HDAC4

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HDAC4
2vqj.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases HDAC4, AHO3, BDMR, HA6116, HD4, HDAC-4, HDAC-A, HDACA, histone deacetylase 4
External IDs MGI: 3036234 HomoloGene: 55946 GeneCards: 9759
RNA expression pattern
PBB GE HDAC4 204225 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006037

NM_207225

RefSeq (protein)

NP_006028.2

NP_997108.1

Location (UCSC) Chr 2: 239.05 – 239.4 Mb Chr 1: 91.93 – 92.18 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Histone deacetylase 4, also known as HDAC4, is a protein that in humans is encoded by the HDAC4 gene.[3][4]

Function[edit]

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.[5] Furthermore, HDAC4 is required for TGFbeta1-induced myofibroblastic differentiation.[6]

Clinical significance[edit]

Studies have shown that HDAC4 regulates bone and muscle development. Harvard University researchers also concluded that it promotes healthy vision: Reduced levels of the protein led to the death of the rod photoreceptors and bipolar cells in the retinas of mice.[7][8]

Interactions[edit]

HDAC4 has been shown to interact with:

See also[edit]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b 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 21783free to read. PMID 10220385. 
  4. ^ Fischle W, Emiliani S, Hendzel MJ, Nagase T, Nomura N, Voelter W, Verdin E (April 1999). "A new family of human histone deacetylases related to Saccharomyces cerevisiae HDA1p". J. Biol. Chem. 274 (17): 11713–20. doi:10.1074/jbc.274.17.11713. PMID 10206986. 
  5. ^ "Entrez Gene: HDAC4 histone deacetylase 4". 
  6. ^ Glenisson W, Castronovo V, Waltregny D (October 2007). "Histone deacetylase 4 is required for TGFbeta1-induced myofibroblastic differentiation.". Biochim Biophys Acta. 1773 (10): 1572–82. doi:10.1016/j.bbamcr.2007.05.016. PMID 17610967. 
  7. ^ Protein for Sight, Scientific American, 300, 3 (March 2009), p. 23
  8. ^ Chen B, Cepko CL (January 2009). "HDAC4 regulates neuronal survival in normal and diseased retinas". Science. 323 (5911): 256–9. doi:10.1126/science.1166226. PMC 3339762free to read. PMID 19131628. 
  9. ^ a b Lemercier C, Brocard MP, Puvion-Dutilleul F, Kao HY, Albagli O, Khochbin S (June 2002). "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor". J. Biol. Chem. 277 (24): 22045–52. doi:10.1074/jbc.M201736200. PMID 11929873. 
  10. ^ 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. 
  11. ^ Zhang CL, McKinsey TA, Olson EN (October 2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation". Mol. Cell. Biol. 22 (20): 7302–12. doi:10.1128/mcb.22.20.7302-7312.2002. PMC 139799free to read. PMID 12242305. 
  12. ^ 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. 
  13. ^ a b c 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. 
  14. ^ a b c Grozinger CM, Schreiber SL (July 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. PMC 16631free to read. PMID 10869435. 
  15. ^ 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. 
  16. ^ a b Zhou X, Richon VM, Wang AH, Yang XJ, Rifkind RA, Marks PA (December 2000). "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. PMC 18918free to read. PMID 11114188. 
  17. ^ Wang AH, Bertos NR, Vezmar M, Pelletier N, Crosato M, Heng HH, Th'ng J, Han J, Yang XJ (November 1999). "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor". Mol. Cell. Biol. 19 (11): 7816–27. doi:10.1128/mcb.19.11.7816. PMC 84849free to read. PMID 10523670. 
  18. ^ Wang AH, Yang XJ (September 2001). "Histone deacetylase 4 possesses intrinsic nuclear import and export signals". Mol. Cell. Biol. 21 (17): 5992–6005. doi:10.1128/mcb.21.17.5992-6005.2001. PMC 87317free to read. PMID 11486037. 
  19. ^ Miska EA, Karlsson C, Langley E, Nielsen SJ, Pines J, Kouzarides T (September 1999). "HDAC4 deacetylase associates with and represses the MEF2 transcription factor". EMBO J. 18 (18): 5099–107. doi:10.1093/emboj/18.18.5099. PMC 1171580free to read. PMID 10487761. 
  20. ^ Lemercier C, Verdel A, Galloo B, Curtet S, Brocard MP, Khochbin S (May 2000). "mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity". J. Biol. Chem. 275 (20): 15594–9. doi:10.1074/jbc.M908437199. PMID 10748098. 
  21. ^ a b 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 316335free to read. PMID 10640275. 
  22. ^ Franco PJ, Li G, Wei LN (August 2003). "Interaction of nuclear receptor zinc finger DNA binding domains with histone deacetylase". Mol. Cell. Endocrinol. 206 (1-2): 1–12. doi:10.1016/s0303-7207(03)00254-5. PMID 12943985. 
  23. ^ Franco PJ, Farooqui M, Seto E, Wei LN (August 2001). "The orphan nuclear receptor TR2 interacts directly with both class I and class II histone deacetylases". Mol. Endocrinol. 15 (8): 1318–28. doi:10.1210/mend.15.8.0682. PMID 11463856. 
  24. ^ Miska EA, Langley E, Wolf D, Karlsson C, Pines J, Kouzarides T (August 2001). "Differential localization of HDAC4 orchestrates muscle differentiation". Nucleic Acids Res. 29 (16): 3439–47. doi:10.1093/nar/29.16.3439. PMC 55849free to read. PMID 11504882. 
  25. ^ 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. 

Further reading[edit]

External links[edit]

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