메뉴 건너뛰기




Volumn 2014, Issue , 2014, Pages

Protein kinase D3 is essential for prostratin-activated transcription of integrated HIV-1 provirus promoter via NF-κB signaling pathway

Author keywords

[No Author keywords available]

Indexed keywords

ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PHORBOL ESTER DERIVATIVE; PROSTRATIN; PROTEIN KINASE D; PROTEIN KINASE D3; UNCLASSIFIED DRUG; BISINDOLYLMALEIMIDE; INDOLE DERIVATIVE; MALEIMIDE DERIVATIVE; PHORBOL ESTER; PROTEIN KINASE C; PROTEIN KINASE C EPSILON; PROTEIN KINASE C NU;

EID: 84929051778     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2014/968027     Document Type: Article
Times cited : (5)

References (40)
  • 1
    • 33747162419 scopus 로고    scopus 로고
    • The regulation of HIV-1 transcription: Molecular targets for chemotherapeutic intervention
    • M. Stevens, E. de Clercq, and J. Balzarini, "The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention, " Medicinal Research Reviews, vol. 26, no. 5, pp. 595-625, 2006.
    • (2006) Medicinal Research Reviews , vol.26 , Issue.5 , pp. 595-625
    • Stevens, M.1    De Clercq, E.2    Balzarini, J.3
  • 2
    • 32944464685 scopus 로고    scopus 로고
    • Scientific rationale for antiretroviral therapy in 2005: Viral reservoirs and resistance evolution
    • R. F. Siliciano, "Scientific rationale for antiretroviral therapy in 2005: viral reservoirs and resistance evolution, " Topics in HIV Medicine, vol. 13, no. 3, pp. 96-100, 2005.
    • (2005) Topics in HIV Medicine , vol.13 , Issue.3 , pp. 96-100
    • Siliciano, R.F.1
  • 3
    • 84866753757 scopus 로고    scopus 로고
    • Human immunodeficiency virus (HIV) latency: The major hurdle in HIV eradication
    • M. Tyagi and M. Bukrinsky, "Human immunodeficiency virus (HIV) latency: the major hurdle in HIV eradication, "Molecular Medicine, vol. 18, no. 7, pp. 1096-1098, 2012.
    • (2012) Molecular Medicine , vol.18 , Issue.7 , pp. 1096-1098
    • Tyagi, M.1    Bukrinsky, M.2
  • 4
    • 84878981012 scopus 로고    scopus 로고
    • Barriers to a cure for HIV: New ways to target and eradicate HIV-1 reservoirs
    • C. Katlama, S. G. Deeks, B. Autran, et al., "Barriers to a cure for HIV: new ways to target and eradicate HIV-1 reservoirs, " The Lancet, vol. 381, no. 9883, pp. 2109-2117, 2013.
    • (2013) The Lancet , vol.381 , Issue.9883 , pp. 2109-2117
    • Katlama, C.1    Deeks, S.G.2    Autran, B.3
  • 5
    • 84885075354 scopus 로고    scopus 로고
    • Therapeutics for HIV-1 reactivation from latency
    • M. Sgarbanti and A. Battistini, "Therapeutics for HIV-1 reactivation from latency, " Current Opinion in Virology, vol. 3, no. 4, pp. 394-401, 2013.
    • (2013) Current Opinion in Virology , vol.3 , Issue.4 , pp. 394-401
    • Sgarbanti, M.1    Battistini, A.2
  • 6
    • 0035892120 scopus 로고    scopus 로고
    • Prostratin: Activation of latent HIV-1 expression suggests a potential inductive adjuvant therapy for HAART
    • J. Kulkosky, D. M. Culnan, J. Roman, et al., "Prostratin: activation of latent HIV-1 expression suggests a potential inductive adjuvant therapy for HAART, " Blood, vol. 98, no. 10, pp. 3006-3015, 2001.
