[HTML][HTML] Histone Demethylase Jumonji D3 (JMJD3) as a Tumor Suppressor by Regulating p53 Protein Nuclear Stabilization

CI Ene, L Edwards, G Riddick, M Baysan, K Woolard… - PloS one, 2012 - journals.plos.org
CI Ene, L Edwards, G Riddick, M Baysan, K Woolard, S Kotliarova, C Lai, G Belova, M Cam
PloS one, 2012journals.plos.org
Histone methylation regulates normal stem cell fate decisions through a coordinated
interplay between histone methyltransferases and demethylases at lineage specific genes.
Malignant transformation is associated with aberrant accumulation of repressive histone
modifications, such as polycomb mediated histone 3 lysine 27 (H3K27me3) resulting in a
histone methylation mediated block to differentiation. The relevance, however, of histone
demethylases in cancer remains less clear. We report that JMJD3, a H3K27me3 …
Histone methylation regulates normal stem cell fate decisions through a coordinated interplay between histone methyltransferases and demethylases at lineage specific genes. Malignant transformation is associated with aberrant accumulation of repressive histone modifications, such as polycomb mediated histone 3 lysine 27 (H3K27me3) resulting in a histone methylation mediated block to differentiation. The relevance, however, of histone demethylases in cancer remains less clear. We report that JMJD3, a H3K27me3 demethylase, is induced during differentiation of glioblastoma stem cells (GSCs), where it promotes a differentiation-like phenotype via chromatin dependent (INK4A/ARF locus activation) and chromatin independent (nuclear p53 protein stabilization) mechanisms. Our findings indicate that deregulation of JMJD3 may contribute to gliomagenesis via inhibition of the p53 pathway resulting in a block to terminal differentiation.
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