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Targeting MLL1 H3K4 methyltransferase activity in mixed-lineage leukemia.
Cao, Fang; Townsend, Elizabeth C; Karatas, Hacer; Xu, Jing; Li, Li; Lee, Shirley; Liu, Liu; Chen, Yong; Ouillette, Peter; Zhu, Jidong; Hess, Jay L; Atadja, Peter; Lei, Ming; Qin, Zhaohui S; Malek, Sami; Wang, Shaomeng; Dou, Yali.
Affiliation
  • Cao F; Department of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
  • Townsend EC; Department of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
  • Karatas H; Department of Medicinal Chemistry, University of Michigan, Ann Arbor, MI 48109, USA; Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA; Comprehensive Cancer Center, University of Michigan, Ann Arbor, MI 48109, USA.
  • Xu J; Department of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
  • Li L; Department of Biostatistics and Bioinformatics, Rollins School of Public Health, Emory University, Atlanta, GA 30322, USA.
  • Lee S; Department of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
  • Liu L; Department of Medicinal Chemistry, University of Michigan, Ann Arbor, MI 48109, USA; Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA; Comprehensive Cancer Center, University of Michigan, Ann Arbor, MI 48109, USA.
  • Chen Y; National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
  • Ouillette P; Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA; Comprehensive Cancer Center, University of Michigan, Ann Arbor, MI 48109, USA.
  • Zhu J; Interdisciplinary Research Center of Biology and Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai 200032, China.
  • Hess JL; Indiana University School of Medicine, Indianapolis, IN 46202-3082, USA.
  • Atadja P; Novartis Institutes for BioMedical Research, Shanghai Novartis Research Inc., Shanghai 201203, China.
  • Lei M; National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China; Department of Biological Chemistry, University of Michigan, Ann Arbor
  • Qin ZS; Department of Biostatistics and Bioinformatics, Rollins School of Public Health, Emory University, Atlanta, GA 30322, USA.
  • Malek S; Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA; Comprehensive Cancer Center, University of Michigan, Ann Arbor, MI 48109, USA.
  • Wang S; Department of Medicinal Chemistry, University of Michigan, Ann Arbor, MI 48109, USA; Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA; Comprehensive Cancer Center, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: shaomeng@umich.edu.
  • Dou Y; Department of Pathology, University of Michigan, Ann Arbor, MI 48109, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: yalid@umich.edu.
Mol Cell ; 53(2): 247-61, 2014 Jan 23.
Article in En | MEDLINE | ID: mdl-24389101
Here we report a comprehensive characterization of our recently developed inhibitor MM-401 that targets the MLL1 H3K4 methyltransferase activity. MM-401 is able to specifically inhibit MLL1 activity by blocking MLL1-WDR5 interaction and thus the complex assembly. This targeting strategy does not affect other mixed-lineage leukemia (MLL) family histone methyltransferases (HMTs), revealing a unique regulatory feature for the MLL1 complex. Using MM-401 and its enantiomer control MM-NC-401, we show that inhibiting MLL1 methyltransferase activity specifically blocks proliferation of MLL cells by inducing cell-cycle arrest, apoptosis, and myeloid differentiation without general toxicity to normal bone marrow cells or non-MLL cells. More importantly, transcriptome analyses show that MM-401 induces changes in gene expression similar to those of MLL1 deletion, supporting a predominant role of MLL1 activity in regulating MLL1-dependent leukemia transcription program. We envision broad applications for MM-401 in basic and translational research.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Histones / Leukemia, Biphenotypic, Acute / Histone-Lysine N-Methyltransferase / Myeloid-Lymphoid Leukemia Protein Limits: Animals / Humans Language: En Journal: Mol Cell Journal subject: BIOLOGIA MOLECULAR Year: 2014 Document type: Article Affiliation country: United States Country of publication: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Histones / Leukemia, Biphenotypic, Acute / Histone-Lysine N-Methyltransferase / Myeloid-Lymphoid Leukemia Protein Limits: Animals / Humans Language: En Journal: Mol Cell Journal subject: BIOLOGIA MOLECULAR Year: 2014 Document type: Article Affiliation country: United States Country of publication: United States