HDAC4

Histone deacetylase 4
	; PDB rendering based on 2h8n.
Available structures
PDB	2H8N, 2O94, 2VQJ, 2VQM, 2VQO, 2VQQ, 2VQV, 2VQW
Identifiers
Symbols	HDAC4; AHO3; BDMR; HA6116; HD4; HDAC-A; HDACA; KIAA0288
External IDs	OMIM: 605314 MGI: 3036234 HomoloGene: 55946 GeneCards: HDAC4 Gene
EC number	3.5.1.98
Gene Ontology
Molecular function	• histone deacetylase activity; • protein binding; • transcription factor binding; • zinc ion binding; • hydrolase activity; • potassium ion binding; • NAD-dependent histone deacetylase activity (H3-K14 specific); • protein deacetylase activity; • activating transcription factor binding; • histone deacetylase activity (H3-K16 specific); • histone deacetylase binding; • sequence-specific DNA binding; • transcription regulatory region DNA binding; • NAD-dependent histone deacetylase activity (H3-K9 specific); • NAD-dependent histone deacetylase activity (H4-K16 specific); • repressing transcription factor binding;
Cellular component	• histone deacetylase complex; • nucleus; • cytoplasm; • cytosol; • transcriptional repressor complex; • Z disc; • neuromuscular junction; • A band; • actomyosin;
Biological process	• negative regulation of transcription from RNA polymerase II promoter; • negative regulation of transcription from RNA polymerase II promoter; • skeletal system development; • osteoblast development; • chromatin remodeling; • inflammatory response; • nervous system development; • positive regulation of cell proliferation; • negative regulation of cell proliferation; • negative regulation of myotube differentiation; • regulation of cardiac muscle contraction by calcium ion signaling; • response to denervation involved in regulation of muscle adaptation; • cardiac muscle hypertrophy in response to stress; • histone deacetylation; • histone deacetylation; • B cell differentiation; • positive regulation of protein sumoylation; • peptidyl-lysine deacetylation; • B cell activation; • response to drug; • regulation of protein binding; • negative regulation of sequence-specific DNA binding transcription factor activity; • negative regulation of osteoblast differentiation; • negative regulation of glycolysis; • negative regulation of transcription, DNA-dependent; • negative regulation of transcription, DNA-dependent; • positive regulation of transcription, DNA-dependent; • positive regulation of transcription from RNA polymerase II promoter; • positive regulation of transcription from RNA polymerase II promoter; • regulation of skeletal muscle fiber development; • positive regulation of sequence-specific DNA binding transcription factor activity; • response to interleukin-1; • histone H3 deacetylation; • histone H4 deacetylation;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs

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

[edit] 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]

[edit] 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]

[edit] See also

Histone deacetylase

[edit] Interactions

HDAC4 has been shown to interact with MEF2C,^[7]^[8] Zinc finger and BTB domain-containing protein 16,^[9]^[10] BCL6,^[10] CBX5,^[11] MAPK3,^[12] Testicular receptor 2,^[13]^[14] MAPK1,^[12] Myocyte-specific enhancer factor 2A,^[15]^[16] Nuclear receptor co-repressor 1,^[17]^[18] Nuclear receptor co-repressor 2,^[17]^[18] YWHAB,^[19] HDAC3,^[1]^[17]^[20]^[19] GATA1,^[21]BTG2, ^[22] and YWHAE.^[23]^[19]

