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HDAC1

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HDAC1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesHDAC1, GON-10, HD1, RPD3, RPD3L1, histone deacetylase 1, KDAC1
External IDsOMIM: 601241; MGI: 108086; HomoloGene: 68426; GeneCards: HDAC1; OMA:HDAC1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004964

NM_008228

RefSeq (protein)

NP_004955

NP_032254

Location (UCSC)Chr 1: 32.29 – 32.33 MbChr 4: 129.41 – 129.44 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Histone deacetylase 1 (HDAC1) is an enzyme that in humans is encoded by the HDAC1 gene.[5]

Function

Histone acetylation and deacetylation, catalyzed by multisubunit complexes, play a key role in the regulation of eukaryotic gene expression. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. It also interacts with retinoblastoma tumor-suppressor protein and this complex is a key element in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2 MTA2, it deacetylates p53 and modulates its effect on cell growth and apoptosis.[6]

Model organisms

Model organisms have been used in the study of HDAC1 function. A conditional knockout mouse line, called Hdac1tm1a(EUCOMM)Wtsi[11][12] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[13][14][15] Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[9][16] Twenty five tests were carried out and two phenotypes were reported. A reduced number of homozygous mutant embryos were identified during gestation, and none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice, and no significant abnormalities were observed in these animals.[9]

