HDAC6

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Histone deacetylase 6
Protein HDAC6 PDB 3C5K.png
Rendering based on PDB 3C5K.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols HDAC6 ; CPBHM; HD6; PPP1R90
External IDs OMIM300272 MGI1333752 HomoloGene31353 ChEMBL: 1865 GeneCards: HDAC6 Gene
EC number 3.5.1.98
RNA expression pattern
PBB GE HDAC6 206846 s at tn.png
PBB GE HDAC6 216224 s at tn.png
PBB GE HDAC6 211722 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 10013 15185
Ensembl ENSG00000094631 ENSMUSG00000031161
UniProt Q9UBN7 Q9Z2V5
RefSeq (mRNA) NM_006044 NM_001130416
RefSeq (protein) NP_006035 NP_001123888
Location (UCSC) Chr HG1436_HG1432_PATCH:
48.66 – 48.68 Mb
Chr X:
7.93 – 7.95 Mb
PubMed search [1] [2]

Histone deacetylase 6 is an enzyme that in humans is encoded by the HDAC6 gene.[1][2]

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.[3]

Clinical relevance[edit]

Mutations in this gene have been associated to Alzheimer's disease.[4]
Over expression of this protein correlates with tumorigenesis and cell survival, HDAC6 also encourages metastasis of cancer cells.[5]

Functions[edit]

Retracts the Cilium of the cell, which is necessary prior to mitosis of the cell.[6]
HDAC also encourages cell motility and catalyzes α-tubulin deacetylation.[7] as a result the enzyme also encourages cancer cell metastasis.[5]
HDAC6 also affects transcription and translation by regulating the heat-shock protein 90 (Hsp90) and stress granules (SGs), respectively.[5]
HDAC6 is also known to bond with high affinity to ubiquitinated proteins.[8] HDAC6 is also required in the formation of SG (Stress granule proteins and is instrumental in SG formation; pharmacological inhibition or genetic removal of HDAC6 abolished SG formation.

Interactions[edit]

HDAC6 has been shown to interact with HDAC11[9] and Zinc finger and BTB domain-containing protein 16.[10]
HDAC6 interacts with SG (Stress granule) protein G3BP1.[8]

See also[edit]

References[edit]

  1. ^ Grozinger CM, Hassig CA, Schreiber SL (Jun 1999). "Three proteins define a class of human histone deacetylases related to yeast Hda1p". Proc Natl Acad Sci U S A 96 (9): 4868–73. doi:10.1073/pnas.96.9.4868. PMC 21783. PMID 10220385. 
  2. ^ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (May 1999). "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 Res 5 (6): 355–64. doi:10.1093/dnares/5.6.355. PMID 10048485. 
  3. ^ "Entrez Gene: HDAC6 histone deacetylase 6". 
  4. ^ Cook, C.; Gendron, T. F.; Scheffel, K.; Carlomagno, Y.; Dunmore, J.; DeTure, M.; Petrucelli, L. (5 April 2012). "Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation". Human Molecular Genetics. doi:10.1093/hmg/dds125. 
  5. ^ a b c "The Role of HDAC6 in Cancer". 
  6. ^ "Lipid helps cells find their way by keeping their 'antennae' up". 
  7. ^ "Histone Deacetylase 6 Regulates Growth Factor-Induced Actin Remodeling and Endocytosis". 
  8. ^ a b "The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response". 
  9. ^ Gao, Lin; Cueto Maria A; Asselbergs Fred; Atadja Peter (Jul 2002). "Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family". J. Biol. Chem. (United States) 277 (28): 25748–55. doi:10.1074/jbc.M111871200. ISSN 0021-9258. PMID 11948178. 
  10. ^ Chauchereau, Anne; Mathieu Marion, de Saintignon Julie, Ferreira Roger, Pritchard Linda L, Mishal Zohair, Dejean Anne, Harel-Bellan Annick (Nov 2004). "HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF". Oncogene (England) 23 (54): 8777–84. doi:10.1038/sj.onc.1208128. ISSN 0950-9232. PMID 15467736. 

Further reading[edit]

External links[edit]

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