메뉴 건너뛰기




Volumn 7, Issue , 2010, Pages

A role for the histone deacetylase HDAC4 in the life-cycle of HIV-1-based vectors

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 4; HISTONE DEACETYLASE 6; INTEGRASE; RETROVIRUS VECTOR; SMALL INTERFERING RNA; VIRUS DNA; HDAC2 PROTEIN, HUMAN; HDAC4 PROTEIN, HUMAN; HDAC6 PROTEIN, HUMAN; HISTONE DEACETYLASE; P31 INTEGRASE PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; REPRESSOR PROTEIN;

EID: 77956569249     PISSN: None     EISSN: 1743422X     Source Type: Journal    
DOI: 10.1186/1743-422X-7-237     Document Type: Article
Times cited : (8)

References (35)
  • 1
    • 14844350172 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and cancer: From cell biology to the clinic
    • 10.1016/j.ejcb.2004.12.010. 15819394
    • Histone deacetylase inhibitors and cancer: from cell biology to the clinic. H Hess-Stumpp, Eur J Cell Biol 2005 84 109 121 10.1016/j.ejcb.2004.12. 010 15819394
    • (2005) Eur J Cell Biol , vol.84 , pp. 109-121
    • Hess-Stumpp, H.1
  • 2
    • 0034663486 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human histone deacetylase, HDAC8
    • 10.1042/0264-6021:3500199. 10926844
    • Cloning and characterization of a novel human histone deacetylase, HDAC8. JJ Buggy ML Sideris P Mak DD Lorimer B McIntosh JM Clark, Biochem J 2000 350 Pt 1 199 205 10.1042/0264-6021:3500199 10926844
    • (2000) Biochem J , vol.350 , Issue.PART 1 , pp. 199-205
    • Buggy, J.J.1    Sideris, M.L.2    Mak, P.3    Lorimer, D.D.4    McIntosh, B.5    Clark, J.M.6
  • 3
    • 0032567640 scopus 로고    scopus 로고
    • Differential display cloning of a novel human histone deacetylase (HDAC3) cDNA from PHA-activated immune cells
    • 10.1006/bbrc.1997.8033. 9464271
    • Differential display cloning of a novel human histone deacetylase (HDAC3) cDNA from PHA-activated immune cells. F Dangond DA Hafler JK Tong J Randall R Kojima N Utku SR Gullans, Biochem Biophys Res Commun 1998 242 648 652 10.1006/bbrc.1997.8033 9464271
    • (1998) Biochem Biophys Res Commun , vol.242 , pp. 648-652
    • Dangond, F.1    Hafler, D.A.2    Tong, J.K.3    Randall, J.4    Kojima, R.5    Utku, N.6    Gullans, S.R.7
  • 5
    • 0034685766 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human class i histone deacetylase that functions as a transcription repressor
    • 10.1074/jbc.M908988199. 10748112
    • Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor. E Hu Z Chen T Fredrickson Y Zhu R Kirkpatrick GF Zhang K Johanson CM Sung R Liu J Winkler, J Biol Chem 2000 275 15254 15264 10.1074/jbc.M908988199 10748112
    • (2000) J Biol Chem , vol.275 , pp. 15254-15264
    • Hu, E.1    Chen, Z.2    Fredrickson, T.3    Zhu, Y.4    Kirkpatrick, R.5    Zhang, G.F.6    Johanson, K.7    Sung, C.M.8    Liu, R.9    Winkler, J.10
  • 6
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3
    • 10.1073/pnas.93.23.12845. 8917507
    • Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3. WM Yang C Inouye Y Zeng D Bearss E Seto, Proc Natl Acad Sci USA 1996 93 12845 12850 10.1073/pnas.93.23. 12845 8917507
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12845-12850
    • Yang, W.M.1    Inouye, C.2    Zeng, Y.3    Bearss, D.4    Seto, E.5
  • 7
    • 0033597115 scopus 로고    scopus 로고
    • A new family of human histone deacetylases related to Saccharomyces cerevisiae HDA1p
    • 10.1074/jbc.274.17.11713. 10206986
    • A new family of human histone deacetylases related to Saccharomyces cerevisiae HDA1p. W Fischle S Emiliani MJ Hendzel T Nagase N Nomura W Voelter E Verdin, J Biol Chem 1999 274 11713 11720 10.1074/jbc.274.17.11713 10206986
    • (1999) J Biol Chem , vol.274 , pp. 11713-11720
    • Fischle, W.1    Emiliani, S.2    Hendzel, M.J.3    Nagase, T.4    Nomura, N.5    Voelter, W.6    Verdin, E.7
  • 8
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hda1p
    • 10.1073/pnas.96.9.4868. 10220385
    • Three proteins define a class of human histone deacetylases related to yeast Hda1p. CM Grozinger CA Hassig SL Schreiber, Proc Natl Acad Sci USA 1999 96 4868 4873 10.1073/pnas.96.9.4868 10220385