Interactions

HDAC1 has been shown to interact with:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000116478Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028800Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Taunton J, Hassig CA, Schreiber SL (May 1996). "A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p". Science. 272 (5260): 408–11. doi:10.1126/science.272.5260.408. PMID 8602529.
  6. ^ "Entrez Gene: HDAC1 histone deacetylase 1".
  7. ^ "Salmonella infection data for Hdac1". Wellcome Trust Sanger Institute.
  8. ^ "Citrobacter infection data for Hdac1". Wellcome Trust Sanger Institute.
  9. ^ a b c Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x.
  10. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  11. ^ "International Knockout Mouse Consortium".
  12. ^ "Mouse Genome Informatics".
  13. ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  14. ^ Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  15. ^ Collins FS, Rossant J, Wurst W (January 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  16. ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  17. ^ Gaughan L, Logan IR, Cook S, Neal DE, Robson CN (July 2002). "Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor". J. Biol. Chem. 277 (29): 25904–13. doi:10.1074/jbc.M203423200. PMID 11994312.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  18. ^ a b David G, Alland L, Hong SH, Wong CW, DePinho RA, Dejean A (May 1998). "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene. 16 (19): 2549–56. doi:10.1038/sj.onc.1202043. PMID 9627120.
  19. ^ Deltour S, Guerardel C, Leprince D (December 1999). "Recruitment of SMRT/N-CoR-mSin3A-HDAC-repressing complexes is not a general mechanism for BTB/POZ transcriptional repressors: the case of HIC-1 and gammaFBP-B". Proc. Natl. Acad. Sci. U.S.A. 96 (26): 14831–6. doi:10.1073/pnas.96.26.14831. PMC 24733. PMID 10611298.
  20. ^ Farioli-Vecchioli S, Tanori M, Micheli L, Mancuso M, Leonardi L, Saran A, Ciotti MT, Ferretti E, Gulino A, Pazzaglia S, Tirone F (July 2007). "Inhibition of medulloblastoma tumorigenesis by the antiproliferative and pro-differentiative gene PC3". FASEB J. 21 (9): 2215–25. doi:10.1096/fj.06-7548com. PMID 17371797.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  21. ^ a b c d e f Yoon YM, Baek KH, Jeong SJ, Shin HJ, Ha GH, Jeon AH, Hwang SG, Chun JS, Lee CW (September 2004). "WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase". FEBS Lett. 575 (1–3): 23–9. doi:10.1016/j.febslet.2004.07.089. PMID 15388328.
  22. ^ Hoogeveen AT, Rossetti S, Stoyanova V, Schonkeren J, Fenaroli A, Schiaffonati L, van Unen L, Sacchi N (September 2002). "The transcriptional corepressor MTG16a contains a novel nucleolar targeting sequence deranged in t (16; 21)-positive myeloid malignancies". Oncogene. 21 (43): 6703–12. doi:10.1038/sj.onc.1205882. PMID 12242670.
  23. ^ Amann JM, Nip J, Strom DK, Lutterbach B, Harada H, Lenny N, Downing JR, Meyers S, Hiebert SW (October 2001). "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain". Mol. Cell. Biol. 21 (19): 6470–83. doi:10.1128/mcb.21.19.6470-6483.2001. PMC 99794. PMID 11533236.
  24. ^ a b c d Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (October 1998). "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex". Nature. 395 (6705): 917–21. doi:10.1038/27699. PMID 9804427.
  25. ^ a b c d Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (February 2002). "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Mol. Cell. Biol. 22 (3): 835–48. doi:10.1128/mcb.22.3.835-848.2002. PMC 133546. PMID 11784859.
  26. ^ a b c d e f g Yao YL, Yang WM (October 2003). "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity". J. Biol. Chem. 278 (43): 42560–8. doi:10.1074/jbc.M302955200. PMID 12920132.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  27. ^ a b c Grozinger CM, Hassig CA, Schreiber SL (April 1999). "Three proteins define a class of human histone deacetylases related to yeast Hda1p". Proc. Natl. Acad. Sci. U.S.A. 96 (9): 4868–73. doi:10.1073/pnas.96.9.4868. PMC 21783. PMID 10220385.
