Histone deacetylase 5: Difference between revisions

HDAC5
Identifiers
Aliases	HDAC5, HD5, NY-CO-9, histone deacetylase 5
External IDs	OMIM: 605315; MGI: 1333784; HomoloGene: 3995; GeneCards: HDAC5; OMA:HDAC5 - orthologs
Gene location (Human)
Chr.	Chromosome 17 (human)
End	44,123,702 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	102,230,166 bp
RNA expression pattern
	Top expressed in
	skin of leg; ; skin of abdomen; ; ganglionic eminence; ; muscle of thigh; ; right frontal lobe; ; popliteal artery; ; tibial arteries; ; right hemisphere of cerebellum; ; apex of heart; ; gastric mucosa;
	Top expressed in
	neural layer of retina; ; perirhinal cortex; ; entorhinal cortex; ; CA3 field; ; primary visual cortex; ; dentate gyrus of hippocampal formation granule cell; ; superior frontal gyrus; ; lip; ; muscle of thigh; ; central gray substance of midbrain;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	NAD-dependent histone deacetylase activity (H3-K14 specific); protein deacetylase activity; histone deacetylase binding; chromatin binding; metal ion binding; protein binding; hydrolase activity; protein kinase C binding; histone deacetylase activity; transcription factor binding; RNA polymerase II cis-regulatory region sequence-specific DNA binding;
Cellular component	Golgi apparatus; histone deacetylase complex; cytoplasm; nucleus; nucleoplasm; cytosol; nuclear speck; protein-containing complex;
Biological process	histone H3 deacetylation; chromatin remodeling; regulation of myotube differentiation; regulation of transcription, DNA-templated; regulation of gene expression, epigenetic; positive regulation of DNA-binding transcription factor activity; regulation of histone H3-K9 acetylation; response to activity; transcription, DNA-templated; protein deacetylation; negative regulation of cell migration involved in sprouting angiogenesis; B cell activation; neuron differentiation; negative regulation of myotube differentiation; cellular response to insulin stimulus; B cell differentiation; inflammatory response; regulation of protein binding; negative regulation of transcription, DNA-templated; cellular response to lipopolysaccharide; positive regulation of transcription by RNA polymerase II; response to cocaine; negative regulation of transcription by RNA polymerase II; histone deacetylation; chromatin organization;
	Sources:Amigo / QuickGO
Orthologs
	10014
	15184
	ENSG00000108840
	ENSMUSG00000008855
	Q9UQL6
	Q9Z2V6
	NM_001015053; NM_005474; NM_139205; NM_001382393
NM_001077696; NM_001284248; NM_001284249; NM_001284250; NM_010412;
	NM_001361596
	NP_001015053; NP_005465; NP_001369322
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

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Revision as of 03:05, 19 January 2021

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 memory consolidation and suggests that development of more selective 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:

