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HDAC3

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(Redirected from RPD3)
HDAC3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesHDAC3, HD3, RPD3, RPD3-2, histone deacetylase 3
External IDsOMIM: 605166; MGI: 1343091; HomoloGene: 48250; GeneCards: HDAC3; OMA:HDAC3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

8841

15183

Ensembl

ENSG00000171720

ENSMUSG00000024454

UniProt

O15379

O88895

RefSeq (mRNA)

NM_003883

NM_010411

RefSeq (protein)

NP_003874
NP_001341968
NP_001341969
NP_001341970

NP_034541

Location (UCSC)Chr 5: 141.62 – 141.64 MbChr 18: 38.07 – 38.09 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Histone deacetylase 3 is an enzyme encoded by the HDAC3 gene in both humans and mice.[5][6][7][8]

Function

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Histones are highly alkaline proteins that package and order DNA into structural units called nucleosomes, which comprise the major protein component of chromatin. The posttranslational and enzymatically mediated lysine acetylation and deacetylation of histone tails change the local chromatin structure by altering the electrostatic attraction between the negatively charged DNA backbone and histones. HDAC3 is a Class I member of the histone deacetylase superfamily (comprising four classes based on function and DNA sequence homology) that is recruited to enhancers to modulate both the epigenome and nearby gene expression. HDAC3 is found exclusively in the cell nucleus, where it is the sole endogenous histone deacetylase biochemically purified in the nuclear-receptor corepressor complex containing NCOR and SMRT (NCOR2). Thus, HDAC3, unlike other HDACs, has a unique role in modulating the transcriptional activities of nuclear receptors.

Alternative functions

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Histone deacetylases can be regulated by endogenous factors, dietary components, synthetic inhibitors and bacteria-derived signals. Studies in mice with a specific deletion of HDAC3 in intestinal epithelial cells (IECs) show a deregulated IEC's gene expression. In these deletion-mutant mice, loss of Paneth cells, impaired IEC function and alterations in intestinal composition of commensal bacteria were observed. These negative effects were not observed in germ-free mice, indicating that the effects of the deletion are only seen in the presence of intestinal microbial colonization. But the negative effects of HDAC3 deletion are not due to the presence of an altered microbiota because normal germ-free mice colonized with the altered microbiota did not show the negative effects seen in deletion mutants.

Although the precise mechanism and the specific signals are not known it is clear that HDAC3 interacts with derived signals of commensal bacteria of the gut microbiota. These interactions are responsible of calibrating epithelial cells responses necessary to establish a normal relationship between the host and the commensal as well as to maintain intestinal homeostasis.[9][10][11][12]

Interactions

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HDAC3 has been shown to interact with:

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000171720 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024454 – 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.
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  7. ^ Montgomery, Rusty L.; Potthoff, Matthew J.; Haberland, Michael; Qi, Xiaoxia; Matsuzaki, Satoshi; Humphries, Kenneth M.; Richardson, James A.; Bassel-Duby, Rhonda; Olson, Eric N. (2008-11-03). "Maintenance of cardiac energy metabolism by histone deacetylase 3 in mice". Journal of Clinical Investigation. 118 (11): 3588–3597. doi:10.1172/jci35847. ISSN 0021-9738. PMC 2556240. PMID 18830415.
  8. ^ Bhaskara, Srividya; Chyla, Brenda J.; Amann, Joseph M.; Knutson, Sarah K.; Cortez, David; Sun, Zu-Wen; Hiebert, Scott W. (2008). "Deletion of Histone Deacetylase 3 Reveals Critical Roles in S Phase Progression and DNA Damage Control". Molecular Cell. 30 (1): 61–72. doi:10.1016/j.molcel.2008.02.030. PMC 2373760. PMID 18406327.
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Further reading

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

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