[edit] References

^ ^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 21783. PMID 10220385. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=21783.
^ 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.
^ "Entrez Gene: HDAC4 histone deacetylase 4". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9759.
^ Glenisson W, Castronovo V, Waltregny D. (Oct 2007). "Histone deacetylase 4 is required for TGFbeta1-induced myofibroblastic differentiation.". Biochim Biophys Acta. 1773 (10): 1572–82. 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. PMID 19131628.
^ Wang, A H; Bertos N R, Vezmar M, Pelletier N, Crosato M, Heng H H, Th'ng J, Han J, Yang X J (Nov. 1999). "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor". Mol. Cell. Biol. (UNITED STATES) 19 (11): 7816–27. ISSN 0270-7306. PMC 84849. PMID 10523670. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84849.
^ Wang, A H; Yang X J (Sep. 2001). "Histone deacetylase 4 possesses intrinsic nuclear import and export signals". Mol. Cell. Biol. (United States) 21 (17): 5992–6005. doi:10.1128/MCB.21.17.5992-6005.2001. ISSN 0270-7306. PMC 87317. PMID 11486037. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=87317.
^ Chauchereau, Anne; Mathieu Marion, de Saintignon Julie, Ferreira Roger, Pritchard Linda L, Mishal Zohair, Dejean Anne, Harel-Bellan Annick (Nov. 2004). "HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF". Oncogene (England) 23 (54): 8777–84. doi:10.1038/sj.onc.1208128. ISSN 0950-9232. PMID 15467736.
^ ^a ^b Lemercier, Claudie; Brocard Marie-Paule, Puvion-Dutilleul Francine, Kao Hung-Ying, Albagli Olivier, Khochbin Saadi (Jun. 2002). "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor". J. Biol. Chem. (United States) 277 (24): 22045–52. doi:10.1074/jbc.M201736200. ISSN 0021-9258. PMID 11929873.
^ Zhang, Chun Li; McKinsey Timothy A, Olson Eric N (Oct. 2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation". Mol. Cell. Biol. (United States) 22 (20): 7302–12. doi:10.1128/MCB.22.20.7302-7312.2002. ISSN 0270-7306. PMC 139799. PMID 12242305. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139799.
^ ^a ^b Zhou, X; Richon V M, Wang A H, Yang X J, Rifkind R A, Marks P A (Dec. 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. (UNITED STATES) 97 (26): 14329–33. doi:10.1073/pnas.250494697. ISSN 0027-8424. PMC 18918. PMID 11114188. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18918.
^ Franco, Peter J; Li Guangjin, Wei Li-Na (Aug. 2003). "Interaction of nuclear receptor zinc finger DNA binding domains with histone deacetylase". Mol. Cell. Endocrinol. (Ireland) 206 (1-2): 1–12. doi:10.1016/S0303-7207(03)00254-5. ISSN 0303-7207. PMID 12943985.
^ Franco, P J; Farooqui M, Seto E, Wei L N (Aug. 2001). "The orphan nuclear receptor TR2 interacts directly with both class I and class II histone deacetylases". Mol. Endocrinol. (United States) 15 (8): 1318–28. doi:10.1210/me.15.8.1318. ISSN 0888-8809. PMID 11463856.
^ Miska, E A; Karlsson C, Langley E, Nielsen S J, Pines J, Kouzarides T (Sep. 1999). "HDAC4 deacetylase associates with and represses the MEF2 transcription factor". EMBO J. (ENGLAND) 18 (18): 5099–107. doi:10.1093/emboj/18.18.5099. ISSN 0261-4189. PMC 1171580. PMID 10487761. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171580.
^ Lemercier, C; Verdel A, Galloo B, Curtet S, Brocard M P, Khochbin S (May. 2000). "mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity". J. Biol. Chem. (UNITED STATES) 275 (20): 15594–9. doi:10.1074/jbc.M908437199. ISSN 0021-9258. PMID 10748098.
^ ^a ^b ^c Fischle, Wolfgang; Dequiedt Franck, Hendzel Michael J, Guenther Matthew G, Lazar Mitchell A, Voelter Wolfgang, Verdin Eric (Jan. 2002). "Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR". Mol. Cell (United States) 9 (1): 45–57. doi:10.1016/S1097-2765(01)00429-4. ISSN 1097-2765. PMID 11804585.
^ ^a ^b Huang, E Y; Zhang J, Miska E A, Guenther M G, Kouzarides T, Lazar M A (Jan. 2000). "Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway". Genes Dev. (UNITED STATES) 14 (1): 45–54. ISSN 0890-9369. PMC 316335. PMID 10640275. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316335.
^ ^a ^b ^c Grozinger, C M; Schreiber S L (Jul. 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. (UNITED STATES) 97 (14): 7835–40. doi:10.1073/pnas.140199597. ISSN 0027-8424. PMC 16631. PMID 10869435. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16631.
^ Fischle, W; Dequiedt F, Fillion M, Hendzel M J, Voelter W, Verdin E (Sep. 2001). "Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo". J. Biol. Chem. (United States) 276 (38): 35826–35. doi:10.1074/jbc.M104935200. ISSN 0021-9258. PMID 11466315.
^ Watamoto, Kouichi; Towatari Masayuki, Ozawa Yukiyasu, Miyata Yasuhiko, Okamoto Mitsunori, Abe Akihiro, Naoe Tomoki, Saito Hidehiko (Dec. 2003). "Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation". Oncogene (England) 22 (57): 9176–84. doi:10.1038/sj.onc.1206902. ISSN 0950-9232. PMID 14668799.
^ 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.
^ Miska, E A; Langley E, Wolf D, Karlsson C, Pines J, Kouzarides T (Aug. 2001). "Differential localization of HDAC4 orchestrates muscle differentiation". Nucleic Acids Res. (England) 29 (16): 3439–47. doi:10.1093/nar/29.16.3439. PMC 55849. PMID 11504882. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=55849.

