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MLL fusion proteins are leukemogenic, but their mechanism is unclear. Induced dimerization of a truncated MLL immortalizes bone marrow and imposes a reversible block on myeloid differentiation associated with upregulation of Hox a7, a9, and Meis1. Both dimerized MLL and exon-duplicated MLL are potent transcriptional activators, suggesting a link between dimerization and partial tandem duplication of DNA binding domains of MLL. Dimerized MLL binds with higher affinity than undimerized MLL to a CpG island within the Hox a9 locus. However, MLL-AF9 is not dimerized in vivo. The data support a model in which either MLL dimerization/exon duplication or fusion to a transcriptional activator results in Hox gene upregulation and ultimately transformation.


Journal article


Cancer Cell

Publication Date





197 - 207


Animals, Bone Marrow Cells, Cell Survival, Cell Transformation, Neoplastic, Cells, Cultured, Cricetinae, Cricetulus, DNA-Binding Proteins, Dimerization, Gene Expression Regulation, Leukemic, Hematopoietic System, Histone-Lysine N-Methyltransferase, Homeodomain Proteins, Humans, Mice, Myeloid Ecotropic Viral Integration Site 1 Protein, Myeloid-Lymphoid Leukemia Protein, Neoplasm Proteins, Oncogene Proteins, