12323.
    • (2001) J Biol Chem , vol.276 , pp. 12317-12323
    • Kim, J.B.1    Sharp, P.A.2
  • 17
    • 27344456057 scopus 로고    scopus 로고
    • Dephosphorylation of CDK9 by protein phosphatase 2A and protein phosphatase-1 in Tat-activated HIV-1 transcription
    • Ammosova T, Washington K, Debebe Z, Brady J, Nekhai S, (2005) Dephosphorylation of CDK9 by protein phosphatase 2A and protein phosphatase-1 in Tat-activated HIV-1 transcription. Retrovirology 2: 47.
    • (2005) Retrovirology , vol.2 , pp. 47
    • Ammosova, T.1    Washington, K.2    Debebe, Z.3    Brady, J.4    Nekhai, S.5
  • 19
    • 27744597059 scopus 로고    scopus 로고
    • Nuclear targeting of protein phosphatase-1 by HIV-1 Tat protein
    • Ammosova T, Jerebtsova M, Beullens M, Lesage B, Jackson A, et al. (2005) Nuclear targeting of protein phosphatase-1 by HIV-1 Tat protein. J Biol Chem 280: 36364-36371.
    • (2005) J Biol Chem , vol.280 , pp. 36364-36371
    • Ammosova, T.1    Jerebtsova, M.2    Beullens, M.3    Lesage, B.4    Jackson, A.5
  • 20
    • 79952782278 scopus 로고    scopus 로고
    • Expression of a Protein Phosphatase 1 Inhibitor, cdNIPP1, Increases CDK9 Threonine 186 Phosphorylation and Inhibits HIV-1 Transcription
    • Ammosova T, Yedavalli VR, Niu X, Jerebtsova M, Van Eynde A, et al. (2011) Expression of a Protein Phosphatase 1 Inhibitor, cdNIPP1, Increases CDK9 Threonine 186 Phosphorylation and Inhibits HIV-1 Transcription. J Biol Chem 286: 3798-3804.
    • (2011) J Biol Chem , vol.286 , pp. 3798-3804
    • Ammosova, T.1    Yedavalli, V.R.2    Niu, X.3    Jerebtsova, M.4    Van Eynde, A.5
  • 21
    • 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
  • 22
    • 0037174844 scopus 로고    scopus 로고
    • Protein phosphatase-1 dephosphorylates the C-terminal domain of RNA polymerase-II
    • Washington K, Ammosova T, Beullens M, Jerebtsova M, Kumar A, et al. (2002) Protein phosphatase-1 dephosphorylates the C-terminal domain of RNA polymerase-II. J Biol Chem 277: 40442-40448.
    • (2002) J Biol Chem , vol.277 , pp. 40442-40448
    • Washington, K.1    Ammosova, T.2    Beullens, M.3    Jerebtsova, M.4    Kumar, A.5
  • 23
    • 0034672212 scopus 로고    scopus 로고
    • The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1) contains a novel binding site for protein phosphatase-1 that is controlled by tyrosine phosphorylation and RNA binding
    • Beullens M, Vulsteke V, Van Eynde A, Jagiello I, Stalmans W, et al. (2000) The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1) contains a novel binding site for protein phosphatase-1 that is controlled by tyrosine phosphorylation and RNA binding. Biochem J 352: 651-658.
    • (2000) Biochem J , vol.352 , pp. 651-658
    • Beullens, M.1    Vulsteke, V.2    Van Eynde, A.3    Jagiello, I.4    Stalmans, W.5
  • 24
    • 0027471557 scopus 로고
    • Cdc25M2 activation of cyclin-dependent kinases by dephosphorylation of threonine-14 and tyrosine-15
    • Sebastian B, Kakizuka A, Hunter T, (1993) Cdc25M2 activation of cyclin-dependent kinases by dephosphorylation of threonine-14 and tyrosine-15. Proc Natl Acad Sci U S A 90: 3521-3524.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3521-3524
    • Sebastian, B.1    Kakizuka, A.2    Hunter, T.3
  • 25
    • 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
  • 26
    • 0031016629 scopus 로고    scopus 로고
    • Dual phosphorylation of the T-loop in cdk7: its role in controlling cyclin H binding and CAK activity
    • Martinez AM, Afshar M, Martin F, Cavadore JC, Labbe JC, et al. (1997) Dual phosphorylation of the T-loop in cdk7: its role in controlling cyclin H binding and CAK activity. Embo J 16: 343-354.
    • (1997) Embo J , vol.16 , pp. 343-354
    • Martinez, A.M.1    Afshar, M.2    Martin, F.3    Cavadore, J.C.4    Labbe, J.C.5
  • 28
    • 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, et al. (2005) 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) J Biol Chem
    • Li, Q.1    Price, J.P.2    Byers, S.A.3    Cheng, D.4    Peng, J.5
  • 29
    • 0026713875 scopus 로고
    • Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15
    • Gu Y, Rosenblatt J, Morgan DO, (1992) Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15. Embo J 11: 3995-4005.
    • (1992) Embo J , vol.11 , pp. 3995-4005
    • Gu, Y.1    Rosenblatt, J.2    Morgan, D.O.3
  • 30
    • 23744467035 scopus 로고    scopus 로고
    • Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4
    • Yang Z, Yik JH, Chen R, He N, Jang MK, et al. (2005) Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4. Mol Cell 19: 535-545.
