Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process

R Pfau, A Tzatsos, SC Kampranis… - Proceedings of the …, 2008 - National Acad Sciences
R Pfau, A Tzatsos, SC Kampranis, OB Serebrennikova, SE Bear, PN Tsichlis
Proceedings of the National Academy of Sciences, 2008National Acad Sciences
A common integration site, cloned from MoMuLV-induced rat T cell lymphomas, was
mapped immediately upstream of Not dead yet-1 (Ndy1)/KDM2B, a gene expressed
primarily in testis, spleen, and thymus, that is also known as FBXL10 or JHDM1B. Ndy1
encodes a nuclear, chromatin-associated protein that harbors Jumonji C (JmjC), CXXC,
PHD, proline-rich, F-box, and leucine-rich repeat domains. Ndy1 and its homolog
Ndy2/KDM2A (FBXL11 or JHDM1A), which is also a target of provirus integration in …
A common integration site, cloned from MoMuLV-induced rat T cell lymphomas, was mapped immediately upstream of Not dead yet-1 (Ndy1)/KDM2B, a gene expressed primarily in testis, spleen, and thymus, that is also known as FBXL10 or JHDM1B. Ndy1 encodes a nuclear, chromatin-associated protein that harbors Jumonji C (JmjC), CXXC, PHD, proline-rich, F-box, and leucine-rich repeat domains. Ndy1 and its homolog Ndy2/KDM2A (FBXL11 or JHDM1A), which is also a target of provirus integration in retrovirus-induced lymphomas, encode proteins that were recently shown to possess Jumonji C-dependent histone H3 K36 dimethyl-demethylase or histone H3 K4 trimethyl-demethylase activities. Here, we show that mouse embryo fibroblasts engineered to express Ndy1 or Ndy2 undergo immortalization in the absence of replicative senescence via a JmjC domain-dependent process that targets the Rb and p53 pathways. Knockdown of endogenous Ndy1 or expression of JmjC domain mutants of Ndy1 promote senescence, suggesting that Ndy1 is a physiological inhibitor of senescence in dividing cells and that inhibition of senescence depends on histone H3 demethylation.
National Acad Sciences