Biology:Histone deacetylase 5
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Histone deacetylase 5 is an enzyme that in humans is encoded by the HDAC5 gene.[1][2][3]
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 the class II histone deacetylase/acuc/apha family. It possesses histone deacetylase activity and represses transcription when tethered to a promoter. It coimmunoprecipitates only with HDAC3 family member and might form multicomplex proteins. It also interacts with myocyte enhancer factor-2 (MEF2) proteins, resulting in repression of MEF2-dependent genes. This gene is thought to be associated with colon cancer. Two transcript variants encoding different isoforms have been found for this gene.[3]
AMP-activated protein kinase regulation of the glucose transporter GLUT4 occurs by phosphorylation of HDAC5.[4]
HDAC5 is involved in memory consolidation and suggests that development of more selective HDAC inhibitors for the treatment of Alzheimer's disease should avoid targeting HDAC5.[5] Its function can be effectively examined by siRNA knockdown based on an independent validation.[6]
HDAC5 overexpression in urothelial carcinoma cell lines inhibits long-term proliferation but can promote epithelial-to-mesenchymal transition (EMT)[7]
Interactions
Histone deacetylase 5 has been shown to interact with:
- BCL6,[8]
- CBX5,[9]
- GATA1,[10]
- HDAC3,[1][11][12][13]
- IKZF1,[14]
- MEF2A,[15]
- NRIP1,[16]
- NCOR1,[11][17]
- NCOR2,[17]
- YWHAQ,[18] and
- ZBTB16.[8][19]
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.
- ↑ "Characterization of human colon cancer antigens recognized by autologous antibodies". International Journal of Cancer 76 (5): 652–8. May 1998. doi:10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P. PMID 9610721.
- ↑ 3.0 3.1 "Entrez Gene: HDAC5 histone deacetylase 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10014.
- ↑ "AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5". Diabetes 57 (4): 860–7. April 2008. doi:10.2337/db07-0843. PMID 18184930. http://diabetes.diabetesjournals.org/content/57/4/860.long.
- ↑ "Loss of HDAC5 impairs memory function: implications for Alzheimer's disease". Journal of Alzheimer's Disease 33 (1): 35–44. January 2013. doi:10.3233/JAD-2012-121009. PMID 22914591.
- ↑ "Validation of RNAi Silencing Efficiency Using Gene Array Data shows 18.5% Failure Rate across 429 Independent Experiments" (in en). Molecular Therapy: Nucleic Acids 5 (9): e366. September 2016. doi:10.1038/mtna.2016.66. PMID 27673562.
- ↑ "HDAC5 Expression in Urothelial Carcinoma Cell Lines Inhibits Long-Term Proliferation but Can Promote Epithelial-to-Mesenchymal Transition". International Journal of Molecular Sciences 20 (9): 2135. April 2019. doi:10.3390/ijms20092135. PMID 31052182.
- ↑ 8.0 8.1 "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.
- ↑ "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.
- ↑ 11.0 11.1 "The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2". Molecular Cell 9 (3): 611–23. March 2002. doi:10.1016/S1097-2765(02)00468-9. PMID 11931768.
- ↑ "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.
- ↑ "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.
- ↑ "A molecular dissection of the repression circuitry of Ikaros". The Journal of Biological Chemistry 277 (31): 27697–705. August 2002. doi:10.1074/jbc.M201694200. PMID 12015313.
- ↑ "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.
- ↑ "Multiple domains of the Receptor-Interacting Protein 140 contribute to transcription inhibition". Nucleic Acids Research 32 (6): 1957–66. 2004. doi:10.1093/nar/gkh524. PMID 15060175.
- ↑ 17.0 17.1 "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.
- ↑ "Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5". Molecular and Cellular Biology 24 (19): 8374–85. October 2004. doi:10.1128/MCB.24.19.8374-8385.2004. PMID 15367659.
- ↑ "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
- "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. http://orbi.ulg.ac.be/bitstream/2268/80861/1/TGI2003.pdf.
- "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.
- "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.
- "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.
- "Chromosomal organization and localization of the human histone deacetylase 5 gene (HDAC5)". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1493 (3): 342–8. October 2000. doi:10.1016/S0167-4781(00)00191-3. PMID 11018260.
- "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.
- "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.
- "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.
- "Identification of a signal-responsive nuclear export sequence in class II histone deacetylases". Molecular and Cellular Biology 21 (18): 6312–21. September 2001. doi:10.1128/MCB.21.18.6312-6321.2001. PMID 11509672.
- "Histone deacetylase 3 associates with and represses the transcription factor GATA-2". Blood 98 (7): 2116–23. October 2001. doi:10.1182/blood.V98.7.2116. PMID 11567998.
- "The hairless gene mutated in congenital hair loss disorders encodes a novel nuclear receptor corepressor". Genes & Development 15 (20): 2687–701. October 2001. doi:10.1101/gad.916701. PMID 11641275.
- "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.
- "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.
- "Histone deacetylase 5 is not a p53 target gene, but its overexpression inhibits tumor cell growth and induces apoptosis". Cancer Research 62 (10): 2913–22. May 2002. PMID 12019172.
External links
- HDAC5+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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