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HDAC6

January 01, 1970

Histone deacetylase 6 is an enzyme that in humans is encoded by the HDAC6 gene.[5][6] HDAC6 has emerged as a highly promising candidate to selectively inhibit as a therapeutic strategy to combat several types of cancer and neurodegenerative disorders.[7]

HDAC6
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesHDAC6, CPBHM, HD6, PPP1R90, JM21, histone deacetylase 6
External IDsOMIM: 300272; MGI: 1333752; HomoloGene: 31353; GeneCards: HDAC6; OMA:HDAC6 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

10013

15185

Ensembl

ENSG00000094631

ENSMUSG00000031161

UniProt

Q9UBN7

Q9Z2V5

RefSeq (mRNA)

NM_001130416
NM_010413

RefSeq (protein)

NP_001123888
NP_034543

Location (UCSC)Chr X: 48.8 – 48.82 MbChr X: 7.8 – 7.81 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function edit

Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromatin structure and affects transcription. The protein encoded by this gene belongs to class II of the histone deacetylase/acuc/apha family. It contains an internal duplication of two catalytic domains that appear to function independently of each other. This protein possesses histone deacetylase activity and represses transcription.[8]

It retracts the cilium of the cell, which is necessary prior to mitosis. [9]

HDAC encourages cell motility and catalyzes α-tubulin deacetylation.[10] As a result the enzyme encourages cancer cell metastasis.[11]

HDAC6 affects transcription and translation by regulating heat-shock protein 90 (Hsp90).

HDAC6 is required in the formation of stress granule (SG) proteins and is instrumental in SG formation; pharmacological inhibition or genetic removal of HDAC6 abolished SG formation.[11]

HDAC6 bonds with high affinity to ubiquitinated proteins.[12]

HDAC6 is involved in leptin sensitivity.[13]

HDAC6 deacetylates tyrosine residue T178 on TAK1.[14]

Clinical relevance edit

Mutations in this gene have been associated to Alzheimer's disease.[15]

Over expression of this protein correlates with tumorigenesis and cell survival. HDAC6 also encourages metastasis of cancer cells.[11]

Since HDAC6 is dysregulated and/or implicated in several cancers and neurodegenerative disorders, pharmacological inhibition of this specific enzyme holds great therapeutic potential and could also limit side effects associated with pan-inhibitors of multiple HDAC enzymes.[7] Selective inhibition of HDAC6 as a strategy to treat cancers is however also subject of debate, since some HDAC6 inhibitors exhibited anti-tumor activity in vitro and in vivo only when administered in high concentrations, which also produced off-target effects. The findings suggest that further study is needed to clarify data on anti-cancer effects of selective HDAC6 inhibitors.[16]

Interactions edit

HDAC6 has been shown to interact with HDAC11[17] and Zinc finger and BTB domain-containing protein 16.[18]

HDAC6 interacts with SG (Stress granule) protein G3BP1.[12]

