HDAC8

From Wikipedia, the free encyclopedia

Histone deacetylase 8

PDB rendering based on 1t64.

Available structures: 1t64, 1t67, 1t69, 1vkg, 1w22

Identifiers

Symbol(s)

HDAC8; RPD3; HDACL1

External IDs

OMIM: 300269 MGI: 1917565 HomoloGene: 41274

Gene ontology
Molecular Function:	• histone deacetylase activity • transcription factor binding • hydrolase activity
Cellular Component:	• histone deacetylase complex • nuclear chromosome • nucleus • cytoplasm
Biological Process:	• negative regulation of transcription from RNA polymerase II promoter • chromatin assembly or disassembly • transcription • regulation of transcription, DNA-dependent • chromatin modification • histone deacetylation

Orthologs

Human

Mouse

Refseq

NM_018486 (mRNA)
NP_060956 (protein)

NM_027382 (mRNA)
NP_081658 (protein)

Location

Chr X: 71.47 - 71.71 Mb

Chr X: 98.51 - 98.71 Mb

Pubmed search

[1]

[2]

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]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

Histone deacetylase

[edit] References

^ ^a ^b Entrez Gene: HDAC8 histone deacetylase 8.

[edit] 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.