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 9
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class i and class II deacetylases promote SMRT-mediated repression
    • 10640276
    • Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. HY Kao M Downes P Ordentlich RM Evans, Genes Dev 2000 14 55 66 10640276
    • (2000) Genes Dev , vol.14 , pp. 55-66
    • Kao, H.Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 10
    • 0033568028 scopus 로고    scopus 로고
    • HDAC4 deacetylase associates with and represses the MEF2 transcription factor
    • 10.1093/emboj/18.18.5099. 10487761
    • HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EA Miska C Karlsson E Langley SJ Nielsen J Pines T Kouzarides, EMBO J 1999 18 5099 5107 10.1093/emboj/18.18.5099 10487761
    • (1999) EMBO J , vol.18 , pp. 5099-5107
    • Miska, E.A.1    Karlsson, C.2    Langley, E.3    Nielsen, S.J.4    Pines, J.5    Kouzarides, T.6
  • 11
    • 0029856225 scopus 로고    scopus 로고
    • HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription
    • 10.1073/pnas.93.25.14503. 8962081
    • HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. SE Rundlett AA Carmen R Kobayashi S Bavykin BM Turner M Grunstein, Proc Natl Acad Sci USA 1996 93 14503 14508 10.1073/pnas.93.25.14503 8962081
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14503-14508
    • Rundlett, S.E.1    Carmen, A.A.2    Kobayashi, R.3    Bavykin, S.4    Turner, B.M.5    Grunstein, M.6
  • 13
    • 0037444803 scopus 로고    scopus 로고
    • Histone deacetylases (HDACs): Characterization of the classical HDAC family
    • 10.1042/BJ20021321. 12429021
    • Histone deacetylases (HDACs): characterization of the classical HDAC family. AJ de Ruijter AH van Gennip HN Caron S Kemp AB van Kuilenburg, Biochem J 2003 370 737 749 10.1042/BJ20021321 12429021
    • (2003) Biochem J , vol.370 , pp. 737-749
    • De Ruijter, A.J.1    Van Gennip, A.H.2    Caron, H.N.3    Kemp, S.4    Van Kuilenburg, A.B.5
  • 14
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • 10.1006/bbrc.2000.3000. 10873683
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. RA Frye, Biochem Biophys Res Commun 2000 273 793 798 10.1006/bbrc.2000.3000 10873683
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 16
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • 10.1016/j.jmb.2004.02.006. 15050820
    • Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. IV Gregoretti YM Lee HV Goodson, J Mol Biol 2004 338 17 31 10.1016/j.jmb.2004.02.006 15050820
    • (2004) J Mol Biol , vol.338 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 17
    • 0037417373 scopus 로고    scopus 로고
    • Histone deacetylase 4 interacts with 53BP1 to mediate the DNA damage response
    • 10.1083/jcb.200209065. 12668657
    • Histone deacetylase 4 interacts with 53BP1 to mediate the DNA damage response. GD Kao WG McKenna MG Guenther RJ Muschel MA Lazar TJ Yen, J Cell Biol 2003 160 1017 1027 10.1083/jcb.200209065 12668657
    • (2003) J Cell Biol , vol.160 , pp. 1017-1027
    • Kao, G.D.1    McKenna, W.G.2    Guenther, M.G.3    Muschel, R.J.4    Lazar, M.A.5    Yen, T.J.6
  • 18
    • 33644859838 scopus 로고    scopus 로고
    • DNA damage promotes histone deacetylase 4 nuclear localization and repression of G2/M promoters, via p53 C-terminal lysines
    • 10.1074/jbc.M507712200. 16293626
    • DNA damage promotes histone deacetylase 4 nuclear localization and repression of G2/M promoters, via p53 C-terminal lysines. V Basile R Mantovani C Imbriano, J Biol Chem 2006 281 2347 2357 10.1074/jbc.M507712200 16293626
    • (2006) J Biol Chem , vol.281 , pp. 2347-2357
    • Basile, V.1    Mantovani, R.2    Imbriano, C.3
  • 19
    • 33845741562 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitor LBH589 increases duration of gamma-H2AX foci and confines HDAC4 to the cytoplasm in irradiated non-small cell lung cancer
    • 10.1158/0008-5472.CAN-06-0049. 17145876
