Histone demethylase JMJD3 contributes to epigenetic control of INK4a/ARF by oncogenic RAS

Genes Dev. 2009 May 15;23(10):1177-82. doi: 10.1101/gad.511109.

Abstract

The INK4a/ARF tumor suppressor locus, a key executor of cellular senescence, is regulated by members of the Polycomb group (PcG) of transcriptional repressors. Here we show that signaling from oncogenic RAS overrides PcG-mediated repression of INK4a by activating the H3K27 demethylase JMJD3 and down-regulating the methyltransferase EZH2. In human fibroblasts, JMJD3 activates INK4a, but not ARF, and causes p16(INK4a)-dependent arrest. In mouse embryo fibroblasts, Jmjd3 activates both Ink4a and Arf and elicits a p53-dependent arrest, echoing the effects of RAS in this system. Our findings directly implicate JMJD3 in the regulation of INK4a/ARF during oncogene-induced senescence and suggest that JMJD3 has the capacity to act as a tumor suppressor.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Cellular Senescence
  • Cyclin-Dependent Kinase Inhibitor p16 / metabolism*
  • Epigenesis, Genetic / genetics*
  • Fibroblasts / cytology
  • Fibroblasts / metabolism
  • Gene Expression Regulation*
  • Humans
  • Jumonji Domain-Containing Histone Demethylases
  • Mice
  • Oxidoreductases, N-Demethylating / metabolism*
  • Signal Transduction
  • ras Proteins / metabolism*

Substances

  • Cyclin-Dependent Kinase Inhibitor p16
  • Jumonji Domain-Containing Histone Demethylases
  • KDM6B protein, human
  • Kdm6b protein, mouse
  • Oxidoreductases, N-Demethylating
  • ras Proteins