    • (2001) Blood , vol.98 , Issue.10 , pp. 3006-3015
    • Kulkosky, J.1    Culnan, D.M.2    Roman, J.3
  • 7
    • 0036315848 scopus 로고    scopus 로고
    • Effects of prostratin on T-cell activation and human immunodeficiency virus latency
    • Y. D. Korin, D. G. Brooks, S. Brown, A. Korotzer, and J. A. Zack, "Effects of prostratin on T-cell activation and human immunodeficiency virus latency, " Journal ofVirology, vol. 76, no. 16, pp. 8118-8123, 2002.
    • (2002) Journal OfVirology , vol.76 , Issue.16 , pp. 8118-8123
    • Korin, Y.D.1    Brooks, D.G.2    Brown, S.3    Korotzer, A.4    Zack, J.A.5
  • 8
    • 79551652566 scopus 로고    scopus 로고
    • Activation of latent HIV-1 expression by protein kinase C agonists. A novel therapeutic approach to eradicate HIV 1 reservoirs
    • G. Sánchez-Duffhues, M. Q. Vo, O. Pérez, et al., "Activation of latent HIV-1 expression by protein kinase C agonists. a novel therapeutic approach to eradicate HIV 1 reservoirs, " Current Drug Targets, vol. 12, no. 3, pp. 348-356, 2011.
    • (2011) Current Drug Targets , vol.12 , Issue.3 , pp. 348-356
    • Sánchez-Duffhues, G.1    Vo, M.Q.2    Pérez, O.3
  • 10
    • 4744359117 scopus 로고    scopus 로고
    • Prostratin antagonizes HIV latency by activating NF-κB
    • S. A. Williams, L.-F. Chen, H. Kwon, et al., "Prostratin antagonizes HIV latency by activating NF-κB, " Journal of Biological Chemistry, vol. 279, no. 40, pp. 42008-42017, 2004.
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.40 , pp. 42008-42017
    • Williams, S.A.1    Chen, L.-F.2    Kwon, H.3
  • 12
    • 0037592334 scopus 로고    scopus 로고
    • Protein kinase Cv/protein kinase D3 nuclear localization, catalytic activation, and intracellular redistribution in response to G proteincoupled receptor agonists
    • O. Rey, J. Yuan, S. H. Young, and E. Rozengurt, "Protein kinase Cv/protein kinase D3 nuclear localization, catalytic activation, and intracellular redistribution in response to G proteincoupled receptor agonists, " Journal of Biological Chemistry, vol. 278, no. 26, pp. 23773-23785, 2003.
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23773-23785
    • Rey, O.1    Yuan, J.2    Young, S.H.3    Rozengurt, E.4
  • 13
    • 0029964752 scopus 로고    scopus 로고
    • Protein kinase D (PKD) activation in intact cells through a protein kinase C-dependent signal transduction pathway
    • J. L. Zugaza, J. Sinnett-Smith, J. van Lint, and E. Rozengurt, "Protein kinase D (PKD) activation in intact cells through a protein kinase C-dependent signal transduction pathway, " The EMBO Journal, vol. 15, no. 22, pp. 6220-6230, 1996.
    • (1996) The EMBO Journal , vol.15 , Issue.22 , pp. 6220-6230
    • Zugaza, J.L.1    Sinnett-Smith, J.2    Van Lint, J.3    Rozengurt, E.4
  • 16
    • 33744926666 scopus 로고    scopus 로고
    • PKD at the crossroads of DAG and PKC signaling
    • Q. J. Wang, "PKD at the crossroads of DAG and PKC signaling, " Trends in Pharmacological Sciences, vol. 27, no. 6, pp. 317-323, 2006.
    • (2006) Trends in Pharmacological Sciences , vol.27 , Issue.6 , pp. 317-323
    • Wang, Q.J.1
  • 17
    • 33645095915 scopus 로고    scopus 로고
    • Activation of protein kinase D3 by signaling through Rac and the subunits of the heterotrimeric G proteins G12 and G13
    • J. Yuan, O. Rey, and E. Rozengurt, "Activation of protein kinase D3 by signaling through Rac and the subunits of the heterotrimeric G proteins G12 and G13, " Cellular Signalling, vol. 18, no. 7, pp. 1051-1062, 2006.