  28. ^ Smirnov DA, Hou S, Ricciardi RP (March 2000). "Association of histone deacetylase with COUP-TF in tumorigenic Ad12-transformed cells and its potential role in shut-off of MHC class I transcription". Virology. 268 (2): 319–28. doi:10.1006/viro.1999.0181. PMID 10704340.
  29. ^ a b Melhuish TA, Wotton D (December 2000). "The interaction of the carboxyl terminus-binding protein with the Smad corepressor TGIF is disrupted by a holoprosencephaly mutation in TGIF". J. Biol. Chem. 275 (50): 39762–6. doi:10.1074/jbc.C000416200. PMID 10995736.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  30. ^ Zhang CL, McKinsey TA, Lu JR, Olson EN (January 2001). "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor". J. Biol. Chem. 276 (1): 35–9. doi:10.1074/jbc.M007364200. PMID 11022042.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  31. ^ Sundqvist A, Sollerbrant K, Svensson C (June 1998). "The carboxy-terminal region of adenovirus E1A activates transcription through targeting of a C-terminal binding protein-histone deacetylase complex". FEBS Lett. 429 (2): 183–8. doi:10.1016/s0014-5793(98)00588-2. PMID 9650586.
  32. ^ a b Wilson BJ, Bates GJ, Nicol SM, Gregory DJ, Perkins ND, Fuller-Pace FV (August 2004). "The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner". BMC Mol. Biol. 5: 11. doi:10.1186/1471-2199-5-11. PMC 514542. PMID 15298701.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  33. ^ Fuks F, Burgers WA, Godin N, Kasai M, Kouzarides T (May 2001). "Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription". EMBO J. 20 (10): 2536–44. doi:10.1093/emboj/20.10.2536. PMC 125250. PMID 11350943.
  34. ^ Aapola U, Liiv I, Peterson P (August 2002). "Imprinting regulator DNMT3L is a transcriptional repressor associated with histone deacetylase activity". Nucleic Acids Res. 30 (16): 3602–8. doi:10.1093/nar/gkf474. PMC 134241. PMID 12177302.
  35. ^ Deplus R, Brenner C, Burgers WA, Putmans P, Kouzarides T, de Launoit Y, Fuks F (September 2002). "Dnmt3L is a transcriptional repressor that recruits histone deacetylase". Nucleic Acids Res. 30 (17): 3831–8. doi:10.1093/nar/gkf509. PMC 137431. PMID 12202768.
  36. ^ Li H, Leo C, Zhu J, Wu X, O'Neil J, Park EJ, Chen JD (March 2000). "Sequestration and inhibition of Daxx-mediated transcriptional repression by PML". Mol. Cell. Biol. 20 (5): 1784–96. doi:10.1128/mcb.20.5.1784-1796.2000. PMC 85360. PMID 10669754.
  37. ^ a b c van der Vlag J, Otte AP (December 1999). "Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation". Nat. Genet. 23 (4): 474–8. doi:10.1038/70602. PMID 10581039.
  38. ^ Vinatzer U, Taplick J, Seiser C, Fonatsch C, Wieser R (September 2001). "The leukaemia-associated transcription factors EVI-1 and MDS1/EVI1 repress transcription and interact with histone deacetylase". Br. J. Haematol. 114 (3): 566–73. doi:10.1046/j.1365-2141.2001.02987.x. PMID 11552981.
  39. ^ Chakraborty S, Senyuk V, Sitailo S, Chi Y, Nucifora G (November 2001). "Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles". J. Biol. Chem. 276 (48): 44936–43. doi:10.1074/jbc.M106733200. PMID 11568182.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  40. ^ Yang WM, Yao YL, Seto E (September 2001). "The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1". EMBO J. 20 (17): 4814–25. doi:10.1093/emboj/20.17.4814. PMC 125595. PMID 11532945.
  41. ^ Watamoto K, Towatari M, Ozawa Y, Miyata Y, Okamoto M, Abe A, Naoe T, Saito H (December 2003). "Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation". Oncogene. 22 (57): 9176–84. doi:10.1038/sj.onc.1206902. PMID 14668799.
  42. ^ a b c d Hakimi MA, Bochar DA, Chenoweth J, Lane WS, Mandel G, Shiekhattar R (May 2002). "A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes". Proc. Natl. Acad. Sci. U.S.A. 99 (11): 7420–5. doi:10.1073/pnas.112008599. PMC 124246. PMID 12032298.
