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Contents

   



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1 Function  





2 Clinical significance  





3 Interactions  





4 See also  





5 References  





6 Further reading  





7 External links  














HDAC4






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HDAC4
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesHDAC4, AHO3, BDMR, HA6116, HD4, HDAC-4, HDAC-A, HDACA, histone deacetylase 4, NEDCHID
External IDsOMIM: 605314; MGI: 3036234; HomoloGene: 55946; GeneCards: HDAC4; OMA:HDAC4 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006037
NM_001378414
NM_001378415
NM_001378416
NM_001378417

NM_207225

RefSeq (protein)

NP_006028
NP_001365343
NP_001365344
NP_001365345
NP_001365346

NP_997108

Location (UCSC)Chr 2: 239.05 – 239.4 MbChr 1: 91.86 – 92.12 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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:

  • BTG2,[12][13]
  • CBX5,[14]
  • GATA1,[15]
  • HDAC3,[5][16][17][18]
  • MAPK1,[19]
  • MAPK3,[19]
  • MEF2C,[20][21]
  • Myocyte-specific enhancer factor 2A,[22][23]
  • Nuclear receptor co-repressor 1,[16][24]
  • Nuclear receptor co-repressor 2,[16][24]
  • Testicular receptor 2,[25][26]
  • YWHAB,[17]
  • YWHAE,[17][27] and
  • Zinc finger and BTB domain-containing protein 16.[11][28]
  • See also[edit]

    References[edit]

  • ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026313Ensembl, May 2017
  • ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ 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. Bibcode:1999PNAS...96.4868G. doi:10.1073/pnas.96.9.4868. PMC 21783. PMID 10220385.
  • ^ 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. doi:10.1074/jbc.274.17.11713. PMID 10206986.
  • ^ "Entrez Gene: HDAC4 histone deacetylase 4".
  • ^ Glenisson W, Castronovo V, Waltregny D (October 2007). "Histone deacetylase 4 is required for TGFbeta1-induced myofibroblastic differentiation". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1773 (10): 1572–82. doi:10.1016/j.bbamcr.2007.05.016. PMID 17610967.
  • ^ Protein for Sight, Scientific American, 300, 3 (March 2009), p. 23
  • ^ 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 3339762. PMID 19131628.
  • ^ 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. doi:10.1074/jbc.M201736200. PMID 11929873.
  • ^ 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. doi:10.1096/fj.06-7548com. PMID 17371797. S2CID 4974360.
  • ^ 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. doi:10.1002/jcp.25467. PMID 27333946. S2CID 4070837.
  • ^ 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. doi:10.1128/mcb.22.20.7302-7312.2002. PMC 139799. PMID 12242305.
  • ^ 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.
  • ^ 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. doi:10.1016/s1097-2765(01)00429-4. hdl:11858/00-001M-0000-002C-9FF9-9. PMID 11804585.
  • ^ 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. Bibcode:2000PNAS...97.7835G. doi:10.1073/pnas.140199597. PMC 16631. PMID 10869435.
  • ^ 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. doi:10.1074/jbc.M104935200. PMID 11466315.
  • ^ 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. Bibcode:2000PNAS...9714329Z. doi:10.1073/pnas.250494697. PMC 18918. PMID 11114188.
  • ^ 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. doi:10.1128/mcb.19.11.7816. PMC 84849. PMID 10523670.
  • ^ Wang AH, Yang XJ (September 2001). "Histone deacetylase 4 possesses intrinsic nuclear import and export signals". Molecular and Cellular Biology. 21 (17): 5992–6005. doi:10.1128/mcb.21.17.5992-6005.2001. PMC 87317. PMID 11486037.
  • ^ 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. doi:10.1093/emboj/18.18.5099. PMC 1171580. PMID 10487761.
  • ^ 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" (PDF). The Journal of Biological Chemistry. 275 (20): 15594–9. doi:10.1074/jbc.M908437199. PMID 10748098. S2CID 39220205.
  • ^ 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. doi:10.1101/gad.14.1.45. PMC 316335. PMID 10640275.
  • ^ 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. doi:10.1016/s0303-7207(03)00254-5. PMID 12943985. S2CID 19487189.
  • ^ 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. doi:10.1210/mend.15.8.0682. PMID 11463856.
  • ^ 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. doi:10.1093/nar/29.16.3439. PMC 55849. PMID 11504882.
  • ^ 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]

  • Verdin E, Dequiedt F, Kasler HG (May 2003). "Class II histone deacetylases: versatile regulators". Trends in Genetics. 19 (5): 286–93. doi:10.1016/S0168-9525(03)00073-8. hdl:2268/80861. PMID 12711221.
  • Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
  • Wolffe AP (May 1997). "Transcriptional control. Sinful repression". Nature. 387 (6628): 16–7. doi:10.1038/387016a0. PMID 9139815. S2CID 29803420.
  • Ohara O, Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Nomura N (February 1997). "Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins". DNA Research. 4 (1): 53–9. doi:10.1093/dnares/4.1.53. PMID 9179496.
  • 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. doi:10.1074/jbc.274.17.11713. PMID 10206986.
  • 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. Bibcode:1999PNAS...96.4868G. doi:10.1073/pnas.96.9.4868. PMC 21783. PMID 10220385.
  • 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. doi:10.1093/emboj/18.18.5099. PMC 1171580. PMID 10487761.
  • 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. doi:10.1128/mcb.19.11.7816. PMC 84849. PMID 10523670.
  • Youn HD, Grozinger CM, Liu JO (July 2000). "Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4". The Journal of Biological Chemistry. 275 (29): 22563–7. doi:10.1074/jbc.C000304200. PMID 10825153.
  • 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. Bibcode:2000PNAS...97.7835G. doi:10.1073/pnas.140199597. PMC 16631. PMID 10869435.
  • Huynh KD, Fischle W, Verdin E, Bardwell VJ (July 2000). "BCoR, a novel corepressor involved in BCL-6 repression". Genes & Development. 14 (14): 1810–23. doi:10.1101/gad.14.14.1810. PMC 316791. PMID 10898795.
  • Li J, Wang J, Wang J, Nawaz Z, Liu JM, Qin J, Wong J (August 2000). "Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3". The EMBO Journal. 19 (16): 4342–50. doi:10.1093/emboj/19.16.4342. PMC 302030. PMID 10944117.
  • Wang AH, Kruhlak MJ, Wu J, Bertos NR, Vezmar M, Posner BI, Bazett-Jones DP, Yang XJ (September 2000). "Regulation of histone deacetylase 4 by binding of 14-3-3 proteins". Molecular and Cellular Biology. 20 (18): 6904–12. doi:10.1128/MCB.20.18.6904-6912.2000. PMC 88766. PMID 10958686.
  • Zhang CL, McKinsey TA, Lu JR, Olson EN (January 2001). "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. doi:10.1074/jbc.M007364200. PMID 11022042.
  • McKinsey TA, Zhang CL, Lu J, Olson EN (November 2000). "Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation". Nature. 408 (6808): 106–11. Bibcode:2000Natur.408..106M. doi:10.1038/35040593. PMC 4459600. PMID 11081517.
  • 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. Bibcode:2000PNAS...9714329Z. doi:10.1073/pnas.250494697. PMC 18918. PMID 11114188.
  • McKinsey TA, Zhang CL, Olson EN (December 2000). "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. Bibcode:2000PNAS...9714400M. doi:10.1073/pnas.260501497. PMC 18930. PMID 11114197.
  • External links[edit]

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


    Retrieved from "https://en.wikipedia.org/w/index.php?title=HDAC4&oldid=1189371786"

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