Disease relevance of Hdac4

• Histone deacetylase 4 controls chondrocyte hypertrophy during skeletogenesis [1].

High impact information on Hdac4

• The C-terminal lysines of p53, which are acetylated and methylated, are required for HDAC4 recruitment and transcriptional repression [2].
• DNA damage promotes histone deacetylase 4 nuclear localization and repression of G2/M promoters, via p53 C-terminal lysines [2].
• Trichostatin treatment, but not HDAC4 functional inactivation, relieves the adriamycin-mediated repression of G(2)/M promoters [2].
• Our results indicate that HDAC4 is a component of the DNA damage response and that post-translational modifications of p53 are important for repression of G(2)/M genes [2].
• A potential target of miR-140, histone deacetylase 4, was validated experimentally and the possible role of miR-140 in long bone development is discussed [3].

Biological context of Hdac4

• In this report, we describe the relationship between p53 and HDAC4 recruitment following DNA damage using immunofluorescence, chromatin immunoprecipitation, and transfection experiments [2].
• Intracellular trafficking of histone deacetylase 4 regulates neuronal cell death [4].
• Finally, an increase of nuclear HDAC4 in granule neurons is also observed in weaver mice, which harbor a mutation that promotes CGN apoptosis [4].
• These results suggest that HDAC4 plays a role in stabilizing the genomes of fully grown oocytes [5].
• Immunocytochemistry localized the HDAC4 protein in the chromosome of fully grown oocytes [5].

Anatomical context of Hdac4

• Therefore, our results suggest that HDAC4 acts on a non-histone protein and plays a role in some other cellular functions of full-grown oocytes [5].
• Moreover, ectopic expression of nuclear-localized HDAC4 promotes neuronal apoptosis and represses the transcriptional activities of myocyte enhancer factor 2 and cAMP response element-binding protein, survival factors in neurons [4].

Associations of Hdac4 with chemical compounds

• However, in response to low-potassium or excitotoxic glutamate conditions that induce neuronal cell death, HDAC4 rapidly translocates into the nucleus of cultured CGNs [4].

Other interactions of Hdac4

• To address this possibility, we examined the expression of p53BP1, which is associated with HDAC4 and plays a critical role in the DNA damage response [5].
• Stage specific expression of histone deacetylase 4 (HDAC4) during oogenesis and early preimplantation development in mice [5].
• Histone deacetylase 4 (HDAC4) undergoes signal-dependent shuttling between the cytoplasm and nucleus, which is regulated in part by calcium/calmodulin-dependent kinase (CaMK)-mediated phosphorylation [4].

Analytical, diagnostic and therapeutic context of Hdac4

• RT-PCR analysis revealed that the expression of HDAC4 was specific for full-grown oocytes [5].

References