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: HDAC4
Gene location (Human)
Chromosome 2 (human)
Chr. Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for HDAC4
Genomic location for HDAC4
Band 2q37.3 Start 239,048,168 bp[1]
End 239,401,654 bp[1]
RNA expression pattern
PBB GE HDAC4 204225 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006037

NM_207225

RefSeq (protein)

NP_006028

NP_997108

Location (UCSC) Chr 2: 239.05 – 239.4 Mb Chr 2: 91.93 – 92.2 Mb
PubMed search [3] [4]
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.[5][6]

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.[7] Furthermore, HDAC4 is required for TGFbeta1-induced myofibroblastic differentiation.[8]

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.[9][10]

Interactions[edit]

HDAC4 has been shown to interact with:

See also[edit]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000068024 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026313 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ a b Grozinger CM, Hassig CA, Schreiber SL (April 1999). "Three proteins define a class of human histone deacetylases related to yeast Hda1p". Proceedings of the National Academy of Sciences of the United States of America. 96 (9): 4868–73. PMC 21783Freely accessible. PMID 10220385. doi:10.1073/pnas.96.9.4868. 
  6. ^ 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". The Journal of Biological Chemistry. 274 (17): 11713–20. PMID 10206986. doi:10.1074/jbc.274.17.11713. 
  7. ^ "Entrez Gene: HDAC4 histone deacetylase 4". 
  8. ^ Glenisson W, Castronovo V, Waltregny D (October 2007). "Histone deacetylase 4 is required for TGFbeta1-induced myofibroblastic differentiation". Biochimica et Biophysica Acta. 1773 (10): 1572–82. PMID 17610967. doi:10.1016/j.bbamcr.2007.05.016. 
  9. ^ Protein for Sight, Scientific American, 300, 3 (March 2009), p. 23
  10. ^ Chen B, Cepko CL (January 2009). "HDAC4 regulates neuronal survival in normal and diseased retinas". Science. 323 (5911): 256–9. PMC 3339762Freely accessible. PMID 19131628. doi:10.1126/science.1166226. 
  11. ^ 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". The Journal of Biological Chemistry. 277 (24): 22045–52. PMID 11929873. doi:10.1074/jbc.M201736200. 
  12. ^ 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 Journal. 21 (9): 2215–25. PMID 17371797. doi:10.1096/fj.06-7548com. 
  13. ^ Micheli L, D'Andrea G, Leonardi L, Tirone F (July 2017). "HDAC1, HDAC4, and HDAC9 Bind to PC3/Tis21/Btg2 and Are Required for Its Inhibition of Cell Cycle Progression and Cyclin D1 Expression" (PDF). Journal of Cellular Physiology. 232 (7): 1696–1707. PMID 27333946. doi:10.1002/jcp.25467. 
  14. ^ 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". Molecular and Cellular Biology. 22 (20): 7302–12. PMC 139799Freely accessible. PMID 12242305. doi:10.1128/mcb.22.20.7302-7312.2002. 
  15. ^ 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. PMID 14668799. doi:10.1038/sj.onc.1206902. 
  16. ^ 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". Molecular Cell. 9 (1): 45–57. PMID 11804585. doi:10.1016/s1097-2765(01)00429-4. 
  17. ^ 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". Proceedings of the National Academy of Sciences of the United States of America. 97 (14): 7835–40. PMC 16631Freely accessible. PMID 10869435. doi:10.1073/pnas.140199597. 
  18. ^ 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". The Journal of Biological Chemistry. 276 (38): 35826–35. PMID 11466315. doi:10.1074/jbc.M104935200. 
  19. ^ 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". Proceedings of the National Academy of Sciences of the United States of America. 97 (26): 14329–33. PMC 18918Freely accessible. PMID 11114188. doi:10.1073/pnas.250494697. 
  20. ^ 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". Molecular and Cellular Biology. 19 (11): 7816–27. PMC 84849Freely accessible. PMID 10523670. doi:10.1128/mcb.19.11.7816. 
  21. ^ Wang AH, Yang XJ (September 2001). "Histone deacetylase 4 possesses intrinsic nuclear import and export signals". Molecular and Cellular Biology. 21 (17): 5992–6005. PMC 87317Freely accessible. PMID 11486037. doi:10.1128/mcb.21.17.5992-6005.2001. 
  22. ^ Miska EA, Karlsson C, Langley E, Nielsen SJ, Pines J, Kouzarides T (September 1999). "HDAC4 deacetylase associates with and represses the MEF2 transcription factor". The EMBO Journal. 18 (18): 5099–107. PMC 1171580Freely accessible. PMID 10487761. doi:10.1093/emboj/18.18.5099. 
  23. ^ 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". The Journal of Biological Chemistry. 275 (20): 15594–9. PMID 10748098. doi:10.1074/jbc.M908437199. 
  24. ^ 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 & Development. 14 (1): 45–54. PMC 316335Freely accessible. PMID 10640275. 
  25. ^ Franco PJ, Li G, Wei LN (August 2003). "Interaction of nuclear receptor zinc finger DNA binding domains with histone deacetylase". Molecular and Cellular Endocrinology. 206 (1–2): 1–12. PMID 12943985. doi:10.1016/s0303-7207(03)00254-5. 
  26. ^ 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". Molecular Endocrinology. 15 (8): 1318–28. PMID 11463856. doi:10.1210/mend.15.8.0682. 
  27. ^ Miska EA, Langley E, Wolf D, Karlsson C, Pines J, Kouzarides T (August 2001). "Differential localization of HDAC4 orchestrates muscle differentiation". Nucleic Acids Research. 29 (16): 3439–47. PMC 55849Freely accessible. PMID 11504882. doi:10.1093/nar/29.16.3439. 
  28. ^ 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. PMID 15467736. doi:10.1038/sj.onc.1208128. 

Further reading[edit]

External links[edit]

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