Research Assistant Professor
Since gene cloning, my research has been focused on ALL1/MLL1 gene, because:
1) its encoding protein is a histone methyltransferase catalyzing histone H3K4 methylation and localizes widely at transcription start site (TSS) of expressed genes.
2) ALL1 gene is frequently rearranged in acute myeloid leukemia, particularly in infant acute lymphocytic leukemia (ALL) with aggressive clinical feature, to generate ALL1 fusion gene. A variety of partner genes are involved in production of ALL1 gene fusion.
3) ALL1 fusion protein, derived from fused gene, is an aberrant epigenetic regulator, inducing H3K4 and H3K79 methylation at TSS of its target genes and extending toward 3’. These histone modifications lead to overexpression of the target genes. Some targets may underlie molecular pathogenesis of ALL1-associated leukemia.
In 2008, we reported about 140 genes as primary targets of ALL1/AF4 fusion protein in ALL. Among them, I am working on a histone demthylase, JMJD1C, which erases repressive methylation mark on H3K9. My current interest is to study a post-translational modification, particularly post-transcriptional cleavage and/or ubiquitination of the protein.
920 Biomedical Research Tower
460 W 12th Avenue
Columbus, OH 43210