    • (2005) Mol Cell , vol.19 , pp. 535-545
    • Yang, Z.1    Yik, J.H.2    Chen, R.3    He, N.4    Jang, M.K.5
  • 31
    • 23744514308 scopus 로고    scopus 로고
    • The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription
    • Jang MK, Mochizuki K, Zhou M, Jeong HS, Brady JN, et al. (2005) The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription. Mol Cell 19: 523-534.
    • (2005) Mol Cell , vol.19 , pp. 523-534
    • Jang, M.K.1    Mochizuki, K.2    Zhou, M.3    Jeong, H.S.4    Brady, J.N.5
  • 32
    • 34547126444 scopus 로고    scopus 로고
    • Regulation of transcript elongation through cooperative and ordered recruitment of cofactors
    • Sharma M, George AA, Singh BN, Sahoo NC, Rao KV, (2007) Regulation of transcript elongation through cooperative and ordered recruitment of cofactors. J Biol Chem 282: 20887-20896.
    • (2007) J Biol Chem , vol.282 , pp. 20887-20896
    • Sharma, M.1    George, A.A.2    Singh, B.N.3    Sahoo, N.C.4    Rao, K.V.5
  • 33
  • 34
    • 26244436628 scopus 로고    scopus 로고
    • RNA interference directed to CDK2 inhibits HIV-1 transcription
    • Ammosova T, Berro R, Kashanchi F, Nekhai S, (2005) RNA interference directed to CDK2 inhibits HIV-1 transcription. Virology 341: 171-178.
    • (2005) Virology , vol.341 , pp. 171-178
    • Ammosova, T.1    Berro, R.2    Kashanchi, F.3    Nekhai, S.4
  • 35
    • 35148823552 scopus 로고    scopus 로고
    • Modulation of the Brd4/P-TEFb interaction by the human T-lymphotropic virus type 1 tax protein
    • Cho WK, Zhou M, Jang MK, Huang K, Jeong SJ, et al. (2007) Modulation of the Brd4/P-TEFb interaction by the human T-lymphotropic virus type 1 tax protein. J Virol 81: 11179-11186.
    • (2007) J Virol , vol.81 , pp. 11179-11186
    • Cho, W.K.1    Zhou, M.2    Jang, M.K.3    Huang, K.4    Jeong, S.J.5
  • 36
    • 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, et al. (1997) Transcription elongation factor P-TEFb is required for HIV-1 tat transactivation in vitro. Genes Dev 11: 2622-2632.
    • (1997) Genes Dev , vol.11 , pp. 2622-2632
    • Zhu, Y.1    Pe'ery, T.2    Peng, J.3    Ramanathan, Y.4    Marshall, N.5
  • 37
    • 0030780092 scopus 로고    scopus 로고
    • TAK, an HIV Tat-associated kinase, is a member of the cyclin-dependent family of protein kinases and is induced by activation of peripheral blood lymphocytes and differentiation of promonocytic cell lines
    • Yang X, Gold MO, Tang DN, Lewis DE, Aguilar-Cordova E, et al. (1997) TAK, an HIV Tat-associated kinase, is a member of the cyclin-dependent family of protein kinases and is induced by activation of peripheral blood lymphocytes and differentiation of promonocytic cell lines. Proc Natl Acad Sci U S A 94: 12331-12336.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12331-12336
    • Yang, X.1    Gold, M.O.2    Tang, D.N.3    Lewis, D.E.4    Aguilar-Cordova, E.5
  • 38
    • 0023780669 scopus 로고
    • Preparation of low-molecular-weight forms of rabbit muscle protein phosphatase
    • DeGuzman A, Lee EY, (1988) Preparation of low-molecular-weight forms of rabbit muscle protein phosphatase. Methods Enzymol 159: 356-368.
    • (1988) Methods Enzymol , vol.159 , pp. 356-368
    • DeGuzman, A.1    Lee, E.Y.2
  • 39
    • 0032031706 scopus 로고    scopus 로고
    • Identification of multiple cyclin subunits of human P-TEFb
    • Peng J, Zhu Y, Milton JT, Price DH, (1998) Identification of multiple cyclin subunits of human P-TEFb. Genes Dev 12: 755-762.
    • (1998) Genes Dev , vol.12 , pp. 755-762
    • Peng, J.1    Zhu, Y.2    Milton, J.T.3    Price, D.H.4
  • 40
    • 0026552386 scopus 로고
    • DNA binding provides a signal for phosphorylation of the RNA polymerase II heptapeptide repeats
    • Peterson SR, Dvir A, Anderson CW, Dynan WS, (1992) DNA binding provides a signal for phosphorylation of the RNA polymerase II heptapeptide repeats. Genes Dev 6: 426-438.
    • (1992) Genes Dev , vol.6 , pp. 426-438
    • Peterson, S.R.1    Dvir, A.2    Anderson, C.W.3    Dynan, W.S.4
  • 41
    • 0034688295 scopus 로고    scopus 로고
    • Cell cycle-dependent stimulation of the HIV-1 promoter by Tat-associated CAK activator
    • Nekhai S, Shukla RR, Fernandez A, Kumar A, Lamb NJ, (2000) Cell cycle-dependent stimulation of the HIV-1 promoter by Tat-associated CAK activator. Virology 266: 246-256.
    • (2000) Virology , vol.266 , pp. 246-256
    • Nekhai, S.1    Shukla, R.R.2    Fernandez, A.3    Kumar, A.4    Lamb, N.J.5


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