See also edit

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000094631 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031161 – 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.
  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): 4868–4873. Bibcode:1999PNAS...96.4868G. doi:10.1073/pnas.96.9.4868. PMC 21783. PMID 10220385.
  6. ^ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, et al. (December 1998). "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 5 (6): 355–364. doi:10.1093/dnares/5.6.355. PMID 10048485.
  7. ^ a b Geurs S, Clarisse D, Baele F, Franceus J, Desmet T, De Bosscher K, D'hooghe M (May 2022). "Identification of mercaptoacetamide-based HDAC6 inhibitors via a lean inhibitor strategy: screening, synthesis, and biological evaluation". Chemical Communications. 58 (42): 6239–6242. doi:10.1039/D2CC01550A. hdl:1854/LU-8752799. PMID 35510683. S2CID 248527466.
  8. ^ "Entrez Gene: HDAC6 histone deacetylase 6".
  9. ^ Krishnamurthy K, Wang G, Silva J, Condie BG, Bieberich E (February 2007). "Ceramide regulates atypical PKCzeta/lambda-mediated cell polarity in primitive ectoderm cells. A novel function of sphingolipids in morphogenesis". The Journal of Biological Chemistry. 282 (5): 3379–3390. doi:10.1074/jbc.M607779200. PMID 17105725.*Lay summary in: "Lipid helps cells find their way by keeping their 'antennae' up". phys.org/news. July 9, 2012.
  10. ^ Gao YS, Hubbert CC, Lu J, Lee YS, Lee JY, Yao TP (December 2007). "Histone deacetylase 6 regulates growth factor-induced actin remodeling and endocytosis". Molecular and Cellular Biology. 27 (24): 8637–8647. doi:10.1128/MCB.00393-07. PMC 2169396. PMID 17938201.
  11. ^ a b c Aldana-Masangkay GI, Sakamoto KM (2011). "The role of HDAC6 in cancer". Journal of Biomedicine & Biotechnology. 2011: 875824. doi:10.1155/2011/875824. PMC 2975074. PMID 21076528.
  12. ^ a b Kwon S, Zhang Y, Matthias P (December 2007). "The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response". Genes & Development. 21 (24): 3381–3394. doi:10.1101/gad.461107. PMC 2113037. PMID 18079183.
  13. ^ Lavars N (2022-01-18). "Targeting an enzyme in fat cells drives rapid weight loss in obese mice". New Atlas. Retrieved 2022-01-18.
  14. ^ Xu G, Niu L, Wang Y, Yang G, Zhu X, Yao Y, et al. (October 2022). "HDAC6-dependent deacetylation of TAK1 enhances sIL-6R release to promote macrophage M2 polarization in colon cancer". Cell Death & Disease. 13 (10): 888. doi:10.1038/s41419-022-05335-1. PMC 9587286. PMID 36270986.
  15. ^ Cook C, Gendron TF, Scheffel K, Carlomagno Y, Dunmore J, DeTure M, Petrucelli L (July 2012). "Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation". Human Molecular Genetics. 21 (13): 2936–2945. doi:10.1093/hmg/dds125. PMC 3373241. PMID 22492994.
  16. ^ Depetter Y, Geurs S, De Vreese R, Goethals S, Vandoorn E, Laevens A, et al. (August 2019). "Selective pharmacological inhibitors of HDAC6 reveal biochemical activity but functional tolerance in cancer models". International Journal of Cancer. 145 (3): 735–747. doi:10.1002/ijc.32169. PMID 30694564.
  17. ^ Gao L, Cueto MA, Asselbergs F, Atadja P (July 2002). "Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family". The Journal of Biological Chemistry. 277 (28): 25748–25755. doi:10.1074/jbc.M111871200. PMID 11948178.
  18. ^ 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): 8777–8784. doi:10.1038/sj.onc.1208128. PMID 15467736.