[edit] Further reading

Pazin MJ, Kadonaga JT (1997). "What's up and down with histone deacetylation and transcription?". Cell 89 (3): 325–8. doi:10.1016/S0092-8674(00)80211-1. PMID 9150131.
Verdin E, Dequiedt F, Kasler HG (2003). "Class II histone deacetylases: versatile regulators.". Trends Genet. 19 (5): 286–93. doi:10.1016/S0168-9525(03)00073-8. PMID 12711221.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139146.
Wolffe AP (1997). "Transcriptional control. Sinful repression.". Nature 387 (6628): 16–7. doi:10.1038/387016a0. PMID 9139815.
Ohara O, Nagase T, Ishikawa K, et al. (1997). "Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins.". DNA Res. 4 (1): 53–9. doi:10.1093/dnares/4.1.53. PMID 9179496.
Fischle W, Emiliani S, Hendzel MJ, et al. (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.
Grozinger CM, Hassig CA, Schreiber SL (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 21783. PMID 10220385. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=21783.
Miska EA, Karlsson C, Langley E, et al. (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 1171580. PMID 10487761. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171580.
Wang AH, Bertos NR, Vezmar M, et al. (1999). "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor.". Mol. Cell. Biol. 19 (11): 7816–27. PMC 84849. PMID 10523670. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84849.
Youn HD, Grozinger CM, Liu JO (2000). "Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4.". J. Biol. Chem. 275 (29): 22563–7. doi:10.1074/jbc.C000304200. PMID 10825153.
Grozinger CM, Schreiber SL (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 16631. PMID 10869435. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16631.
Huynh KD, Fischle W, Verdin E, Bardwell VJ (2000). "BCoR, a novel corepressor involved in BCL-6 repression.". Genes Dev. 14 (14): 1810–23. doi:10.1101/gad.14.14.1810. PMC 316791. PMID 10898795. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316791.
Li J, Wang J, Wang J, et al. (2000). "Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3.". EMBO J. 19 (16): 4342–50. doi:10.1093/emboj/19.16.4342. PMC 302030. PMID 10944117. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=302030.
Wang AH, Kruhlak MJ, Wu J, et al. (2000). "Regulation of histone deacetylase 4 by binding of 14-3-3 proteins.". Mol. Cell. Biol. 20 (18): 6904–12. doi:10.1128/MCB.20.18.6904-6912.2000. PMC 88766. PMID 10958686. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=88766.
Zhang CL, McKinsey TA, Lu JR, Olson EN (2001). "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor.". J. Biol. Chem. 276 (1): 35–9. doi:10.1074/jbc.M007364200. PMID 11022042.
McKinsey TA, Zhang CL, Lu J, Olson EN (2000). "Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation.". Nature 408 (6808): 106–11. doi:10.1038/35040593. PMID 11081517.
Zhou X, Richon VM, Wang AH, et al. (2001). "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 18918. PMID 11114188. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18918.
McKinsey TA, Zhang CL, Olson EN (2001). "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.". Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14400–5. doi:10.1073/pnas.260501497. PMC 18930. PMID 11114197. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18930.

[edit] External links

MeSH HDAC4+protein,+human

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

[pmid10220385-0] 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 21783. PMID 10220385. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=21783.

[pmid10206986-1] 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.

[entrez-2] "Entrez Gene: HDAC4 histone deacetylase 4". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9759.

[3] Glenisson W, Castronovo V, Waltregny D. (Oct 2007). "Histone deacetylase 4 is required for TGFbeta1-induced myofibroblastic differentiation.". Biochim Biophys Acta. 1773 (10): 1572–82. PMID 17610967.

[4] Protein for Sight, Scientific American, 300, 3 (March 2009), p. 23

[pmid19131628-5] 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. PMID 19131628.

[pmid10523670-6] Wang, A H; Bertos N R, Vezmar M, Pelletier N, Crosato M, Heng H H, Th'ng J, Han J, Yang X J (Nov. 1999). "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor". Mol. Cell. Biol. (UNITED STATES) 19 (11): 7816–27. ISSN 0270-7306. PMC 84849. PMID 10523670. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84849.

[pmid11486037-7] Wang, A H; Yang X J (Sep. 2001). "Histone deacetylase 4 possesses intrinsic nuclear import and export signals". Mol. Cell. Biol. (United States) 21 (17): 5992–6005. doi:10.1128/MCB.21.17.5992-6005.2001. ISSN 0270-7306. PMC 87317. PMID 11486037. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=87317.

[pmid15467736-8] Chauchereau, Anne; Mathieu Marion, de Saintignon Julie, Ferreira Roger, Pritchard Linda L, Mishal Zohair, Dejean Anne, Harel-Bellan Annick (Nov. 2004). "HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF". Oncogene (England) 23 (54): 8777–84. doi:10.1038/sj.onc.1208128. ISSN 0950-9232. PMID 15467736.

