Jumonji domain-containing protein 3 (JMJD3) a Histone H3K27 Demethylase

Fri, 09/28/2012 - 12:15

Jumonji domain-containing protein 3 (JMJD3), identified as H3K27me3 demethylase, controls the expression of key regulators and markers of neurogenesis, and is required for commitment to the neural lineage. Nevertheless, the precise molecular targets of JMJD3 remain largely uncharacterized. The regulation of JMJD3 appears to be highly gene- and context- specific, suggesting interplay with specific molecules to promote fine-tuning more than the on/off alternation of methylation status. It is possible that cellular events responsible for JMJD3 activity are similar to those observed during cell cycle arrest at G1/S or G2/M, or senescence (1). In a recent study, the endogenous levels of JMJD3 were investigated in the neural stem cells (NSC) by RT-PCR, Western blot and immunocytochemistry using anti-JMJD3 antibodies. Available data suggests that JMJD3 mRNA and protein levels significantly increased in NSC differentiation leading to  increased JMJD3 activity as detected by a significant decrease in trimethylation state of H3K27me3 (2).

"]Western Blot: JMJD3 Antibody [NBP1-06640] Western Blot: JMJD3 Antibody [NBP1-06640

 Histone methylation is an important epigenetic phenomenon that participates in a diverse array of cellular processes and has been found to be associated with cancers. In vitro biochemical experiments demonstrated that JMJD3 directly catalyzes the demethylation and that JMJD3 is upregulated in cancers as determined by anti-JMJD3 antibodies (3). Future work directed to understand whether the methylation status of H3K27 is altered in several cancers and the role of H3K27 methylation and JMJD3 in cancer development and progression is an open area of research.

  1. PMID: 21074716
  2. PMID: 21483786
  3. PMID: 17923864

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