Further reading edit

  • Pazin MJ, Kadonaga JT (May 1997). "What's up and down with histone deacetylation and transcription?". Cell. 89 (3): 325–328. doi:10.1016/S0092-8674(00)80211-1. PMID 9150131. S2CID 11488594.
  • Wolffe AP (May 1997). "Transcriptional control. Sinful repression". Nature. 387 (6628): 16–17. doi:10.1038/387016a0. PMID 9139815. S2CID 29803420.
  • Huynh KD, Fischle W, Verdin E, Bardwell VJ (July 2000). "BCoR, a novel corepressor involved in BCL-6 repression". Genes & Development. 14 (14): 1810–1823. doi:10.1101/gad.14.14.1810. PMC 316791. PMID 10898795.
  • Mahlknecht U, Schnittger S, Landgraf F, Schoch C, Ottmann OG, Hiddemann W, Hoelzer D (2001). "Assignment of the human histone deacetylase 6 gene (HDAC6) to X chromosome p11.23 by in situ hybridization". Cytogenetics and Cell Genetics. 93 (1–2): 135–136. doi:10.1159/000056967. PMID 11474198. S2CID 41821644.
  • Kao HY, Lee CH, Komarov A, Han CC, Evans RM (January 2002). "Isolation and characterization of mammalian HDAC10, a novel histone deacetylase". The Journal of Biological Chemistry. 277 (1): 187–193. doi:10.1074/jbc.M108931200. PMID 11677242.
  • Seigneurin-Berny D, Verdel A, Curtet S, Lemercier C, Garin J, Rousseaux S, Khochbin S (December 2001). "Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways". Molecular and Cellular Biology. 21 (23): 8035–8044. doi:10.1128/MCB.21.23.8035-8044.2001. PMC 99970. PMID 11689694.
  • Tong JJ, Liu J, Bertos NR, Yang XJ (March 2002). "Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain". Nucleic Acids Research. 30 (5): 1114–1123. doi:10.1093/nar/30.5.1114. PMC 101247. PMID 11861901.
  • Gao L, Cueto MA, Asselbergs F, Atadja P (July 2002). "Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family". The Journal of Biological Chemistry. 277 (28): 25748–25755. doi:10.1074/jbc.M111871200. PMID 11948178.
  • Hubbert C, Guardiola A, Shao R, Kawaguchi Y, Ito A, Nixon A, et al. (May 2002). "HDAC6 is a microtubule-associated deacetylase". Nature. 417 (6887): 455–458. Bibcode:2002Natur.417..455H. doi:10.1038/417455a. PMID 12024216. S2CID 4373254.
  • Kirsh O, Seeler JS, Pichler A, Gast A, Müller S, Miska E, et al. (June 2002). "The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase". The EMBO Journal. 21 (11): 2682–2691. doi:10.1093/emboj/21.11.2682. PMC 125385. PMID 12032081.
  • Hook SS, Orian A, Cowley SM, Eisenman RN (October 2002). "Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes". Proceedings of the National Academy of Sciences of the United States of America. 99 (21): 13425–13430. Bibcode:2002PNAS...9913425H. doi:10.1073/pnas.172511699. PMC 129689. PMID 12354939.
  • Westendorf JJ, Zaidi SK, Cascino JE, Kahler R, van Wijnen AJ, Lian JB, et al. (November 2002). "Runx2 (Cbfa1, AML-3) interacts with histone deacetylase 6 and represses the p21(CIP1/WAF1) promoter". Molecular and Cellular Biology. 22 (22): 7982–7992. doi:10.1128/MCB.22.22.7982-7992.2002. PMC 134736. PMID 12391164.
  • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E (February 2003). "The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase". Molecular Cell. 11 (2): 437–444. doi:10.1016/S1097-2765(03)00038-8. PMID 12620231.
  • Voelter-Mahlknecht S, Mahlknecht U (July 2003). "Cloning and structural characterization of the human histone deacetylase 6 gene". International Journal of Molecular Medicine. 12 (1): 87–93. doi:10.3892/ijmm.12.1.87. PMID 12792815.
  • Brush MH, Guardiola A, Connor JH, Yao TP, Shenolikar S (February 2004). "Deactylase inhibitors disrupt cellular complexes containing protein phosphatases and deacetylases". The Journal of Biological Chemistry. 279 (9): 7685–7691. doi:10.1074/jbc.M310997200. PMID 14670976.
  • Pandey UB, Batlevi Y, Baehrecke EH, Taylor JP (Nov–Dec 2007). "HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration". Autophagy. 3 (6): 643–645. doi:10.4161/auto.5050. PMID 17912024.
  • Pandey UB, Nie Z, Batlevi Y, McCray BA, Ritson GP, Nedelsky NB, et al. (June 2007). "HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS". Nature. 447 (7146): 859–863. Bibcode:2007Natur.447..860P. doi:10.1038/nature05853. PMID 17568747. S2CID 4365061.