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.
^ ^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.
^ Scanlan MJ, Chen YT, Williamson B, Gure AO, Stockert E, Gordan JD, et al. (May 1998). "Characterization of human colon cancer antigens recognized by autologous antibodies". International Journal of Cancer. 76 (5): 652–8. doi:10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P. PMID 9610721.
^ ^a ^b "Entrez Gene: HDAC5 histone deacetylase 5".
^ McGee SL, van Denderen BJ, Howlett KF, Mollica J, Schertzer JD, Kemp BE, Hargreaves M (April 2008). "AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5". Diabetes. 57 (4): 860–7. doi:10.2337/db07-0843. PMID 18184930. S2CID 17274354.
^ Agis-Balboa RC, Pavelka Z, Kerimoglu C, Fischer A (January 2013). "Loss of HDAC5 impairs memory function: implications for Alzheimer's disease". Journal of Alzheimer's Disease. 33 (1): 35–44. doi:10.3233/JAD-2012-121009. hdl:2434/223089. PMID 22914591.
^ Munkácsy G, Sztupinszki Z, Herman P, Bán B, Pénzváltó Z, Szarvas N, Győrffy B (September 2016). "Validation of RNAi Silencing Efficiency Using Gene Array Data shows 18.5% Failure Rate across 429 Independent Experiments". Molecular Therapy. Nucleic Acids. 5 (9): e366. doi:10.1038/mtna.2016.66. PMC 5056990. PMID 27673562.
^ Jaguva Vasudevan AA, Hoffmann MJ, Beck ML, Poschmann G, Petzsch P, Wiek C, et al. (April 2019). "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. doi:10.3390/ijms20092135. PMC 6539474. PMID 31052182.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ ^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.
^ 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, et al. (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 Zhang J, Kalkum M, Chait BT, Roeder RG (March 2002). "The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2". Molecular Cell. 9 (3): 611–23. doi:10.1016/S1097-2765(02)00468-9. PMID 11931768.
^ 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.
^ 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.
^ Koipally J, Georgopoulos K (August 2002). "A molecular dissection of the repression circuitry of Ikaros". The Journal of Biological Chemistry. 277 (31): 27697–705. doi:10.1074/jbc.M201694200. PMID 12015313.
^ 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. doi:10.1074/jbc.M908437199. PMID 10748098.
^ Castet A, Boulahtouf A, Versini G, Bonnet S, Augereau P, Vignon F, et al. (2004). "Multiple domains of the Receptor-Interacting Protein 140 contribute to transcription inhibition". Nucleic Acids Research. 32 (6): 1957–66. doi:10.1093/nar/gkh524. PMC 390375. PMID 15060175.
^ ^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. PMC 316335. PMID 10640275.
^ Vega RB, Harrison BC, Meadows E, Roberts CR, Papst PJ, Olson EN, McKinsey TA (October 2004). "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. doi:10.1128/MCB.24.19.8374-8385.2004. PMC 516754. PMID 15367659.
^ Chauchereau A, Mathieu M, de Saintignon J, Ferreira R, Pritchard LL, Mishal Z, et al. (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.

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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000108840 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000008855 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10220385-5] 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.

[pmid9610721-6] Scanlan MJ, Chen YT, Williamson B, Gure AO, Stockert E, Gordan JD, et al. (May 1998). "Characterization of human colon cancer antigens recognized by autologous antibodies". International Journal of Cancer. 76 (5): 652–8. doi:10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P. PMID 9610721.

[entrez-7] "Entrez Gene: HDAC5 histone deacetylase 5".

[8] McGee SL, van Denderen BJ, Howlett KF, Mollica J, Schertzer JD, Kemp BE, Hargreaves M (April 2008). "AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5". Diabetes. 57 (4): 860–7. doi:10.2337/db07-0843. PMID 18184930. S2CID 17274354.

[pmid22914591-9] Agis-Balboa RC, Pavelka Z, Kerimoglu C, Fischer A (January 2013). "Loss of HDAC5 impairs memory function: implications for Alzheimer's disease". Journal of Alzheimer's Disease. 33 (1): 35–44. doi:10.3233/JAD-2012-121009. hdl:2434/223089. PMID 22914591.

[10] Munkácsy G, Sztupinszki Z, Herman P, Bán B, Pénzváltó Z, Szarvas N, Győrffy B (September 2016). "Validation of RNAi Silencing Efficiency Using Gene Array Data shows 18.5% Failure Rate across 429 Independent Experiments". Molecular Therapy. Nucleic Acids. 5 (9): e366. doi:10.1038/mtna.2016.66. PMC 5056990. PMID 27673562.

[11] Jaguva Vasudevan AA, Hoffmann MJ, Beck ML, Poschmann G, Petzsch P, Wiek C, et al. (April 2019). "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. doi:10.3390/ijms20092135. PMC 6539474. PMID 31052182.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[pmid11929873-12] 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.

[pmid12242305-13] 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.

[pmid14668799-14] Watamoto K, Towatari M, Ozawa Y, Miyata Y, Okamoto M, Abe A, et al. (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.

