Histona deacetilasa 3

Histona deacetilasa 3
HUGO	4854
Símbolo	HDAC3
Símbolos alt.	RPD3; HD3; RPD3-2
Datos genéticos
Locus	Cr. 5 q31.3
Bases de datos
Entrez	8841
OMIM	605166
RefSeq	NP_003874
UniProt	O15379

La histona deacetilasa 3 (HDAC3) es una enzima codificada en humanos por el gen hdac3.^{[1] [2]}

Función

Las histonas juegan un papel crucial en la regulación de la transcripción, en la progresión del ciclo celular y en procesos de desarrollo. La acetilación/desacetilación de histonas altera la estructura del cromosoma, variando así la accesibilidad de los factores de transcripción al ADN. La HDAC3 pertenece a la familia de histona deacetilasas acuc/alfa. Esta proteína tiene actividad histona deacetilasa y reprime la transcripción cuando se une a los promotores diana. Podría participar en la regulación de la transcripción a través de su unión con el factor de transcripción con dedos de zinc YY1. HDAC3 también puede reprimir la función de p53 y así modular la proliferación celular y la apoptosis. El gen hdac3 es un potencial supresor tumoral.^[3]

Interacciones

La histona deacetilasa 3 ha demostrado ser capaz de interaccionar con:

• HDAC9^{[4] [5]}
• HDAC7A^[6]
• Proteína del retinoblastoma^{[7] [8]}
• RBBP4^[9]
• Receptor testicular^{[10] [11] [12]}
• MAP3K7IP2^[13]
• PPAR delta^{[11] [14]}
• GTF2I^{[15] [16]}
• HDAC5^{[17] [18] [19] [20]}
• RELA^[21]
• MAPK11^[22]
• TBL1X^{[19] [23]}
• NCOR1^{[24] [25] [18] [6] [19] [26] [27]}
• Ciclina D1^{[28] [29]}
• NCOR2^{[24] [25] [23] [18] [30] [26] [27]}
• ZBTB33^[24]
• SUV39H1^[31]
• PPAR gamma^{[11] [7]}
• TCP1^[30]
• HDAC4^{[17] [18] [6] [20]}
• CBFA2T3^{[32] [33]}
• GPS2^[19]
• YY1^{[34] [35]}
• RUNX2^[36]
• GATA1^[37]
• GATA2^[38]
• Proteína de la leucemia promielocítica^[39]
• Ubiquitina C.^[40]