External links edit

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

January 01, 1970
hdac6, histone, deacetylase, enzyme, that, humans, encoded, gene, emerged, highly, promising, candidate, selectively, inhibit, therapeutic, strategy, combat, several, types, cancer, neurodegenerative, disorders, available, structurespdbortholog, search, pdbe, . Histone deacetylase 6 is an enzyme that in humans is encoded by the HDAC6 gene 5 6 HDAC6 has emerged as a highly promising candidate to selectively inhibit as a therapeutic strategy to combat several types of cancer and neurodegenerative disorders 7 HDAC6Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes3C5K 3GV4 3PHD 5EDU 5KH7IdentifiersAliasesHDAC6 CPBHM HD6 PPP1R90 JM21 histone deacetylase 6External IDsOMIM 300272 MGI 1333752 HomoloGene 31353 GeneCards HDAC6 OMA HDAC6 orthologsGene location Human Chr X chromosome human 1 BandXp11 23Start48 801 377 bp 1 End48 824 982 bp 1 Gene location Mouse Chr X chromosome mouse 2 BandX A1 1 X 3 58 cMStart7 796 359 bp 2 End7 814 128 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inanterior pituitaryright lobe of liverganglionic eminencesural nervecanal of the cervixright lobe of thyroid glandleft uterine tubeleft lobe of thyroid glandgastric mucosakidneyTop expressed inentorhinal cortexislet of Langerhansyolk sacmedullary collecting ductdorsomedial hypothalamic nucleusdorsal tegmental nucleussuperior colliculusplacentaolfactory bulbkidneyMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionhistone deacetylase binding misfolded protein binding metal ion binding enzyme binding NAD dependent histone deacetylase activity H3 K14 specific beta catenin binding zinc ion binding polyubiquitin modification dependent protein binding protein binding tau protein binding dynein complex binding Hsp90 protein binding histone deacetylase activity microtubule binding alpha tubulin binding ubiquitin binding beta tubulin binding actin binding hydrolase activity ubiquitin protein ligase binding tubulin deacetylase activity RNA polymerase II cis regulatory region sequence specific DNA binding protein deacetylase activity acetylspermidine deacetylase activityCellular componentcytosol perinuclear region of cytoplasm caveola microtubule nucleus multivesicular body cell projection microtubule associated complex aggresome dynein complex histone deacetylase complex perikaryon axon inclusion body dendrite cell leading edge cytoplasmic microtubule cell body neuron projection nucleoplasm cytoplasm protein containing complexBiological processHsp90 deacetylation protein quality control for misfolded or incompletely synthesized proteins response to organic substance cellular response to topologically incorrect protein tubulin deacetylation regulation of establishment of protein localization ubiquitin dependent protein catabolic process via the multivesicular body sorting pathway response to growth factor intracellular protein transport aggresome assembly negative regulation of proteolysis histone H3 deacetylation positive regulation of signal transduction peptidyl lysine deacetylation response to misfolded protein regulation of transcription DNA templated regulation of protein stability ubiquitin dependent protein catabolic process mitochondrion localization positive regulation of epithelial cell migration regulation of fat cell differentiation transcription DNA templated regulation of autophagy of mitochondrion polyubiquitinated misfolded protein transport response to toxic substance positive regulation of hydrogen peroxide mediated programmed cell death regulation of microtubule based movement regulation of signaling receptor activity protein polyubiquitination protein deacetylation negative regulation of hydrogen peroxide metabolic process regulation of autophagy negative regulation of oxidoreductase