  43. ^ a b Johnson CA, White DA, Lavender JS, O'Neill LP, Turner BM (March 2002). "Human class I histone deacetylase complexes show enhanced catalytic activity in the presence of ATP and co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70". J. Biol. Chem. 277 (11): 9590–7. doi:10.1074/jbc.M107942200. PMID 11777905.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  44. ^ a b Cai RL, Yan-Neale Y, Cueto MA, Xu H, Cohen D (September 2000). "HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins". J. Biol. Chem. 275 (36): 27909–16. doi:10.1074/jbc.M000168200. PMID 10846170.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  45. ^ a b Fischer DD, Cai R, Bhatia U, Asselbergs FA, Song C, Terry R, Trogani N, Widmer R, Atadja P, Cohen D (February 2002). "Isolation and characterization of a novel class II histone deacetylase, HDAC10". J. Biol. Chem. 277 (8): 6656–66. doi:10.1074/jbc.M108055200. PMID 11739383.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  46. ^ Hakimi MA, Dong Y, Lane WS, Speicher DW, Shiekhattar R (February 2003). "A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes". J. Biol. Chem. 278 (9): 7234–9. doi:10.1074/jbc.M208992200. PMID 12493763.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  47. ^ Fischle W, Dequiedt F, Hendzel MJ, Guenther MG, Lazar MA, Voelter W, Verdin E (January 2002). "Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR". Mol. Cell. 9 (1): 45–57. doi:10.1016/s1097-2765(01)00429-4. PMID 11804585.
  48. ^ Fischle W, Dequiedt F, Fillion M, Hendzel MJ, Voelter W, Verdin E (September 2001). "Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo". J. Biol. Chem. 276 (38): 35826–35. doi:10.1074/jbc.M104935200. PMID 11466315.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  49. ^ a b Ashburner BP, Westerheide SD, Baldwin AS (October 2001). "The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression". Mol. Cell. Biol. 21 (20): 7065–77. doi:10.1128/MCB.21.20.7065-7077.2001. PMC 99882. PMID 11564889.
  50. ^ a b c d e f g h i Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (August 1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
  51. ^ a b c Hassig CA, Tong JK, Fleischer TC, Owa T, Grable PG, Ayer DE, Schreiber SL (March 1998). "A role for histone deacetylase activity in HDAC1-mediated transcriptional repression". Proc. Natl. Acad. Sci. U.S.A. 95 (7): 3519–24. doi:10.1073/pnas.95.7.3519. PMC 19868. PMID 9520398.
  52. ^ a b c Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (May 1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell. 89 (3): 357–64. doi:10.1016/s0092-8674(00)80216-0. PMID 9150135.
  53. ^ Melhuish TA, Gallo CM, Wotton D (August 2001). "TGIF2 interacts with histone deacetylase 1 and represses transcription". J. Biol. Chem. 276 (34): 32109–14. doi:10.1074/jbc.M103377200. PMID 11427533.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  54. ^ Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W (April 2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes Dev. 17 (7): 896–911. doi:10.1101/gad.252103. PMC 196026. PMID 12670868.
  55. ^ Vietor I, Vadivelu SK, Wick N, Hoffman R, Cotten M, Seiser C, Fialka I, Wunderlich W, Haase A, Korinkova G, Brosch G, Huber LA (September 2002). "TIS7 interacts with the mammalian SIN3 histone deacetylase complex in epithelial cells". EMBO J. 21 (17): 4621–31. doi:10.1093/emboj/cdf461. PMC 125408. PMID 12198164.
  56. ^ a b Koipally J, Renold A, Kim J, Georgopoulos K (June 1999). "Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes". EMBO J. 18 (11): 3090–100. doi:10.1093/emboj/18.11.3090. PMC 1171390. PMID 10357820.
  57. ^ Koipally J, Georgopoulos K (August 2002). "A molecular dissection of the repression circuitry of Ikaros". J. Biol. Chem. 277 (31): 27697–705. doi:10.1074/jbc.M201694200. PMID 12015313.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  58. ^ Vieyra D, Loewith R, Scott M, Bonnefin P, Boisvert FM, Cheema P, Pastyryeva S, Meijer M, Johnston RN, Bazett-Jones DP, McMahon S, Cole MD, Young D, Riabowol K (August 2002). "Human ING1 proteins differentially regulate histone acetylation". J. Biol. Chem. 277 (33): 29832–9. doi:10.1074/jbc.M200197200. PMID 12015309.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  59. ^ Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F (December 2002). "MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase". J. Biol. Chem. 277 (50): 48714–23. doi:10.1074/jbc.M208461200. PMID 12354758.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  60. ^ Saito M, Ishikawa F (September 2002). "The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2". J. Biol. Chem. 277 (38): 35434–9. doi:10.1074/jbc.M203455200. PMID 12124384.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  61. ^ Ding Z, Gillespie LL, Paterno GD (January 2003). "Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain". Mol. Cell. Biol. 23 (1): 250–8. doi:10.1128/mcb.23.1.250-258.2003. PMC 140656. PMID 12482978.