Véase también

• Histona deacetilasa

Referencias

1. ↑ Emiliani S, Fischle W, Van Lint C, Al-Abed Y, Verdin E (Apr 1998). «Characterization of a human RPD3 ortholog, HDAC3». Proc Natl Acad Sci U S A 95 (6):  pp. 2795–800. PMID 9501169. 
2. ↑ Dangond F, Hafler DA, Tong JK, Randall J, Kojima R, Utku N, Gullans SR (Mar 1998). «Differential display cloning of a novel human histone deacetylase (HDAC3) cDNA from PHA-activated immune cells». Biochem Biophys Res Commun 242 (3):  pp. 648–52. doi:10.1006/bbrc.1997.8033. PMID 9464271. 
3. ↑ «Entrez Gene: HDAC3 histone deacetylase 3».
4. ↑ Petrie, Kevin; Guidez Fabien, Howell Louise, Healy Lyn, Waxman Samuel, Greaves Mel, Zelent Arthur (May. 2003). «The histone deacetylase 9 gene encodes multiple protein isoforms». J. Biol. Chem. (United States) 278 (18):  pp. 16059–72. doi:10.1074/jbc.M212935200. ISSN 0021-9258. PMID 12590135. 
5. ↑ Zhou, X; Richon V M, Rifkind R A, Marks P A (Feb. 2000). «Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (3):  pp. 1056–61. ISSN 0027-8424. PMID 10655483. 
6. ↑ ^{a b c} 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):  pp. 35826–35. doi:10.1074/jbc.M104935200. ISSN 0021-9258. PMID 11466315. 
7. ↑ ^{a b} Fajas, Lluis; Egler Viviane, Reiter Raphael, Hansen Jacob, Kristiansen Karsten, Debril Marie-Bernard, Miard Stéphanie, Auwerx Johan (Dec. 2002). «The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation». Dev. Cell (United States) 3 (6):  pp. 903–10. ISSN 1534-5807. PMID 12479814. 
8. ↑ Lai, A; Lee J M, Yang W M, DeCaprio J A, Kaelin W G, Seto E, Branton P E (Oct. 1999). «RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins». Mol. Cell. Biol. (UNITED STATES) 19 (10):  pp. 6632–41. ISSN 0270-7306. PMID 10490602. 
9. ↑ Nicolas, E; Ait-Si-Ali S, Trouche D (Aug. 2001). «The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein». Nucleic Acids Res. (England) 29 (15):  pp. 3131–6. PMID 11470869. 
10. ↑ Li, Guangjin; Franco Peter J, Wei Li-Na (Oct. 2003). «Identification of histone deacetylase-3 domains that interact with the orphan nuclear receptor TR2». Biochem. Biophys. Res. Commun. (United States) 310 (2):  pp. 384–90. ISSN 0006-291X. PMID 14521922. 
11. ↑ ^{a b c} 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):  pp. 1–12. ISSN 0303-7207. PMID 12943985. 
12. ↑ 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):  pp. 1318–28. ISSN 0888-8809. PMID 11463856. 
13. ↑ Baek, Sung Hee; Ohgi Kenneth A, Rose David W, Koo Edward H, Glass Christopher K, Rosenfeld Michael G (Jul. 2002). «Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein». Cell (United States) 110 (1):  pp. 55–67. ISSN 0092-8674. PMID 12150997. 
14. ↑ Shi, Yanhong; Hon Michelle, Evans Ronald M (Mar. 2002). «The peroxisome proliferator-activated receptor delta, an integrator of transcriptional repression and nuclear receptor signaling». Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (5):  pp. 2613–8. doi:10.1073/pnas.052707099. ISSN 0027-8424. PMID 11867749. 
15. ↑ Wen, Yu-Der; Cress W Douglas, Roy Ananda L, Seto Edward (Jan. 2003). «Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I». J. Biol. Chem. (United States) 278 (3):  pp. 1841–7. doi:10.1074/jbc.M206528200. ISSN 0021-9258. PMID 12393887. 
16. ↑ Tussié-Luna, María Isabel; Bayarsaihan Dashzeveg, Seto Edward, Ruddle Frank H, Roy Ananda L (Oct. 2002). «Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxbeta». Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (20):  pp. 12807–12. doi:10.1073/pnas.192464499. ISSN 0027-8424. PMID 12239342. 
17. ↑ ^{a b} Grozinger, C M; Hassig C A, Schreiber S L (Apr. 1999). «Three proteins define a class of human histone deacetylases related to yeast Hda1p». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (9):  pp. 4868–73. ISSN 0027-8424. PMID 10220385. 
18. ↑ ^{a b c d} 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):  pp. 45–57. ISSN 1097-2765. PMID 11804585. 
19. ↑ ^{a b c d} Zhang, Jinsong; Kalkum Markus, Chait Brian T, Roeder Robert G (Mar. 2002). «The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2». Mol. Cell (United States) 9 (3):  pp. 611–23. ISSN 1097-2765. PMID 11931768. 
20. ↑ ^{a b} 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):  pp. 7835–40. doi:10.1073/pnas.140199597. ISSN 0027-8424. PMID 10869435. 
21. ↑ Chen Lf; Fischle W, Verdin E, Greene W C (Aug. 2001). «Duration of nuclear NF-kappaB action regulated by reversible acetylation». Science (United States) 293 (5535):  pp. 1653–7. doi:10.1126/science.1062374. ISSN 0036-8075. PMID 11533489. 
22. ↑ Mahlknecht, Ulrich; Will Jutta, Varin Audrey, Hoelzer Dieter, Herbein Georges (Sep. 2004). «Histone deacetylase 3, a class I histone deacetylase, suppresses MAPK11-mediated activating transcription factor-2 activation and represses TNF gene expression». J. Immunol. (United States) 173 (6):  pp. 3979–90. ISSN 0022-1767. PMID 15356147. 