activity regulation of androgen receptor signaling pathway negative regulation of transcription DNA templated cellular response to misfolded protein positive regulation of chaperone mediated protein complex assembly regulation of gene expression epigenetic negative regulation of protein containing complex disassembly autophagy negative regulation of microtubule depolymerization lysosome localization histone deacetylation cellular response to hydrogen peroxide collateral sprouting dendritic spine morphogenesis cilium assembly regulation of macroautophagy parkin mediated stimulation of mitophagy in response to mitochondrial depolarization positive regulation of mitophagy in response to mitochondrial depolarization chromatin organization positive regulation of protein oligomerization protein containing complex disassembly positive regulation of peptidyl serine phosphorylation polyamine deacetylation spermidine deacetylationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez1001315185EnsemblENSG00000094631ENSMUSG00000031161UniProtQ9UBN7Q9Z2V5RefSeq mRNA NM 006044NM 001321225NM 001321226NM 001321227NM 001321228NM 001321229NM 001321230NM 001321231NM 001130416NM 010413RefSeq protein NP 001308154NP 001308155NP 001308156NP 001308157NP 001308158NP 001308159NP 001308160NP 006035NP 001123888NP 034543Location UCSC Chr X 48 8 48 82 MbChr X 7 8 7 81 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Clinical relevance 3 Interactions 4 See also 5 References 6 Further reading 7 External linksFunction editHistones play a critical role in transcriptional regulation cell cycle progression and developmental events Histone acetylation deacetylation alters chromatin structure and affects transcription The protein encoded by this gene belongs to class II of the histone deacetylase acuc apha family It contains an internal duplication of two catalytic domains that appear to function independently of each other This protein possesses histone deacetylase activity and represses transcription 8 It retracts the cilium of the cell which is necessary prior to mitosis 9 HDAC encourages cell motility and catalyzes a tubulin deacetylation 10 As a result the enzyme encourages cancer cell metastasis 11 HDAC6 affects transcription and translation by regulating heat shock protein 90 Hsp90 HDAC6 is required in the formation of stress granule SG proteins and is instrumental in SG formation pharmacological inhibition or genetic removal of HDAC6 abolished SG formation 11 HDAC6 bonds with high affinity to ubiquitinated proteins 12 HDAC6 is involved in leptin sensitivity 13 HDAC6 deacetylates tyrosine residue T178 on TAK1 14 Clinical relevance editMutations in this gene have been associated to Alzheimer s disease 15 Over expression of this protein correlates with tumorigenesis and cell survival HDAC6 also encourages metastasis of cancer cells 11 Since HDAC6 is dysregulated and or implicated in several cancers and neurodegenerative disorders pharmacological inhibition of this specific enzyme holds great therapeutic potential and could also limit side effects associated with pan inhibitors of multiple HDAC enzymes 7 Selective inhibition of HDAC6 as a strategy to treat cancers is however also subject of debate since some HDAC6 inhibitors exhibited anti tumor activity in vitro and in vivo only when administered in high concentrations which also produced off target effects The findings suggest that further study is needed to clarify data on anti cancer effects of selective HDAC6 inhibitors 16 Interactions editHDAC6 has been shown to interact with HDAC11 17 and Zinc finger and BTB domain containing protein 16 18 HDAC6 interacts with SG Stress granule protein G3BP1 12 See also editHistone deacetylaseReferences edit a b c GRCh38 Ensembl release 89 ENSG00000094631 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000031161 