  62. ^ Xia ZB, Anderson M, Diaz MO, Zeleznik-Le NJ (July 2003). "MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein". Proc. Natl. Acad. Sci. U.S.A. 100 (14): 8342–7. doi:10.1073/pnas.1436338100. PMC 166231. PMID 12829790.
  63. ^ Mazumdar A, Wang RA, Mishra SK, Adam L, Bagheri-Yarmand R, Mandal M, Vadlamudi RK, Kumar R (January 2001). "Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor". Nat. Cell Biol. 3 (1): 30–7. doi:10.1038/35050532. PMID 11146623.
  64. ^ a b c d You A, Tong JK, Grozinger CM, Schreiber SL (February 2001). "CoREST is an integral component of the CoREST- human histone deacetylase complex". Proc. Natl. Acad. Sci. U.S.A. 98 (4): 1454–8. doi:10.1073/pnas.98.4.1454. PMC 29278. PMID 11171972.
  65. ^ a b c Yasui D, Miyano M, Cai S, Varga-Weisz P, Kohwi-Shigematsu T (October 2002). "SATB1 targets chromatin remodelling to regulate genes over long distances". Nature. 419 (6907): 641–5. doi:10.1038/nature01084. PMID 12374985.
  66. ^ Ito A, Kawaguchi Y, Lai CH, Kovacs JJ, Higashimoto Y, Appella E, Yao TP (November 2002). "MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation". EMBO J. 21 (22): 6236–45. doi:10.1093/emboj/cdf616. PMC 137207. PMID 12426395.
  67. ^ a b c Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A (September 1999). "MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex". Nat. Genet. 23 (1): 58–61. doi:10.1038/12659. PMID 10471499.
  68. ^ Brackertz M, Boeke J, Zhang R, Renkawitz R (October 2002). "Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3". J. Biol. Chem. 277 (43): 40958–66. doi:10.1074/jbc.M207467200. PMID 12183469.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  69. ^ Wotton D, Lo RS, Lee S, Massagué J (April 1999). "A Smad transcriptional corepressor". Cell. 97 (1): 29–39. doi:10.1016/s0092-8674(00)80712-6. PMID 10199400.
  70. ^ a b Polesskaya A, Rudnicki MA (October 2001). "A MyoD-dependent differentiation checkpoint: ensuring genome integrity". Dev. Cell. 3 (6): 757–8. doi:10.1016/s1534-5807(02)00372-6. PMID 12479798.
  71. ^ Mal A, Sturniolo M, Schiltz RL, Ghosh MK, Harter ML (April 2001). "A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program". EMBO J. 20 (7): 1739–53. doi:10.1093/emboj/20.7.1739. PMC 145490. PMID 11285237.
  72. ^ a b Zhong H, May MJ, Jimi E, Ghosh S (March 2002). "The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1". Mol. Cell. 9 (3): 625–36. doi:10.1016/s1097-2765(02)00477-x. PMID 11931769.
  73. ^ Underhill C, Qutob MS, Yee SP, Torchia J (December 2000). "A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1". J. Biol. Chem. 275 (51): 40463–70. doi:10.1074/jbc.M007864200. PMID 11013263.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  74. ^ Milutinovic S, Zhuang Q, Szyf M (June 2002). "Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification". J. Biol. Chem. 277 (23): 20974–8. doi:10.1074/jbc.M202504200. PMID 11929879.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  75. ^ Iwase S, Januma A, Miyamoto K, Shono N, Honda A, Yanagisawa J, Baba T (September 2004). "Characterization of BHC80 in BRAF-HDAC complex, involved in neuron-specific gene repression". Biochem. Biophys. Res. Commun. 322 (2): 601–8. doi:10.1016/j.bbrc.2004.07.163. PMID 15325272.
  76. ^ Joshi B, Ko D, Ordonez-Ercan D, Chellappan SP (December 2003). "A putative coiled-coil domain of prohibitin is sufficient to repress E2F1-mediated transcription and induce apoptosis". Biochem. Biophys. Res. Commun. 312 (2): 459–66. doi:10.1016/j.bbrc.2003.10.148. PMID 14637159.
