Histone deacetylase 5
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| Location (UCSC) | Chr 17: 44.08 – 44.12 Mb | Chr 11: 102.19 – 102.23 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
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Histone deacetylase 5 is an enzyme that in humans is encoded by the HDAC5 gene.[5][6][7]
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.[7]
AMP-activated protein kinase regulation of the glucose transporter GLUT4 occurs by phosphorylation of HDAC5.[8]
HDAC5 is involved in
HDAC inhibitors for the treatment of Alzheimer's disease should avoid targeting HDAC5.[9] Its function can be effectively examined by siRNA knockdown based on an independent validation.[10]
HDAC5 overexpression in
urothelial carcinoma cell lines inhibits long-term proliferation but can promote epithelial-to-mesenchymal transition (EMT)[11]
Interactions
Histone deacetylase 5 has been shown to
interact
with:
See also
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000108840 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000008855 – Ensembl, 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.
- ^ PMID 10220385.
- S2CID 916155.
- ^ a b "Entrez Gene: HDAC5 histone deacetylase 5".
- S2CID 17274354.
- PMID 22914591.
- PMID 27673562.
- PMID 31052182.
- ^ PMID 11929873.
- PMID 12242305.
- S2CID 24491249.
- ^ PMID 11931768.
- PMID 11804585.
- PMID 10869435.
- PMID 12015313.
- PMID 10748098.
- PMID 15060175.
- ^ PMID 10640275.
- PMID 15367659.
- S2CID 26092755.
Further reading
- Verdin E, Dequiedt F, Kasler HG (May 2003). "Class II histone deacetylases: versatile regulators" (PDF). Trends in Genetics. 19 (5): 286–93. PMID 12711221.
- 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. PMID 10640275.
- 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". The Journal of Biological Chemistry. 275 (20): 15594–9. PMID 10748098.
- 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. 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. PMID 10898795.
- PMID 11018260.
- 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. 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. PMID 11081517.
- 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. PMID 11114197.
- 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. PMID 11466315.
- McKinsey TA, Zhang CL, Olson EN (September 2001). "Identification of a signal-responsive nuclear export sequence in class II histone deacetylases". Molecular and Cellular Biology. 21 (18): 6312–21. PMID 11509672.
- Ozawa Y, Towatari M, Tsuzuki S, Hayakawa F, Maeda T, Miyata Y, et al. (October 2001). "Histone deacetylase 3 associates with and represses the transcription factor GATA-2". Blood. 98 (7): 2116–23. PMID 11567998.
- Potter GB, Beaudoin GM, DeRenzo CL, Zarach JM, Chen SH, Thompson CC (October 2001). "The hairless gene mutated in congenital hair loss disorders encodes a novel nuclear receptor corepressor". Genes & Development. 15 (20): 2687–701. PMID 11641275.
- 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. PMID 11804585.
- 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. PMID 11929873.
- Huang Y, Tan M, Gosink M, Wang KK, Sun Y (May 2002). "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. PMID 12019172.
External links
- HDAC5+protein,+human at the U.S. 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.