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 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 4873 Bibcode 1999PNAS 96 4868G doi 10 1073 pnas 96 9 4868 PMC 21783 PMID 10220385 Nagase T Ishikawa K Suyama M Kikuno R Hirosawa M Miyajima N et al December 1998 Prediction of the coding sequences of unidentified human genes XII The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro DNA Research 5 6 355 364 doi 10 1093 dnares 5 6 355 PMID 10048485 a b Geurs S Clarisse D Baele F Franceus J Desmet T De Bosscher K D hooghe M May 2022 Identification of mercaptoacetamide based HDAC6 inhibitors via a lean inhibitor strategy screening synthesis and biological evaluation Chemical Communications 58 42 6239 6242 doi 10 1039 D2CC01550A hdl 1854 LU 8752799 PMID 35510683 S2CID 248527466 Entrez Gene HDAC6 histone deacetylase 6 Krishnamurthy K Wang G Silva J Condie BG Bieberich E February 2007 Ceramide regulates atypical PKCzeta lambda mediated cell polarity in primitive ectoderm cells A novel function of sphingolipids in morphogenesis The Journal of Biological Chemistry 282 5 3379 3390 doi 10 1074 jbc M607779200 PMID 17105725 Lay summary in Lipid helps cells find their way by keeping their antennae up phys org news July 9 2012 Gao YS Hubbert CC Lu J Lee YS Lee JY Yao TP December 2007 Histone deacetylase 6 regulates growth factor induced actin remodeling and endocytosis Molecular and Cellular Biology 27 24 8637 8647 doi 10 1128 MCB 00393 07 PMC 2169396 PMID 17938201 a b c Aldana Masangkay GI Sakamoto KM 2011 The role of HDAC6 in cancer Journal of Biomedicine amp Biotechnology 2011 875824 doi 10 1155 2011 875824 PMC 2975074 PMID 21076528 a b Kwon S Zhang Y Matthias P December 2007 The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response Genes amp Development 21 24 3381 3394 doi 10 1101 gad 461107 PMC 2113037 PMID 18079183 Lavars N 2022 01 18 Targeting an enzyme in fat cells drives rapid weight loss in obese mice New Atlas Retrieved 2022 01 18 Xu G Niu L Wang Y Yang G Zhu X Yao Y et al October 2022 HDAC6 dependent deacetylation of TAK1 enhances sIL 6R release to promote macrophage M2 polarization in colon cancer Cell Death amp Disease 13 10 888 doi 10 1038 s41419 022 05335 1 PMC 9587286 PMID 36270986 Cook C Gendron TF Scheffel K Carlomagno Y Dunmore J DeTure M Petrucelli L July 2012 Loss of HDAC6 a novel CHIP substrate alleviates abnormal tau accumulation Human Molecular Genetics 21 13 2936 2945 doi 10 1093 hmg dds125 PMC 3373241 PMID 22492994 Depetter Y Geurs S De Vreese R Goethals S Vandoorn E Laevens A et al August 2019 Selective pharmacological inhibitors of HDAC6 reveal biochemical activity but functional tolerance in cancer models International Journal of Cancer 145 3 735 747 doi 10 1002 ijc 32169 PMID 30694564 Gao L Cueto MA Asselbergs F Atadja P July 2002 Cloning and functional characterization of HDAC11 a novel member of the human histone deacetylase family The Journal of Biological Chemistry 277 28 25748 25755 doi 10 1074 jbc M111871200 PMID 11948178 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 8784 doi 10 1038 sj onc 1208128 PMID 15467736 Further reading editPazin MJ Kadonaga JT May 1997 What s up and down with histone deacetylation and transcription Cell 89 3 325 328 doi 10 1016 S0092 8674 00 80211 1 PMID 9150131 S2CID 11488594 Wolffe AP May 1997 Transcriptional control Sinful repression Nature 387 6628 16 17 doi 10 1038 387016a0 PMID 9139815 S2CID 29803420 Huynh KD Fischle W Verdin E Bardwell VJ July 2000 BCoR a novel corepressor involved in BCL 6 repression Genes amp Development 14 14 1810 1823 doi 10 1101 gad 14 14 1810 PMC 316791 PMID 10898795 Mahlknecht U Schnittger S Landgraf F Schoch C Ottmann OG Hiddemann W Hoelzer D 2001 Assignment of the human histone deacetylase 6 gene HDAC6 to X chromosome p11 23 by in situ hybridization Cytogenetics