    • Histone deacetylase (HDAC) inhibitor LBH589 increases duration of gamma-H2AX foci and confines HDAC4 to the cytoplasm in irradiated non-small cell lung cancer. L Geng KC Cuneo A Fu T Tu PW Atadja DE Hallahan, Cancer Res 2006 66 11298 11304 10.1158/0008-5472.CAN-06-0049 17145876
    • (2006) Cancer Res , vol.66 , pp. 11298-11304
    • Geng, L.1    Cuneo, K.C.2    Fu, A.3    Tu, T.4    Atadja, P.W.5    Hallahan, D.E.6
  • 20
    • 0033597450 scopus 로고    scopus 로고
    • A role for DNA-PK in retroviral DNA integration
    • 10.1126/science.284.5414.644. 10213687
    • A role for DNA-PK in retroviral DNA integration. R Daniel RA Katz AM Skalka, Science 1999 284 644 647 10.1126/science.284.5414.644 10213687
    • (1999) Science , vol.284 , pp. 644-647
    • Daniel, R.1    Katz, R.A.2    Skalka, A.M.3
  • 21
    • 0036385935 scopus 로고    scopus 로고
    • Effect of Ku80 depletion on the preintegrative steps of HIV-1 replication in human cells
    • 10.1006/viro.2002.1515. 12202210
    • Effect of Ku80 depletion on the preintegrative steps of HIV-1 replication in human cells. L Jeanson F Subra S Vaganay M Hervy E Marangoni J Bourhis JF Mouscadet, Virology 2002 300 100 108 10.1006/viro.2002.1515 12202210
    • (2002) Virology , vol.300 , pp. 100-108
    • Jeanson, L.1    Subra, F.2    Vaganay, S.3    Hervy, M.4    Marangoni, E.5    Bourhis, J.6    Mouscadet, J.F.7
  • 22
    • 0035876374 scopus 로고    scopus 로고
    • Role of the non-homologous DNA end joining pathway in the early steps of retroviral infection
    • 10.1093/emboj/20.12.3272. 11406603
    • Role of the non-homologous DNA end joining pathway in the early steps of retroviral infection. L Li JM Olvera KE Yoder RS Mitchell SL Butler M Lieber SL Martin FD Bushman, EMBO J 2001 20 3272 3281 10.1093/emboj/20.12.3272 11406603
    • (2001) EMBO J , vol.20 , pp. 3272-3281
    • Li, L.1    Olvera, J.M.2    Yoder, K.E.3    Mitchell, R.S.4    Butler, S.L.5    Lieber, M.6    Martin, S.L.7    Bushman, F.D.8
  • 23
    • 33947398161 scopus 로고    scopus 로고
    • Following the path of the virus: The exploitation of host DNA repair mechanisms by retroviruses
    • 10.1021/cb600131q. 17163676
    • Following the path of the virus: the exploitation of host DNA repair mechanisms by retroviruses. JA Smith R Daniel, ACS Chem Biol 2006 1 217 226 10.1021/cb600131q 17163676
    • (2006) ACS Chem Biol , vol.1 , pp. 217-226
    • Smith, J.A.1    Daniel, R.2
  • 24
    • 16244383862 scopus 로고    scopus 로고
    • The cellular protein daxx interacts with avian sarcoma virus integrase and viral DNA to repress viral transcription
    • 10.1128/JVI.79.8.4610-4618.2005. 15795247
    • The cellular protein daxx interacts with avian sarcoma virus integrase and viral DNA to repress viral transcription. JG Greger RA Katz AM Ishov GG Maul AM Skalka, J Virol 2005 79 4610 4618 10.1128/JVI.79.8.4610-4618.2005 15795247
    • (2005) J Virol , vol.79 , pp. 4610-4618
    • Greger, J.G.1    Katz, R.A.2    Ishov, A.M.3    Maul, G.G.4    Skalka, A.M.5
  • 26
    • 40349086876 scopus 로고    scopus 로고
    • Evidence that the Nijmegen breakage syndrome protein, an early sensor of double-strand DNA breaks (DSB), is involved in HIV-1 post-integration repair by recruiting the ataxia telangiectasia-mutated kinase in a process similar to, but distinct from, cellular DSB repair
    • 10.1186/1743-422X-5-11. 18211700
    • Evidence that the Nijmegen breakage syndrome protein, an early sensor of double-strand DNA breaks (DSB), is involved in HIV-1 post-integration repair by recruiting the ataxia telangiectasia-mutated kinase in a process similar to, but distinct from, cellular DSB repair. JA Smith FX Wang H Zhang KJ Wu KJ Williams R Daniel, Virol J 2008 5 11 10.1186/1743-422X-5-11 18211700
    • (2008) Virol J , vol.5 , pp. 11
    • Smith, J.A.1    Wang, F.X.2    Zhang, H.3    Wu, K.J.4    Williams, K.J.5    Daniel, R.6
  • 27
    • 0035141303 scopus 로고    scopus 로고
    • Wortmannin potentiates integrase-mediated killing of lymphocytes and reduces the efficiency of stable transduction by retroviruses
