H3K4me3 is a pivotal mark of active chromatin because it acts as a platform for the binding of multiple histone acetyltransferases, histone demethylases and nucleosome-remodeling complexes [ 44, 100].
For example, multiple studies have demonstrated that histone demethylases are substrates of SCF E3 ligase complexes and can be polyubiquitylated and targeted for proteasomal degradation [ 82– 82].
Histone methylation levels, which are determined by the action of both histone demethylases and methyltransferases, impact multiple biological processes by affecting gene expression activity.
Previously, mouse models for histone methyl transferases and histone demethylases have been characterized with multiple developmental defects [31] [33], [62].
(44) As mentioned above, IDH1 mutations induce the accumulation of 2-HG, which acts as an inhibitor of multiple a-ketoglutarate (a-KG -dependent dioxygena-KG -dependent histone demethyla-KG -dependentT protein family.
Furthermore, histone demethylases often form protein complexes with multiple reader domains.
LSD1 (Lysine Specific Demethylase I) is one of the histone demethylases, which removes one methyl group from mono- or di-methylated lysine residue.
Highly enriched subsets of HIF-1α ChIP hits included multiple enzymes of the glycolytic pathway, autophagic targets and jumonji domain (JmjC) containing histone demethylases.
Our RNA-seq analysis provides the first evidence that of multiple families of epigenetic regulators, only DNA methyltransferase (DNMT3L), histone methyltransferase (SETDB2), and histone demethylases (KDM4A) were particularly up-regulated by Poly (I C) and LPS stimulation in microglia, with LPS being more potent than Poly (I C).
JmjC-domain containing histone demethylases (JHDMs) play critical roles in many key cellular processes and have been implicated in multiple disease conditions.
