Disease relevance of Hdac3

• Further, Hdac3 overexpression did not augment isoproterenol-induced cardiac hypertrophy when compared with wild-type littermates [1].

High impact information on Hdac3

• Regulation of relB in dendritic cells by means of modulated association of vitamin D receptor and histone deacetylase 3 with the promoter [2].
• N-terminal region, C-terminal region, nuclear export signal, and deacetylation activity of histone deacetylase-3 are essential for the viability of the DT40 chicken B cell line [3].
• The histone-binding code of nuclear receptor co-repressors matches the substrate specificity of histone deacetylase 3 [4].
• Through the use of HDAC inhibitors and coimmunoprecipitations, we furthermore demonstrate that the effects of RB on PPARgamma-mediated control of the cell cycle and apoptosis depend on the recruitment of histone deacetylase 3 (HDAC3) to PPARgamma [5].
• Histone deacetylase-3 interacts with a TEL mutant that cannot bind N-CoR, suggesting that this is a direct interaction with TEL [6].

Biological context of Hdac3

• Assignment of the histone deacetylase gene (Hdac3) to mouse chromosome 18B3 by in situ hybridization [7].
• In combination, these data hence demonstrate that the effects of PPARgamma on cell proliferation and apoptosis are dependent on the presence of an RB-HDAC3 complex [5].
• Modulation of splicing events in histone deacetylase 3 by various extracellular and signal transduction pathways [8].
• A panel of deleted mouse X chromosome somatic cell hybrids derived from the embryonic stem cell line HD3 shows preferential breakage in the Hprt-DXHX254E region [9].

Anatomical context of Hdac3

• The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation [10].
• Hairless contains a novel nuclear matrix targeting signal and associates with histone deacetylase 3 in nuclear speckles [11].
• A panel of 91 somatic cell hybrids containing deleted mouse X chromosomes and falling into seven nested intervals has been isolated and characterized from fusions involving the murine embryonic stem cell HD3 [9].

Other interactions of Hdac3

• Our observations suggest that the co-repressor CtBP1 and HDAC3 are part of transcription silencing complex that mediates the transcriptional repression by Glis2 [12].

References