HDAC8

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Histone deacetylase 8
PDB rendering based on 1t64.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols HDAC8 ; RPD3; HDACL1
External IDs Template:OMIM5 Template:MGI HomoloGene41274
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Histone deacetylase 8, also known as HDAC8, is a human gene.[1]

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 class I of the histone deacetylase/acuc/apha family. It has histone deacetylase activity and represses transcription when tethered to a promoter.[1]

See also

References

  1. 1.0 1.1 "Entrez Gene: HDAC8 histone deacetylase 8".

Further reading

  • Verdin E, Dequiedt F, Kasler HG (2003). "Class II histone deacetylases: versatile regulators". Trends Genet. 19 (5): 286–93. PMID 12711221.
  • Hu E, Chen Z, Fredrickson T; et al. (2000). "Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor". J. Biol. Chem. 275 (20): 15254–64. doi:10.1074/jbc.M908988199. PMID 10748112.
  • McDonell N, Ramser J, Francis F; et al. (2000). "Characterization of a highly complex region in Xq13 and mapping of three isodicentric breakpoints associated with preleukemia". Genomics. 64 (3): 221–9. doi:10.1006/geno.2000.6128. PMID 10756090.
  • Van den Wyngaert I, de Vries W, Kremer A; et al. (2000). "Cloning and characterization of human histone deacetylase 8". FEBS Lett. 478 (1–2): 77–83. PMID 10922473.
  • Buggy JJ, Sideris ML, Mak P; et al. (2001). "Cloning and characterization of a novel human histone deacetylase, HDAC8". Biochem. J. 350 Pt 1: 199–205. PMID 10926844.
  • Amann JM, Nip J, Strom DK; et al. (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. PMID 11533236.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Durst KL, Lutterbach B, Kummalue T; et al. (2003). "The inv(16) fusion protein associates with corepressors via a smooth muscle myosin heavy-chain domain". Mol. Cell. Biol. 23 (2): 607–19. PMID 12509458.
  • Rodriguez M, Yu X, Chen J, Songyang Z (2004). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". J. Biol. Chem. 278 (52): 52914–8. doi:10.1074/jbc.C300407200. PMID 14578343.
  • Johnson JM, Castle J, Garrett-Engele P; et al. (2004). "Genome-wide survey of human alternative pre-mRNA splicing with exon junction microarrays". Science. 302 (5653): 2141–4. doi:10.1126/science.1090100. PMID 14684825.
  • Lee H, Rezai-Zadeh N, Seto E (2004). "Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A.". Mol. Cell. Biol. 24 (2): 765–73. PMID 14701748.
  • Vannini A, Volpari C, Filocamo G; et al. (2004). "Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor". Proc. Natl. Acad. Sci. U.S.A. 101 (42): 15064–9. doi:10.1073/pnas.0404603101. PMID 15477595.
  • Waltregny D, North B, Van Mellaert F; et al. (2005). "Screening of histone deacetylases (HDAC) expression in human prostate cancer reveals distinct class I HDAC profiles between epithelial and stromal cells". European journal of histochemistry : EJH. 48 (3): 273–90. PMID 15590418.
  • Waltregny D, Glénisson W, Tran SL; et al. (2006). "Histone deacetylase HDAC8 associates with smooth muscle alpha-actin and is essential for smooth muscle cell contractility". FASEB J. 19 (8): 966–8. doi:10.1096/fj.04-2303fje. PMID 15772115.
  • Gantt SL, Gattis SG, Fierke CA (2006). "Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion". Biochemistry. 45 (19): 6170–8. doi:10.1021/bi060212u. PMID 16681389.
  • Lee H, Sengupta N, Villagra A; et al. (2006). "Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation". Mol. Cell. Biol. 26 (14): 5259–69. doi:10.1128/MCB.01971-05. PMID 16809764.
  • Vannini A, Volpari C, Gallinari P; et al. (2007). "Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex". EMBO Rep. 8 (9): 879–84. doi:10.1038/sj.embor.7401047. PMID 17721440.
  • Nakagawa M, Oda Y, Eguchi T; et al. (2007). "Expression profile of class I histone deacetylases in human cancer tissues". Oncol. Rep. 18 (4): 769–74. PMID 17786334.

External links

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