HDAC3

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Histone deacetylase 3
Identifiers
Symbols HDAC3; HD3; RPD3; RPD3-2
External IDs OMIM: 605166 MGI: 1343091 HomoloGene: 48250 GeneCards: HDAC3 Gene
EC number 3.5.1.98
RNA expression pattern
PBB GE HDAC3 216326 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 8841 15183
Ensembl ENSG00000171720 ENSMUSG00000024454
UniProt O15379 Q3UM33
RefSeq (mRNA) NM_003883.3 NM_010411.2
RefSeq (protein) NP_003874.2 NP_034541.2
Location (UCSC) Chr 5:
141 – 141.02 Mb		 Chr 18:
38.1 – 38.11 Mb
PubMed search [1] [2]

Histone deacetylase 3 is an enzyme that in humans is encoded by the HDAC3 gene.[1][2]

Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family. It has histone deacetylase activity and represses transcription when tethered to a promoter. It may participate in the regulation of transcription through its binding with the zinc-finger transcription factor YY1. This protein can also down-regulate p53 function and thus modulate cell growth and apoptosis. This gene is regarded as a potential tumor suppressor gene.[3]

Contents

[edit] Model organisms

Model organisms have been used in the study of HDAC3 function. A conditional knockout mouse line, called Hdac3tm1a(EUCOMM)Wtsi[8][9] 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.[10][11][12]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[6][13]

Twenty six tests were carried out on mutant mice and two significant abnormalities were observed.[6] No homozygous mutant embryos were identified during gestation, and in a separate study none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; no significant abnormalities were observed in these animals.[6]

[edit] Interactions

HDAC3 has been shown to interact with HDAC9,[14][15] HDAC7A,[16] Retinoblastoma protein,[17][18] RBBP4,[19] Testicular receptor 2,[20][21][22] MAP3K7IP2,[23] Peroxisome proliferator-activated receptor delta,[21][24] GTF2I,[25][26] Histone deacetylase 5,[27][28][29][30] RELA,[31] MAPK11,[32] TBL1X,[29][33] Nuclear receptor co-repressor 1,[34][35][28][16][29][36][37] Cyclin D1,[38][39] Nuclear receptor co-repressor 2,[34][35][33][28][40][36][37] ZBTB33,[34] SUV39H1,[41] Peroxisome proliferator-activated receptor gamma,[21][17] T-complex 1,[40] HDAC4,[27][28][16][30] CBFA2T3,[42][43] GPS2,[29] YY1,[44][45] RUNX2,[46] GATA1,[47] GATA2,[48] Promyelocytic leukemia protein[49] and Ubiquitin C.[50]

[edit] See also

[edit] References

  1. ^ Emiliani S, Fischle W, Van Lint C, Al-Abed Y, Verdin E (Apr 1998). "Characterization of a human RPD3 ortholog, HDAC3". Proc Natl Acad Sci U S A 95 (6): 2795–800. doi:10.1073/pnas.95.6.2795. PMC 19648. PMID 9501169. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=19648. 
  2. ^ Dangond F, Hafler DA, Tong JK, Randall J, Kojima R, Utku N, Gullans SR (Mar 1998). "Differential display cloning of a novel human histone deacetylase (HDAC3) cDNA from PHA-activated immune cells". Biochem Biophys Res Commun 242 (3): 648–52. doi:10.1006/bbrc.1997.8033. PMID 9464271. 
  3. ^ "Entrez Gene: HDAC3 histone deacetylase 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8841. 
  4. ^ "Salmonella infection data for Hdac3". Wellcome Trust Sanger Institute. http://www.sanger.ac.uk/mouseportal/phenotyping/MAGF/salmonella-challenge/. 
  5. ^ "Citrobacter infection data for Hdac3". Wellcome Trust Sanger Institute. http://www.sanger.ac.uk/mouseportal/phenotyping/MAGF/citrobacter-challenge/. 
  6. ^ a b c d 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. 
  7. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  8. ^ "International Knockout Mouse Consortium". http://www.knockoutmouse.org/martsearch/search?query=Hdac3. 
  9. ^ "Mouse Genome Informatics". http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4433408. 
  10. ^ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M. et al. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMID 21677750.  edit
  11. ^ Dolgin E (June 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718. 
  12. ^ 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. 
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  17. ^ a b Fajas, Lluis; Egler Viviane, Reiter Raphael, Hansen Jacob, Kristiansen Karsten, Debril Marie-Bernard, Miard Stéphanie, Auwerx Johan (Dec. 2002). "The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation". Dev. Cell (United States) 3 (6): 903–10. doi:10.1016/S1534-5807(02)00360-X. ISSN 1534-5807. PMID 12479814. 
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  25. ^ Wen, Yu-Der; Cress W Douglas, Roy Ananda L, Seto Edward (Jan. 2003). "Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I". J. Biol. Chem. (United States) 278 (3): 1841–7. doi:10.1074/jbc.M206528200. ISSN 0021-9258. PMID 12393887. 
  26. ^ Tussié-Luna, María Isabel; Bayarsaihan Dashzeveg, Seto Edward, Ruddle Frank H, Roy Ananda L (Oct. 2002). "Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxbeta". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (20): 12807–12. doi:10.1073/pnas.192464499. ISSN 0027-8424. PMC 130541. PMID 12239342. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=130541. 
  27. ^ a b Grozinger, C M; Hassig C A, Schreiber S L (Apr. 1999). "Three proteins define a class of human histone deacetylases related to yeast Hda1p". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (9): 4868–73. doi:10.1073/pnas.96.9.4868. ISSN 0027-8424. PMC 21783. PMID 10220385. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=21783. 
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  29. ^ a b c d Zhang, Jinsong; Kalkum Markus, Chait Brian T, Roeder Robert G (Mar. 2002). "The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2". Mol. Cell (United States) 9 (3): 611–23. doi:10.1016/S1097-2765(02)00468-9. ISSN 1097-2765. PMID 11931768. 
  30. ^ a b Grozinger, C M; Schreiber S L (Jul. 2000). "Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (14): 7835–40. doi:10.1073/pnas.140199597. ISSN 0027-8424. PMC 16631. PMID 10869435. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16631. 
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  32. ^ Mahlknecht, Ulrich; Will Jutta, Varin Audrey, Hoelzer Dieter, Herbein Georges (Sep. 2004). "Histone deacetylase 3, a class I histone deacetylase, suppresses MAPK11-mediated activating transcription factor-2 activation and represses TNF gene expression". J. Immunol. (United States) 173 (6): 3979–90. ISSN 0022-1767. PMID 15356147. 
  33. ^ a b Guenther, M G; Lane W S, Fischle W, Verdin E, Lazar M A, Shiekhattar R (May. 2000). "A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness". Genes Dev. (UNITED STATES) 14 (9): 1048–57. ISSN 0890-9369. PMC 316569. PMID 10809664. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316569. 
  34. ^ a b c Yoon, Ho-Geun; Chan Doug W, Reynolds Albert B, Qin Jun, Wong Jiemin (Sep. 2003). "N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso". Mol. Cell (United States) 12 (3): 723–34. doi:10.1016/j.molcel.2003.08.008. ISSN 1097-2765. PMID 14527417. 
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  39. ^ Lin, Huei-Min; Zhao Li, Cheng Sheue-Yann (Aug. 2002). "Cyclin D1 Is a Ligand-independent Co-repressor for Thyroid Hormone Receptors". J. Biol. Chem. (United States) 277 (32): 28733–41. doi:10.1074/jbc.M203380200. ISSN 0021-9258. PMID 12048199. 
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[edit] Further reading

[edit] External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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