  77. ^ a b Wang S, Fusaro G, Padmanabhan J, Chellappan SP (December 2002). "Prohibitin co-localizes with Rb in the nucleus and recruits N-CoR and HDAC1 for transcriptional repression". Oncogene. 21 (55): 8388–96. doi:10.1038/sj.onc.1205944. PMID 12466959.
  78. ^ Khan MM, Nomura T, Kim H, Kaul SC, Wadhwa R, Shinagawa T, Ichikawa-Iwata E, Zhong S, Pandolfi PP, Ishii S (June 2001). "Role of PML and PML-RARalpha in Mad-mediated transcriptional repression". Mol. Cell. 7 (6): 1233–43. doi:10.1016/s1097-2765(01)00257-x. PMID 11430826.
  79. ^ Wu WS, Vallian S, Seto E, Yang WM, Edmondson D, Roth S, Chang KS (April 2001). "The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases". Mol. Cell. Biol. 21 (7): 2259–68. doi:10.1128/MCB.21.7.2259-2268.2001. PMC 86860. PMID 11259576.
  80. ^ a b Zhang Y, Dufau ML (June 2003). "Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes". J. Steroid Biochem. Mol. Biol. 85 (2–5): 401–14. doi:10.1016/s0960-0760(03)00230-9. PMID 12943729.
  81. ^ a b c Zhang Y, Dufau ML (September 2002). "Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex". J. Biol. Chem. 277 (36): 33431–8. doi:10.1074/jbc.M204417200. PMID 12091390.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  82. ^ Nicolas E, Ait-Si-Ali S, Trouche D (August 2001). "The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein". Nucleic Acids Res. 29 (15): 3131–6. doi:10.1093/nar/29.15.3131. PMC 55834. PMID 11470869.
  83. ^ Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE (May 1997). "Histone deacetylase activity is required for full transcriptional repression by mSin3A". Cell. 89 (3): 341–7. doi:10.1016/s0092-8674(00)80214-7. PMID 9150133.
  84. ^ Kiernan R, Brès V, Ng RW, Coudart MP, El Messaoudi S, Sardet C, Jin DY, Emiliani S, Benkirane M (January 2003). "Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65". J. Biol. Chem. 278 (4): 2758–66. doi:10.1074/jbc.M209572200. PMID 12419806.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  85. ^ Anderson LA, Perkins ND (August 2002). "The large subunit of replication factor C interacts with the histone deacetylase, HDAC1". J. Biol. Chem. 277 (33): 29550–4. doi:10.1074/jbc.M200513200. PMID 12045192.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  86. ^ a b c Ferreira R, Magnaghi-Jaulin L, Robin P, Harel-Bellan A, Trouche D (September 1998). "The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase". Proc. Natl. Acad. Sci. U.S.A. 95 (18): 10493–8. doi:10.1073/pnas.95.18.10493. PMC 27922. PMID 9724731.
  87. ^ a b Lai A, Lee JM, Yang WM, DeCaprio JA, Kaelin WG, Seto E, Branton PE (October 1999). "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins". Mol. Cell. Biol. 19 (10): 6632–41. doi:10.1128/mcb.19.10.6632. PMC 84642. PMID 10490602.
  88. ^ Dick FA, Sailhamer E, Dyson NJ (May 2000). "Mutagenesis of the pRB pocket reveals that cell cycle arrest functions are separable from binding to viral oncoproteins". Mol. Cell. Biol. 20 (10): 3715–27. doi:10.1128/mcb.20.10.3715-3727.2000. PMC 85672. PMID 10779361.
  89. ^ Fuks F, Burgers WA, Brehm A, Hughes-Davies L, Kouzarides T (January 2000). "DNA methyltransferase Dnmt1 associates with histone deacetylase activity". Nat. Genet. 24 (1): 88–91. doi:10.1038/71750. PMID 10615135.
  90. ^ Luo RX, Postigo AA, Dean DC (February 1998). "Rb interacts with histone deacetylase to repress transcription". Cell. 92 (4): 463–73. doi:10.1016/s0092-8674(00)80940-x. PMID 9491888.
  91. ^ Bouzahzah B, Fu M, Iavarone A, Factor VM, Thorgeirsson SS, Pestell RG (August 2000). "Transforming growth factor-beta1 recruits histone deacetylase 1 to a p130 repressor complex in transgenic mice in vivo". Cancer Res. 60 (16): 4531–7. PMID 10969803.
  92. ^ Huang NE, Lin CH, Lin YS, Yu WC (June 2003). "Modulation of YY1 activity by SAP30". Biochem. Biophys. Res. Commun. 306 (1): 267–75. doi:10.1016/S0006-291X(03)00966-5. PMID 12788099.
  93. ^ Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D (June 1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Mol. Cell. 1 (7): 1021–31. doi:10.1016/s1097-2765(00)80102-1. PMID 9651585.
