Biology:HDAC4

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Histone deacetylase 4, also known as HDAC4, is a protein that in humans is encoded by the HDAC4 gene.[1][2]

Function

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.[3] Furthermore, HDAC4 is required for TGFbeta1-induced myofibroblastic differentiation.[4]

Clinical significance

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.[5][6]

Interactions

HDAC4 has been shown to interact with:


See also

References

  1. ↑ 1.0 1.1 "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. April 1999. doi:10.1073/pnas.96.9.4868. PMID 10220385. Bibcode: 1999PNAS...96.4868G. 
  2. ↑ "A new family of human histone deacetylases related to Saccharomyces cerevisiae HDA1p". The Journal of Biological Chemistry 274 (17): 11713–20. April 1999. doi:10.1074/jbc.274.17.11713. PMID 10206986. 
  3. ↑ "Entrez Gene: HDAC4 histone deacetylase 4". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9759. 
  4. ↑ "Histone deacetylase 4 is required for TGFbeta1-induced myofibroblastic differentiation". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1773 (10): 1572–82. October 2007. doi:10.1016/j.bbamcr.2007.05.016. PMID 17610967. 
  5. ↑ Protein for Sight, Scientific American, 300, 3 (March 2009), p. 23
  6. ↑ "HDAC4 regulates neuronal survival in normal and diseased retinas". Science 323 (5911): 256–9. January 2009. doi:10.1126/science.1166226. PMID 19131628. 
  7. ↑ 7.0 7.1 "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor". The Journal of Biological Chemistry 277 (24): 22045–52. June 2002. doi:10.1074/jbc.M201736200. PMID 11929873. 
  8. ↑ "Inhibition of medulloblastoma tumorigenesis by the antiproliferative and pro-differentiative gene PC3". FASEB Journal 21 (9): 2215–25. July 2007. doi:10.1096/fj.06-7548com. PMID 17371797. 
  9. ↑ "HDAC1, HDAC4, and HDAC9 Bind to PC3/Tis21/Btg2 and Are Required for Its Inhibition of Cell Cycle Progression and Cyclin D1 Expression". Journal of Cellular Physiology 232 (7): 1696–1707. July 2017. doi:10.1002/jcp.25467. PMID 27333946. http://www.inmm.cnr.it/tirone/pdfs/Micheli_et_al-2017-J_Cell_Physiol%20PC3-HDACs.pdf. 
  10. ↑ "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. October 2002. doi:10.1128/mcb.22.20.7302-7312.2002. PMID 12242305. 
  11. ↑ "Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation". Oncogene 22 (57): 9176–84. December 2003. doi:10.1038/sj.onc.1206902. PMID 14668799. 
  12. ↑ 12.0 12.1 12.2 "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. January 2002. doi:10.1016/s1097-2765(01)00429-4. PMID 11804585. 
  13. ↑ 13.0 13.1 13.2 "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. July 2000. doi:10.1073/pnas.140199597. PMID 10869435. Bibcode: 2000PNAS...97.7835G. 
  14. ↑ "Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo". The Journal of Biological Chemistry 276 (38): 35826–35. September 2001. doi:10.1074/jbc.M104935200. PMID 11466315. 
  15. ↑ 15.0 15.1 "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. December 2000. doi:10.1073/pnas.250494697. PMID 11114188. Bibcode: 2000PNAS...9714329Z. 
  16. ↑ "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor". Molecular and Cellular Biology 19 (11): 7816–27. November 1999. doi:10.1128/mcb.19.11.7816. PMID 10523670. 
  17. ↑ "Histone deacetylase 4 possesses intrinsic nuclear import and export signals". Molecular and Cellular Biology 21 (17): 5992–6005. September 2001. doi:10.1128/mcb.21.17.5992-6005.2001. PMID 11486037. 
  18. ↑ "HDAC4 deacetylase associates with and represses the MEF2 transcription factor". The EMBO Journal 18 (18): 5099–107. September 1999. doi:10.1093/emboj/18.18.5099. PMID 10487761. 
  19. ↑ "mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity". The Journal of Biological Chemistry 275 (20): 15594–9. May 2000. doi:10.1074/jbc.M908437199. PMID 10748098. https://hal.archives-ouvertes.fr/hal-00379796/file/Lemercier_JBC_2000.pdf. 
  20. ↑ 20.0 20.1 "Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway". Genes & Development 14 (1): 45–54. January 2000. doi:10.1101/gad.14.1.45. PMID 10640275. 
  21. ↑ "Interaction of nuclear receptor zinc finger DNA binding domains with histone deacetylase". Molecular and Cellular Endocrinology 206 (1–2): 1–12. August 2003. doi:10.1016/s0303-7207(03)00254-5. PMID 12943985. 
  22. ↑ "The orphan nuclear receptor TR2 interacts directly with both class I and class II histone deacetylases". Molecular Endocrinology 15 (8): 1318–28. August 2001. doi:10.1210/mend.15.8.0682. PMID 11463856. 
  23. ↑ "Differential localization of HDAC4 orchestrates muscle differentiation". Nucleic Acids Research 29 (16): 3439–47. August 2001. doi:10.1093/nar/29.16.3439. PMID 11504882. 
  24. ↑ "HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF". Oncogene 23 (54): 8777–84. November 2004. doi:10.1038/sj.onc.1208128. PMID 15467736. 

Further reading

External links

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



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