[pmid11931768-15] Zhang J, Kalkum M, Chait BT, Roeder RG (March 2002). "The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2". Molecular Cell. 9 (3): 611–23. doi:10.1016/S1097-2765(02)00468-9. PMID 11931768.

[pmid11804585-16] 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.

[pmid10869435-17] 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.

[pmid12015313-18] Koipally J, Georgopoulos K (August 2002). "A molecular dissection of the repression circuitry of Ikaros". The Journal of Biological Chemistry. 277 (31): 27697–705. doi:10.1074/jbc.M201694200. PMID 12015313.

[pmid10748098-19] 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. doi:10.1074/jbc.M908437199. PMID 10748098.

[pmid15060175-20] Castet A, Boulahtouf A, Versini G, Bonnet S, Augereau P, Vignon F, et al. (2004). "Multiple domains of the Receptor-Interacting Protein 140 contribute to transcription inhibition". Nucleic Acids Research. 32 (6): 1957–66. doi:10.1093/nar/gkh524. PMC 390375. PMID 15060175.

[pmid10640275-21] 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. PMC 316335. PMID 10640275.

[pmid15367659-22] Vega RB, Harrison BC, Meadows E, Roberts CR, Papst PJ, Olson EN, McKinsey TA (October 2004). "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. doi:10.1128/MCB.24.19.8374-8385.2004. PMC 516754. PMID 15367659.

[pmid15467736-23] Chauchereau A, Mathieu M, de Saintignon J, Ferreira R, Pritchard LL, Mishal Z, et al. (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.

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 * {{cite journal | vauthors = Lemercier C, Verdel A, Galloo B, Curtet S, Brocard MP, Khochbin S | title = mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity | journal = The Journal of Biological Chemistry | volume = 275 | issue = 20 | pages = 15594–9 | date = May 2000 | pmid = 10748098 | doi = 10.1074/jbc.M908437199 | doi-access = free }}
 * {{cite journal | vauthors = Grozinger CM, Schreiber SL | title = Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 14 | pages = 7835–40 | date = July 2000 | pmid = 10869435 | pmc = 16631 | doi = 10.1073/pnas.140199597 | bibcode = 2000PNAS...97.7835G }}
-* {{cite journal | vauthors = Huynh KD, Fischle W, Verdin E, Bardwell VJ | title = BCoR, a novel corepressor involved in BCL-6 repression | journal = Genes & Development | volume = 14 | issue = 14 | pages = 1810–23 | date = July 2000 | pmid = 10898795 | pmc = 316791 | doi = 10.1101/gad.14.14.1810 | doi-broken-date = 2020-12-11 }}
+* {{cite journal | vauthors = Huynh KD, Fischle W, Verdin E, Bardwell VJ | title = BCoR, a novel corepressor involved in BCL-6 repression | journal = Genes & Development | volume = 14 | issue = 14 | pages = 1810–23 | date = July 2000 | pmid = 10898795 | pmc = 316791 | doi = 10.1101/gad.14.14.1810 | doi-broken-date = 2021-01-19 }}
 * {{cite journal | vauthors = Mahlknecht U, Schnittger S, Ottmann OG, Schoch C, Mosebach M, Hiddemann W, Hoelzer D | title = Chromosomal organization and localization of the human histone deacetylase 5 gene (HDAC5) | journal = Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression | volume = 1493 | issue = 3 | pages = 342–8 | date = October 2000 | pmid = 11018260 | doi = 10.1016/S0167-4781(00)00191-3 | author-link = Mahlknecht U }}
 * {{cite journal | vauthors = Zhang CL, McKinsey TA, Lu JR, Olson EN | title = Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor | journal = The Journal of Biological Chemistry | volume = 276 | issue = 1 | pages = 35–9 | date = January 2001 | pmid = 11022042 | doi = 10.1074/jbc.M007364200 | doi-access = free }}

v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase
3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase
3.5.5: Nitriles/ Aminohydrolases	Nitrilase
3.5.99: Other	Riboflavinase Thiaminase II

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)