HDAC4

From Wikipedia, the free encyclopedia

Histone deacetylase 4

PDB rendering based on 2h8n.

Available structures: 2h8n, 2o94

Identifiers

Symbol(s)

HDAC4; HA6116; HD4; HDAC-A; HDACA; KIAA0288

External IDs

OMIM: 605314 MGI: 3036234 HomoloGene: 55946

Gene ontology
Molecular Function:	• DNA binding • histone deacetylase activity • transcription factor binding • transcription repressor activity • hydrolase activity
Cellular Component:	• histone deacetylase complex • nucleus • cytoplasm
Biological Process:	• negative regulation of transcription from RNA polymerase II promoter • skeletal development • transcription • regulation of transcription, DNA-dependent • inflammatory response • cell cycle • multicellular organismal development • nervous system development • negative regulation of cell proliferation • chromatin modification • B cell differentiation • negative regulation of striated muscle development

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_006037 (mRNA)
NP_006028 (protein)

NM_207225 (mRNA)
NP_997108 (protein)

Location

Chr 2: 239.64 - 239.99 Mb

Chr 1: 93.76 - 93.89 Mb

Pubmed search

[1]

[2]

Histone deacetylase 4, also known as HDAC4, is a human gene.

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 II of the histone deacetylase/acuc/apha family. It possesses histone deacetylase activity and represses transcription when tethered to a promoter. This protein does not bind DNA directly, but through transcription factors MEF2C and MEF2D. It seems to interact in a multiprotein complex with RbAp48 and HDAC3.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

Histone deacetylase

[edit] References

^ Entrez Gene: HDAC4 histone deacetylase 4.

[edit] Further reading

Pazin MJ, Kadonaga JT (1997). "What's up and down with histone deacetylation and transcription?". Cell 89 (3): 325–8. PMID 9150131.
Verdin E, Dequiedt F, Kasler HG (2003). "Class II histone deacetylases: versatile regulators.". Trends Genet. 19 (5): 286–93. PMID 12711221.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174.
Wolffe AP (1997). "Transcriptional control. Sinful repression.". Nature 387 (6628): 16–7. doi:10.1038/387016a0. PMID 9139815.
Ohara O, Nagase T, Ishikawa K, et al. (1997). "Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins.". DNA Res. 4 (1): 53–9. PMID 9179496.
Fischle W, Emiliani S, Hendzel MJ, et al. (1999). "A new family of human histone deacetylases related to Saccharomyces cerevisiae HDA1p.". J. Biol. Chem. 274 (17): 11713–20. PMID 10206986.
Grozinger CM, Hassig CA, Schreiber SL (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. PMID 10220385.
Miska EA, Karlsson C, Langley E, et al. (1999). "HDAC4 deacetylase associates with and represses the MEF2 transcription factor.". EMBO J. 18 (18): 5099–107. doi:10.1093/emboj/18.18.5099. PMID 10487761.
Wang AH, Bertos NR, Vezmar M, et al. (1999). "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor.". Mol. Cell. Biol. 19 (11): 7816–27. PMID 10523670.
Youn HD, Grozinger CM, Liu JO (2000). "Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4.". J. Biol. Chem. 275 (29): 22563–7. doi:10.1074/jbc.C000304200. PMID 10825153.
Grozinger CM, Schreiber SL (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. 97 (14): 7835–40. doi:10.1073/pnas.140199597. PMID 10869435.
Huynh KD, Fischle W, Verdin E, Bardwell VJ (2000). "BCoR, a novel corepressor involved in BCL-6 repression.". Genes Dev. 14 (14): 1810–23. PMID 10898795.
Li J, Wang J, Wang J, et al. (2000). "Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3.". EMBO J. 19 (16): 4342–50. doi:10.1093/emboj/19.16.4342. PMID 10944117.
Wang AH, Kruhlak MJ, Wu J, et al. (2000). "Regulation of histone deacetylase 4 by binding of 14-3-3 proteins.". Mol. Cell. Biol. 20 (18): 6904–12. PMID 10958686.
Zhang CL, McKinsey TA, Lu JR, Olson EN (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.
McKinsey TA, Zhang CL, Lu J, Olson EN (2000). "Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation.". Nature 408 (6808): 106–11. doi:10.1038/35040593. PMID 11081517.
Zhou X, Richon VM, Wang AH, et al. (2001). "Histone deacetylase 4 associates with extracellular signal-regulated kinases 1 and 2, and its cellular localization is regulated by oncogenic Ras.". Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14329–33. doi:10.1073/pnas.250494697. PMID 11114188.
McKinsey TA, Zhang CL, Olson EN (2001). "Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5.". Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14400–5. doi:10.1073/pnas.260501497. PMID 11114197.