  94. ^ Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I (August 2004). "HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations". Nat. Struct. Mol. Biol. 11 (8): 738–46. doi:10.1038/nsmb798. PMID 15235594.
  95. ^ Yochum GS, Ayer DE (July 2001). "Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex". Mol. Cell. Biol. 21 (13): 4110–8. doi:10.1128/MCB.21.13.4110-4118.2001. PMC 87072. PMID 11390640.
  96. ^ a b Fleischer TC, Yun UJ, Ayer DE (May 2003). "Identification and characterization of three new components of the mSin3A corepressor complex". Mol. Cell. Biol. 23 (10): 3456–67. doi:10.1128/mcb.23.10.3456-3467.2003. PMC 164750. PMID 12724404.
  97. ^ Yang L, Mei Q, Zielinska-Kwiatkowska A, Matsui Y, Blackburn ML, Benedetti D, Krumm AA, Taborsky GJ, Chansky HA (February 2003). "An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B". Biochem. J. 369 (Pt 3): 651–7. doi:10.1042/BJ20020854. PMC 1223118. PMID 12398767.
  98. ^ Zhang J, Kalkum M, Chait BT, Roeder RG (March 2002). "The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2". Mol. Cell. 9 (3): 611–23. doi:10.1016/s1097-2765(02)00468-9. PMID 11931768.
  99. ^ Huang EY, Zhang J, Miska EA, Guenther MG, Kouzarides T, Lazar MA (January 2000). "Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway". Genes Dev. 14 (1): 45–54. PMC 316335. PMID 10640275.
  100. ^ Shi Y, Downes M, Xie W, Kao HY, Ordentlich P, Tsai CC, Hon M, Evans RM (May 2001). "Sharp, an inducible cofactor that integrates nuclear receptor repression and activation". Genes Dev. 15 (9): 1140–51. doi:10.1101/gad.871201. PMC 312688. PMID 11331609.
  101. ^ Alland L, David G, Shen-Li H, Potes J, Muhle R, Lee HC, Hou H, Chen K, DePinho RA (April 2002). "Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex". Mol. Cell. Biol. 22 (8): 2743–50. doi:10.1128/mcb.22.8.2743-2750.2002. PMC 133736. PMID 11909966.
  102. ^ Vaute O, Nicolas E, Vandel L, Trouche D (January 2002). "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Res. 30 (2): 475–81. doi:10.1093/nar/30.2.475. PMC 99834. PMID 11788710.
  103. ^ Di Padova M, Bruno T, De Nicola F, Iezzi S, D'Angelo C, Gallo R, Nicosia D, Corbi N, Biroccio A, Floridi A, Passananti C, Fanciulli M (September 2003). "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter". J. Biol. Chem. 278 (38): 36496–504. doi:10.1074/jbc.M306694200. PMID 12847090.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  104. ^ Singh J, Murata K, Itahana Y, Desprez PY (March 2002). "Constitutive expression of the Id-1 promoter in human metastatic breast cancer cells is linked with the loss of NF-1/Rb/HDAC-1 transcription repressor complex". Oncogene. 21 (12): 1812–22. doi:10.1038/sj.onc.1205252. PMID 11896613.
  105. ^ Sun JM, Chen HY, Moniwa M, Litchfield DW, Seto E, Davie JR (September 2002). "The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2". J. Biol. Chem. 277 (39): 35783–6. doi:10.1074/jbc.C200378200. PMID 12176973.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  106. ^ a b Tsai SC, Valkov N, Yang WM, Gump J, Sullivan D, Seto E (November 2000). "Histone deacetylase interacts directly with DNA topoisomerase II". Nat. Genet. 26 (3): 349–53. doi:10.1038/81671. PMID 11062478.
  107. ^ a b Johnson CA, Padget K, Austin CA, Turner BM (February 2001). "Deacetylase activity associates with topoisomerase II and is necessary for etoposide-induced apoptosis". J. Biol. Chem. 276 (7): 4539–42. doi:10.1074/jbc.C000824200. PMID 11136718.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  108. ^ Chauchereau A, Mathieu M, de Saintignon J, Ferreira R, Pritchard LL, Mishal Z, Dejean A, Harel-Bellan A (November 2004). "HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF". Oncogene. 23 (54): 8777–84. doi:10.1038/sj.onc.1208128. PMID 15467736.
  109. ^ Wong CW, Privalsky ML (October 1998). "Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6". J. Biol. Chem. 273 (42): 27695–702. doi:10.1074/jbc.273.42.27695. PMID 9765306.{{cite journal}}: CS1 maint: unflagged free DOI (link)

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