and Cell Genetics 93 1 2 135 136 doi 10 1159 000056967 PMID 11474198 S2CID 41821644 Kao HY Lee CH Komarov A Han CC Evans RM January 2002 Isolation and characterization of mammalian HDAC10 a novel histone deacetylase The Journal of Biological Chemistry 277 1 187 193 doi 10 1074 jbc M108931200 PMID 11677242 Seigneurin Berny D Verdel A Curtet S Lemercier C Garin J Rousseaux S Khochbin S December 2001 Identification of components of the murine histone deacetylase 6 complex link between acetylation and ubiquitination signaling pathways Molecular and Cellular Biology 21 23 8035 8044 doi 10 1128 MCB 21 23 8035 8044 2001 PMC 99970 PMID 11689694 Tong JJ Liu J Bertos NR Yang XJ March 2002 Identification of HDAC10 a novel class II human histone deacetylase containing a leucine rich domain Nucleic Acids Research 30 5 1114 1123 doi 10 1093 nar 30 5 1114 PMC 101247 PMID 11861901 Gao L Cueto MA Asselbergs F Atadja P July 2002 Cloning and functional characterization of HDAC11 a novel member of the human histone deacetylase family The Journal of Biological Chemistry 277 28 25748 25755 doi 10 1074 jbc M111871200 PMID 11948178 Hubbert C Guardiola A Shao R Kawaguchi Y Ito A Nixon A et al May 2002 HDAC6 is a microtubule associated deacetylase Nature 417 6887 455 458 Bibcode 2002Natur 417 455H doi 10 1038 417455a PMID 12024216 S2CID 4373254 Kirsh O Seeler JS Pichler A Gast A Muller S Miska E et al June 2002 The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase The EMBO Journal 21 11 2682 2691 doi 10 1093 emboj 21 11 2682 PMC 125385 PMID 12032081 Hook SS Orian A Cowley SM Eisenman RN October 2002 Histone deacetylase 6 binds polyubiquitin through its zinc finger PAZ domain and copurifies with deubiquitinating enzymes Proceedings of the National Academy of Sciences of the United States of America 99 21 13425 13430 Bibcode 2002PNAS 9913425H doi 10 1073 pnas 172511699 PMC 129689 PMID 12354939 Westendorf JJ Zaidi SK Cascino JE Kahler R van Wijnen AJ Lian JB et al November 2002 Runx2 Cbfa1 AML 3 interacts with histone deacetylase 6 and represses the p21 CIP1 WAF1 promoter Molecular and Cellular Biology 22 22 7982 7992 doi 10 1128 MCB 22 22 7982 7992 2002 PMC 134736 PMID 12391164 North BJ Marshall BL Borra MT Denu JM Verdin E February 2003 The human Sir2 ortholog SIRT2 is an NAD dependent tubulin deacetylase Molecular Cell 11 2 437 444 doi 10 1016 S1097 2765 03 00038 8 PMID 12620231 Voelter Mahlknecht S Mahlknecht U July 2003 Cloning and structural characterization of the human histone deacetylase 6 gene International Journal of Molecular Medicine 12 1 87 93 doi 10 3892 ijmm 12 1 87 PMID 12792815 Brush MH Guardiola A Connor JH Yao TP Shenolikar S February 2004 Deactylase inhibitors disrupt cellular complexes containing protein phosphatases and deacetylases The Journal of Biological Chemistry 279 9 7685 7691 doi 10 1074 jbc M310997200 PMID 14670976 Pandey UB Batlevi Y Baehrecke EH Taylor JP Nov Dec 2007 HDAC6 at the intersection of autophagy the ubiquitin proteasome system and neurodegeneration Autophagy 3 6 643 645 doi 10 4161 auto 5050 PMID 17912024 Pandey UB Nie Z Batlevi Y McCray BA Ritson GP Nedelsky NB et al June 2007 HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS Nature 447 7146 859 863 Bibcode 2007Natur 447 860P doi 10 1038 nature05853 PMID 17568747 S2CID 4365061 External links editHDAC6 protein human at the U S National Library of Medicine Medical Subject Headings MeSH HDAC6 human gene location in the UCSC Genome Browser HDAC6 human gene details in the UCSC Genome Browser This article incorporates text from the United States National Library of Medicine which is in the public domain Portal nbsp Biology Retrieved from https en wikipedia org w index php title HDAC6 amp oldid 1213126798, wikipedia, wiki, book, books, library,

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