[pmid11929873-9] Lemercier, Claudie; Brocard Marie-Paule, Puvion-Dutilleul Francine, Kao Hung-Ying, Albagli Olivier, Khochbin Saadi (Jun. 2002). "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor". J. Biol. Chem. (United States) 277 (24): 22045–52. doi:10.1074/jbc.M201736200. ISSN 0021-9258. PMID 11929873.

[pmid12242305-10] Zhang, Chun Li; McKinsey Timothy A, Olson Eric N (Oct. 2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation". Mol. Cell. Biol. (United States) 22 (20): 7302–12. doi:10.1128/MCB.22.20.7302-7312.2002. ISSN 0270-7306. PMC 139799. PMID 12242305. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139799.

[pmid11114188-11] Zhou, X; Richon V M, Wang A H, Yang X J, Rifkind R A, Marks P A (Dec. 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. (UNITED STATES) 97 (26): 14329–33. doi:10.1073/pnas.250494697. ISSN 0027-8424. PMC 18918. PMID 11114188. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18918.

[pmid12943985-12] Franco, Peter J; Li Guangjin, Wei Li-Na (Aug. 2003). "Interaction of nuclear receptor zinc finger DNA binding domains with histone deacetylase". Mol. Cell. Endocrinol. (Ireland) 206 (1-2): 1–12. doi:10.1016/S0303-7207(03)00254-5. ISSN 0303-7207. PMID 12943985.

[pmid11463856-13] Franco, P J; Farooqui M, Seto E, Wei L N (Aug. 2001). "The orphan nuclear receptor TR2 interacts directly with both class I and class II histone deacetylases". Mol. Endocrinol. (United States) 15 (8): 1318–28. doi:10.1210/me.15.8.1318. ISSN 0888-8809. PMID 11463856.

[pmid10487761-14] Miska, E A; Karlsson C, Langley E, Nielsen S J, Pines J, Kouzarides T (Sep. 1999). "HDAC4 deacetylase associates with and represses the MEF2 transcription factor". EMBO J. (ENGLAND) 18 (18): 5099–107. doi:10.1093/emboj/18.18.5099. ISSN 0261-4189. PMC 1171580. PMID 10487761. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171580.

[pmid10748098-15] Lemercier, C; Verdel A, Galloo B, Curtet S, Brocard M P, Khochbin S (May. 2000). "mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity". J. Biol. Chem. (UNITED STATES) 275 (20): 15594–9. doi:10.1074/jbc.M908437199. ISSN 0021-9258. PMID 10748098.

[pmid11804585-16] Fischle, Wolfgang; Dequiedt Franck, Hendzel Michael J, Guenther Matthew G, Lazar Mitchell A, Voelter Wolfgang, Verdin Eric (Jan. 2002). "Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR". Mol. Cell (United States) 9 (1): 45–57. doi:10.1016/S1097-2765(01)00429-4. ISSN 1097-2765. PMID 11804585.

[pmid10640275-17] Huang, E Y; Zhang J, Miska E A, Guenther M G, Kouzarides T, Lazar M A (Jan. 2000). "Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway". Genes Dev. (UNITED STATES) 14 (1): 45–54. ISSN 0890-9369. PMC 316335. PMID 10640275. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316335.

[pmid10869435-18] Grozinger, C M; Schreiber S L (Jul. 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. (UNITED STATES) 97 (14): 7835–40. doi:10.1073/pnas.140199597. ISSN 0027-8424. PMC 16631. PMID 10869435. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16631.

[pmid11466315-19] Fischle, W; Dequiedt F, Fillion M, Hendzel M J, Voelter W, Verdin E (Sep. 2001). "Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo". J. Biol. Chem. (United States) 276 (38): 35826–35. doi:10.1074/jbc.M104935200. ISSN 0021-9258. PMID 11466315.

[pmid14668799-20] Watamoto, Kouichi; Towatari Masayuki, Ozawa Yukiyasu, Miyata Yasuhiko, Okamoto Mitsunori, Abe Akihiro, Naoe Tomoki, Saito Hidehiko (Dec. 2003). "Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation". Oncogene (England) 22 (57): 9176–84. doi:10.1038/sj.onc.1206902. ISSN 0950-9232. PMID 14668799.

[pmid17371797-21] 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.

[pmid11504882-22] Miska, E A; Langley E, Wolf D, Karlsson C, Pines J, Kouzarides T (Aug. 2001). "Differential localization of HDAC4 orchestrates muscle differentiation". Nucleic Acids Res. (England) 29 (16): 3439–47. doi:10.1093/nar/29.16.3439. PMC 55849. PMID 11504882. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=55849.

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HDAC4

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[edit] Clinical significance

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