ASH1L Links Histone H3 Lysine 36 Dimethylation to MLL Leukemia.

@article{Zhu2016ASH1LLH,
  title={ASH1L Links Histone H3 Lysine 36 Dimethylation to MLL Leukemia.},
  author={Li Zhu and Qin Li and Stephen Hon-Kit Wong and Min Huang and Brianna J. Klein and Jinfeng Shen and Larissa M. Ikenouye and Masayuki Onishi and Dominik Schneidawind and Corina Buechele and Loren L. Hansen and Jes{\'u}s Duque-Afonso and Fangfang Zhu and Gl{\`o}ria Mas Mart{\'i}n and Or P Gozani and Ravindra Majeti and Tatiana G Kutateladze and Michael L. Cleary},
  journal={Cancer discovery},
  year={2016},
  volume={6 7},
  pages={770-83}
}
UNLABELLED Numerous studies in multiple systems support that histone H3 lysine 36 dimethylation (H3K36me2) is associated with transcriptional activation; however, the underlying mechanisms are not well defined. Here, we show that the H3K36me2 chromatin mark written by the ASH1L histone methyltransferase is preferentially bound in vivo by LEDGF, a mixed-lineage leukemia (MLL)-associated protein that colocalizes with MLL, ASH1L, and H3K36me2 on chromatin genome wide. Furthermore, ASH1L… CONTINUE READING