    • 10.1128/MCB.21.4.1164-1172.2001. 11158303
    • Wortmannin potentiates integrase-mediated killing of lymphocytes and reduces the efficiency of stable transduction by retroviruses. R Daniel RA Katz G Merkel JC Hittle TJ Yen AM Skalka, Mol Cell Biol 2001 21 1164 1172 10.1128/MCB.21.4.1164-1172.2001 11158303
    • (2001) Mol Cell Biol , vol.21 , pp. 1164-1172
    • Daniel, R.1    Katz, R.A.2    Merkel, G.3    Hittle, J.C.4    Yen, T.J.5    Skalka, A.M.6
  • 29
    • 4544345125 scopus 로고    scopus 로고
    • Caspase-mediated specific cleavage of human histone deacetylase 4
    • 10.1074/jbc.M402475200. 15205465
    • Caspase-mediated specific cleavage of human histone deacetylase 4. F Liu M Dowling XJ Yang GD Kao, J Biol Chem 2004 279 34537 34546 10.1074/jbc. M402475200 15205465
    • (2004) J Biol Chem , vol.279 , pp. 34537-34546
    • Liu, F.1    Dowling, M.2    Yang, X.J.3    Kao, G.D.4
  • 30
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease
    • 10.1126/science.277.5324.373. 9219695
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. TW Kim WH Pettingell YK Jung DM Kovacs RE Tanzi, Science 1997 277 373 376 10.1126/science.277.5324.373 9219695
    • (1997) Science , vol.277 , pp. 373-376
    • Kim, T.W.1    Pettingell, W.H.2    Jung, Y.K.3    Kovacs, D.M.4    Tanzi, R.E.5
  • 31
    • 65449166411 scopus 로고    scopus 로고
    • Novel structural insights into class i and II histone deacetylases
    • 10.2174/156802609788085304. 19355988
    • Novel structural insights into class I and II histone deacetylases. R Ficner, Curr Top Med Chem 2009 9 235 240 10.2174/156802609788085304 19355988
    • (2009) Curr Top Med Chem , vol.9 , pp. 235-240
    • Ficner, R.1
  • 32
    • 0037162715 scopus 로고    scopus 로고
    • HIV-1 integration in the human genome favors active genes and local hotspots
    • 10.1016/S0092-8674(02)00864-4. 12202041
    • HIV-1 integration in the human genome favors active genes and local hotspots. AR Schroder P Shinn H Chen C Berry JR Ecker F Bushman, Cell 2002 110 521 529 10.1016/S0092-8674(02)00864-4 12202041
    • (2002) Cell , vol.110 , pp. 521-529
    • Schroder, A.R.1    Shinn, P.2    Chen, H.3    Berry, C.4    Ecker, J.R.5    Bushman, F.6
  • 33
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • 10.1126/science.272.5259.263. 8602510
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. L Naldini U Blomer P Gallay D Ory R Mulligan FH Gage IM Verma D Trono, Science 1996 272 263 267 10.1126/science.272.5259.263 8602510
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1    Blomer, U.2    Gallay, P.3    Ory, D.4    Mulligan, R.5    Gage, F.H.6    Verma, I.M.7    Trono, D.8
  • 34
    • 3543122311 scopus 로고    scopus 로고
    • Evidence that stable retroviral transduction and cell survival following DNA integration depend on components of the nonhomologous end joining repair pathway
    • 10.1128/JVI.78.16.8573-8581.2004. 15280466
    • Evidence that stable retroviral transduction and cell survival following DNA integration depend on components of the nonhomologous end joining repair pathway. R Daniel JG Greger RA Katz KD Taganov X Wu JC Kappes AM Skalka, J Virol 2004 78 8573 8581 10.1128/JVI.78.16.8573-8581.2004 15280466
    • (2004) J Virol , vol.78 , pp. 8573-8581
    • Daniel, R.1    Greger, J.G.2    Katz, R.A.3    Taganov, K.D.4    Wu, X.5    Kappes, J.C.6    Skalka, A.M.7
  • 35
    • 77957752456 scopus 로고    scopus 로고
    • A role for the Werner syndrome protein in epigenetic inactivation of the pluripotency factor Oct4
    • 10.1111/j.1474-9726.2010.00585.x. 20477760
    • A role for the Werner syndrome protein in epigenetic inactivation of the pluripotency factor Oct4. JA Smith AM Ndoye K Geary MP Lisanti O Igoucheva R Daniel, Aging Cell 2010 9 580 591 10.1111/j.1474-9726.2010.00585.x 20477760
    • (2010) Aging Cell , vol.9 , pp. 580-591
    • Smith, J.A.1    Ndoye, A.M.2    Geary, K.3    Lisanti, M.P.4    Igoucheva, O.5    Daniel, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.