    • (2006) Cellular Signalling , vol.18 , Issue.7 , pp. 1051-1062
    • Yuan, J.1    Rey, O.2    Rozengurt, E.3
  • 19
    • 32044462036 scopus 로고    scopus 로고
    • Essential role for protein kinase D family kinases in the regulation of class II histone deacetylases in B lymphocytes
    • S. A. Matthews, P. Liu, M. Spitaler, et al., "Essential role for protein kinase D family kinases in the regulation of class II histone deacetylases in B lymphocytes, " Molecular and Cellular Biology, vol. 26, no. 4, pp. 1569-1577, 2006.
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.4 , pp. 1569-1577
    • Matthews, S.A.1    Liu, P.2    Spitaler, M.3
  • 20
    • 61749088806 scopus 로고    scopus 로고
    • Brd4 coactivates transcriptional activation of NF-κB via specific binding to acetylated RelA
    • B. Huang, X.-D. Yang, M.-M. Zhou, K. Ozato, and L.-F. Chen, "Brd4 coactivates transcriptional activation of NF-κB via specific binding to acetylated RelA, " Molecular and Cellular Biology, vol. 29, no. 5, pp. 1375-1387, 2009.
    • (2009) Molecular and Cellular Biology , vol.29 , Issue.5 , pp. 1375-1387
    • Huang, B.1    Yang, X.-D.2    Zhou, M.-M.3    Ozato, K.4    Chen, L.-F.5
  • 21
    • 83755220044 scopus 로고    scopus 로고
    • Signal-induced Brd4 release from chromatin is essential for its role transition from chromatin targeting to transcriptional regulation
    • N. Ai, X. Hu, F. Ding, et al., "Signal-induced Brd4 release from chromatin is essential for its role transition from chromatin targeting to transcriptional regulation, " Nucleic Acids Research, vol. 39, no. 22, pp. 9592-9604, 2011.
    • (2011) Nucleic Acids Research , vol.39 , Issue.22 , pp. 9592-9604
    • Ai, N.1    Hu, X.2    Ding, F.3
  • 22
    • 81155162596 scopus 로고    scopus 로고
    • An efficient approach for site-directed mutagenesis using central overlapping primers
    • H. Wang, N. Zhou, F. Ding, et al., "An efficient approach for site-directed mutagenesis using central overlapping primers, " Analytical Biochemistry, vol. 418, no. 2, pp. 304-306, 2011.
    • (2011) Analytical Biochemistry , vol.418 , Issue.2 , pp. 304-306
    • Wang, H.1    Zhou, N.2    Ding, F.3
  • 23
    • 33750295885 scopus 로고    scopus 로고
    • Transfection of mammalian cells using linear polyethylenimine is a simple and effective means of producing recombinant adeno-associated virus vectors
    • S. E. Reed, E. M. Staley, J. P. Mayginnes, D. J. Pintel, and G. E. Tullis, "Transfection of mammalian cells using linear polyethylenimine is a simple and effective means of producing recombinant adeno-associated virus vectors, " Journal of Virological Methods, vol. 138, no. 1-2, pp. 85-98, 2006.
    • (2006) Journal of Virological Methods , vol.138 , Issue.1-2 , pp. 85-98
    • Reed, S.E.1    Staley, E.M.2    Mayginnes, J.P.3    Pintel, D.J.4    Tullis, G.E.5
  • 24
    • 57349090221 scopus 로고    scopus 로고
    • Epigenetic silencing of human immunodeficiency virus (HIV) transcription by formation of restrictive chromatin structures at the viral long terminal repeat drives the progressive entry of HIV into latency
    • R. Pearson, K. K. Young, J. Hokello, et al., "Epigenetic silencing of human immunodeficiency virus (HIV) transcription by formation of restrictive chromatin structures at the viral long terminal repeat drives the progressive entry of HIV into latency, " Journal of Virology, vol. 82, no. 24, pp. 12291-12303, 2008.
    • (2008) Journal of Virology , vol.82 , Issue.24 , pp. 12291-12303
    • Pearson, R.1    Young, K.K.2    Hokello, J.3
  • 25
    • 44149117974 scopus 로고    scopus 로고
    • PP2B and PP1 cooperatively disrupt 7SK snRNP to release P-TEFb for transcription in response to Ca2+ signaling
    • R. Chen, M. Liu, H. Li, et al., "PP2B and PP1 cooperatively disrupt 7SK snRNP to release P-TEFb for transcription in response to Ca2+ signaling, " Genes and Development, vol. 22, no. 10, pp. 1356-1368, 2008.
