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:
- BCL6,[7]
- BTG2,[8][9]
- CBX5,[10]
- GATA1,[11]
- HDAC3,[1][12][13][14]
- MAPK1,[15]
- MAPK3,[15]
- MEF2C,[16][17]
- Myocyte-specific enhancer factor 2A,[18][19]
- Nuclear receptor co-repressor 1,[12][20]
- Nuclear receptor co-repressor 2,[12][20]
- Testicular receptor 2,[21][22]
- YWHAB,[13]
- YWHAE,[13][23] and
- Zinc finger and BTB domain-containing protein 16.[7][24]
See also
References
- ↑ 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.
- ↑ "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.
- ↑ "Entrez Gene: HDAC4 histone deacetylase 4". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9759.
- ↑ "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.
- ↑ Protein for Sight, Scientific American, 300, 3 (March 2009), p. 23
- ↑ "HDAC4 regulates neuronal survival in normal and diseased retinas". Science 323 (5911): 256–9. January 2009. doi:10.1126/science.1166226. PMID 19131628.
- ↑ 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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ 12.0 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.
- ↑ 13.0 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.
- ↑ "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.
- ↑ 15.0 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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ 20.0 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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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
- "What's up and down with histone deacetylation and transcription?". Cell 89 (3): 325–8. May 1997. doi:10.1016/S0092-8674(00)80211-1. PMID 9150131.
- "Class II histone deacetylases: versatile regulators". Trends in Genetics 19 (5): 286–93. May 2003. doi:10.1016/S0168-9525(03)00073-8. PMID 12711221.
- "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry 236 (1): 107–13. April 1996. doi:10.1006/abio.1996.0138. PMID 8619474.
- "Large-scale concatenation cDNA sequencing". Genome Research 7 (4): 353–8. April 1997. doi:10.1101/gr.7.4.353. PMID 9110174.
- "Transcriptional control. Sinful repression". Nature 387 (6628): 16–7. May 1997. doi:10.1038/387016a0. PMID 9139815. https://zenodo.org/record/1233198.
- "Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins". DNA Research 4 (1): 53–9. February 1997. doi:10.1093/dnares/4.1.53. PMID 9179496.
- "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.
- "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.
- "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.
- "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.
- "Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4". The Journal of Biological Chemistry 275 (29): 22563–7. July 2000. doi:10.1074/jbc.C000304200. PMID 10825153.
- "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.
- "BCoR, a novel corepressor involved in BCL-6 repression". Genes & Development 14 (14): 1810–23. July 2000. doi:10.1101/gad.14.14.1810. PMID 10898795.
- "Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3". The EMBO Journal 19 (16): 4342–50. August 2000. doi:10.1093/emboj/19.16.4342. PMID 10944117.
- "Regulation of histone deacetylase 4 by binding of 14-3-3 proteins". Molecular and Cellular Biology 20 (18): 6904–12. September 2000. doi:10.1128/MCB.20.18.6904-6912.2000. PMID 10958686.
- "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor". The Journal of Biological Chemistry 276 (1): 35–9. January 2001. doi:10.1074/jbc.M007364200. PMID 11022042.
- "Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation". Nature 408 (6808): 106–11. November 2000. doi:10.1038/35040593. PMID 11081517. Bibcode: 2000Natur.408..106M.
- "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.
- "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". Proceedings of the National Academy of Sciences of the United States of America 97 (26): 14400–5. December 2000. doi:10.1073/pnas.260501497. PMID 11114197. Bibcode: 2000PNAS...9714400M.
External links
- HDAC4+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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