23. ↑ ^{a b} Guenther, M G; Lane W S, Fischle W, Verdin E, Lazar M A, Shiekhattar R (May. 2000). «A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness». Genes Dev. (UNITED STATES) 14 (9):  pp. 1048–57. ISSN 0890-9369. PMID 10809664. 
24. ↑ ^{a b c} Yoon, Ho-Geun; Chan Doug W, Reynolds Albert B, Qin Jun, Wong Jiemin (Sep. 2003). «N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso». Mol. Cell (United States) 12 (3):  pp. 723–34. ISSN 1097-2765. PMID 14527417. 
25. ↑ ^{a b} Yoon, Ho-Geun; Chan Doug W, Huang Zhi-Qing, Li Jiwen, Fondell Joseph D, Qin Jun, Wong Jiemin (Mar. 2003). «Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1». EMBO J. (England) 22 (6):  pp. 1336–46. doi:10.1093/emboj/cdg120. ISSN 0261-4189. PMID 12628926. 
26. ↑ ^{a b} Li, J; Wang J, Wang J, Nawaz Z, Liu J M, Qin J, Wong J (Aug. 2000). «Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3». EMBO J. (ENGLAND) 19 (16):  pp. 4342–50. doi:10.1093/emboj/19.16.4342. ISSN 0261-4189. PMID 10944117. 
27. ↑ ^{a b} Underhill, C; Qutob M S, Yee S P, Torchia J (Dec. 2000). «A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1». J. Biol. Chem. (UNITED STATES) 275 (51):  pp. 40463–70. doi:10.1074/jbc.M007864200. ISSN 0021-9258. PMID 11013263. 
28. ↑ Petre-Draviam, Christin E; Williams Erin B, Burd Craig J, Gladden Andrew, Moghadam Hamed, Meller Jaroslaw, Diehl J Alan, Knudsen Karen E (Jan. 2005). «A central domain of cyclin D1 mediates nuclear receptor corepressor activity». Oncogene (England) 24 (3):  pp. 431–44. doi:10.1038/sj.onc.1208200. ISSN 0950-9232. PMID 15558026. 
29. ↑ Lin, Huei-Min; Zhao Li, Cheng Sheue-Yann (Aug. 2002). «Cyclin D1 Is a Ligand-independent Co-repressor for Thyroid Hormone Receptors». J. Biol. Chem. (United States) 277 (32):  pp. 28733–41. doi:10.1074/jbc.M203380200. ISSN 0021-9258. PMID 12048199. 
30. ↑ ^{a b} Guenther, Matthew G; Yu Jiujiu, Kao Gary D, Yen Tim J, Lazar Mitchell A (Dec. 2002). «Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex». Genes Dev. (United States) 16 (24):  pp. 3130–5. doi:10.1101/gad.1037502. ISSN 0890-9369. PMID 12502735. 
31. ↑ Vaute, Olivier; Nicolas Estelle, Vandel Laurence, Trouche Didier (Jan. 2002). «Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases». Nucleic Acids Res. (England) 30 (2):  pp. 475–81. PMID 11788710. 
32. ↑ Hoogeveen, André T; Rossetti Stefano, Stoyanova Violeta, Schonkeren Joris, Fenaroli Angelia, Schiaffonati Luisa, van Unen Leontine, Sacchi Nicoletta (Sep. 2002). «The transcriptional corepressor MTG16a contains a novel nucleolar targeting sequence deranged in t (16; 21)-positive myeloid malignancies». Oncogene (England) 21 (43):  pp. 6703–12. doi:10.1038/sj.onc.1205882. ISSN 0950-9232. PMID 12242670. 
33. ↑ Amann, J M; Nip J, Strom D K, Lutterbach B, Harada H, Lenny N, Downing J R, Meyers S, Hiebert S W (Oct. 2001). «ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain». Mol. Cell. Biol. (United States) 21 (19):  pp. 6470–83. ISSN 0270-7306. PMID 11533236. 
34. ↑ Yang, W M; Yao Y L, Sun J M, Davie J R, Seto E (Oct. 1997). «Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family». J. Biol. Chem. (UNITED STATES) 272 (44):  pp. 28001–7. ISSN 0021-9258. PMID 9346952. 
35. ↑ Yao, Y L; Yang W M, Seto E (Sep. 2001). «Regulation of transcription factor YY1 by acetylation and deacetylation». Mol. Cell. Biol. (United States) 21 (17):  pp. 5979–91. ISSN 0270-7306. PMID 11486036. 
36. ↑ Schroeder, Tania M; Kahler Rachel A, Li Xiaodong, Westendorf Jennifer J (Oct. 2004). «Histone deacetylase 3 interacts with runx2 to repress the osteocalcin promoter and regulate osteoblast differentiation». J. Biol. Chem. (United States) 279 (40):  pp. 41998–2007. doi:10.1074/jbc.M403702200. ISSN 0021-9258. PMID 15292260. 
37. ↑ 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):  pp. 9176–84. doi:10.1038/sj.onc.1206902. ISSN 0950-9232. PMID 14668799. 
38. ↑ Ozawa, Y; Towatari M, Tsuzuki S, Hayakawa F, Maeda T, Miyata Y, Tanimoto M, Saito H (Oct. 2001). «Histone deacetylase 3 associates with and represses the transcription factor GATA-2». Blood (United States) 98 (7):  pp. 2116–23. ISSN 0006-4971. PMID 11567998. 
39. ↑ Wu, W S; Vallian S, Seto E, Yang W M, Edmondson D, Roth S, Chang K S (Apr. 2001). «The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases». Mol. Cell. Biol. (United States) 21 (7):  pp. 2259–68. doi:10.1128/MCB.21.7.2259-2268.2001. ISSN 0270-7306. PMID 11259576. 
40. ↑ Tan, Fengwei; Lu Lifang, Cai Yun, Wang Jinglan, Xie Yunfei, Wang Lin, Gong Yanhua, Xu Bing-E, Wu Jun, Luo Ying, Qiang Boqin, Yuan Jiangang, Sun Xiaoqing, Peng Xiaozhong (Jul. 2008). «Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells». Proteomics (Germany) 8 (14):  pp. 2885–96. doi:10.1002/pmic.200700887. PMID 18655026. 

Enlaces externos

• MeSH HDAC3+protein,+human