    • (2008) Genes and Development , vol.22 , Issue.10 , pp. 1356-1368
    • Chen, R.1    Liu, M.2    Li, H.3
  • 26
    • 0035891271 scopus 로고    scopus 로고
    • The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription
    • Z. Yang, Q. Zhu, K. Luo, and Q. Zhou, "The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription, " Nature, vol. 414, no. 6861, pp. 317-322, 2001.
    • (2001) Nature , vol.414 , Issue.6861 , pp. 317-322
    • Yang, Z.1    Zhu, Q.2    Luo, K.3    Zhou, Q.4
  • 28
    • 0037414763 scopus 로고    scopus 로고
    • Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain
    • R. T. Waldron and E. Rozengurt, "Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain, " Journal of Biological Chemistry, vol. 278, no. 1, pp. 154-163, 2003.
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 154-163
    • Waldron, R.T.1    Rozengurt, E.2
  • 29
    • 0030603158 scopus 로고    scopus 로고
    • Inhibition of protein kinase C μ by various inhibitors. Differentiation from protein kinase c isoenzymes
    • M. Gschwendt, S. Dieterich, J. Rennecke, W. Kittstein, H.-J. Mueller, and F.-J. Johannes, "Inhibition of protein kinase C μ by various inhibitors. Differentiation from protein kinase c isoenzymes, " FEBS Letters, vol. 392, no. 2, pp. 77-80, 1996.
    • (1996) FEBS Letters , vol.392 , Issue.2 , pp. 77-80
    • Gschwendt, M.1    Dieterich, S.2    Rennecke, J.3    Kittstein, W.4    Mueller, H.-J.5    Johannes, F.-J.6
  • 30
    • 0027157640 scopus 로고
    • Selective inhibition of protein kinase C isozymes by the indolocarbazole Go 6976
    • G. Martiny-Baron, M. G. Kazanietz, H. Mischak, et al., "Selective inhibition of protein kinase C isozymes by the indolocarbazole Go 6976, " Journal of Biological Chemistry, vol. 268, no. 13, pp. 9194-9197, 1993.
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.13 , pp. 9194-9197
    • Martiny-Baron, G.1    Kazanietz, M.G.2    Mischak, H.3
  • 31
    • 0032104245 scopus 로고    scopus 로고
    • The extended protein kinase C superfamily
    • H. Mellor and P. J. Parker, "The extended protein kinase C superfamily, " Biochemical Journal, vol. 332, part 2, pp. 281-292, 1998.
    • (1998) Biochemical Journal , vol.332 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 32
    • 10844235691 scopus 로고    scopus 로고
    • Protein kinase D2 mediates activation of nuclear factor κb by Bcr-Abl in Bcr-Abl+ humanmyeloid leukemia cells
    • T. Mihailovic, M. Marx, A. Auer, et al., "Protein kinase D2 mediates activation of nuclear factor κB by Bcr-Abl in Bcr-Abl+ humanmyeloid leukemia cells, " Cancer Research, vol. 64, no. 24, pp. 8939-8944, 2004.
    • (2004) Cancer Research , vol.64 , Issue.24 , pp. 8939-8944
    • Mihailovic, T.1    Marx, M.2    Auer, A.3
  • 33
    • 4844224721 scopus 로고    scopus 로고
    • Activation loop phosphorylation controls protein kinase D-dependent activation of nuclear factor κb
    • P. Storz, H. Döppler, and A. Toker, "Activation loop phosphorylation controls protein kinase D-dependent activation of nuclear factor κB, " Molecular Pharmacology, vol. 66, no. 4, pp. 870-879, 2004.
    • (2004) Molecular Pharmacology , vol.66 , Issue.4 , pp. 870-879
    • Storz, P.1    Döppler, H.2    Toker, A.3
  • 34
    • 84872191888 scopus 로고    scopus 로고
    • PKD2 andPKD3promoteprostate cancer cell invasion by modulating NF-κB-and HDAC1-mediated expression and activation of uPA
    • Z. Zou, F. Zeng, W. Xu, et al., "PKD2 andPKD3promoteprostate cancer cell invasion by modulating NF-κB-and HDAC1-mediated expression and activation of uPA, " Journal of Cell Science, vol. 125, part 20, pp. 4800-4811, 2012.
    • (2012) Journal of Cell Science , vol.125 , pp. 4800-4811
    • Zou, Z.1    Zeng, F.2    Xu, W.3
  • 35
    • 0030772376 scopus 로고    scopus 로고
    • Novel inhibitors of cytokine-induced IκB phosphorylation and endothelial cell adhesion molecule expression show anti-inflammatory effects in vivo
    • J. W. Pierce, R. Schoenleber, G. Jesmok, et al., "Novel inhibitors of cytokine-induced IκB phosphorylation and endothelial cell adhesion molecule expression show anti-inflammatory effects in vivo, " Journal of Biological Chemistry, vol. 272, no. 34, pp. 21096-21103, 1997.
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.34 , pp. 21096-21103
    • Pierce, J.W.1    Schoenleber, R.2    Jesmok, G.3
  • 36
    • 33745815978 scopus 로고    scopus 로고
    • Protein kinase D intracellular localization and activity control kinase D-interacting substrate of 220-kDa traffic through a postsynaptic density-95/discs large/zonula occludens-1-binding motif
    • L. Sánchez-Ruiloba, N. Cabrera-Poch, M. Rodríguez-Martínez, et al., "Protein kinase D intracellular localization and activity control kinase D-interacting substrate of 220-kDa traffic through a postsynaptic density-95/discs large/zonula occludens-1-binding motif, " Journal of Biological Chemistry, vol. 281, no. 27, pp. 18888-18900, 2006.
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.27 , pp. 18888-18900
    • Sánchez-Ruiloba, L.1    Cabrera-Poch, N.2    Rodríguez-Martínez, M.3
  • 37
    • 59049087726 scopus 로고    scopus 로고
    • PKD3 is the predominant protein kinase D isoform in mouse exocrine pancreas and promotes hormone-induced amylase secretion
    • L. A. Chen, J. Li, S. R. Silva, et al., "PKD3 is the predominant protein kinase D isoform in mouse exocrine pancreas and promotes hormone-induced amylase secretion, " Journal of Biological Chemistry, vol. 284, no. 4, pp. 2459-2471, 2009.
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.4 , pp. 2459-2471
    • Chen, L.A.1    Li, J.2    Silva, S.R.3
  • 38
    • 33644621946 scopus 로고    scopus 로고
    • The C-terminal tail of protein kinase D2 and protein kinase D3 regulates their intracellular distribution
    • R. Papazyan, E. Rozengurt, and O. Rey, "The C-terminal tail of protein kinase D2 and protein kinase D3 regulates their intracellular distribution, " Biochemical and Biophysical Research Communications, vol. 342, no. 3, pp. 685-689, 2006.
    • (2006) Biochemical and Biophysical Research Communications , vol.342 , Issue.3 , pp. 685-689
    • Papazyan, R.1    Rozengurt, E.2    Rey, O.3
  • 39
    • 33646169213 scopus 로고    scopus 로고
    • The nuclear import of protein kinase D3 requires its catalytic activity
    • O. Rey, R. Papazyan, R. T. Waldron, et al., "The nuclear import of protein kinase D3 requires its catalytic activity, " Journal of Biological Chemistry, vol. 281, no. 8, pp. 5149-5157, 2006.
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.8 , pp. 5149-5157
    • Rey, O.1    Papazyan, R.2    Waldron, R.T.3
  • 40
    • 0037413711 scopus 로고    scopus 로고
    • Protein kinase D mediates a stressinduced NF-κB activation and survival pathway
    • P. Storz and A. Toker, "Protein kinase D mediates a stressinduced NF-κB activation and survival pathway, " The EMBO Journal, vol. 22, no. 1, pp. 109-120, 2003.
    • (2003) The EMBO Journal , vol.22 , Issue.1 , pp. 109-120
    • Storz, P.1    Toker, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.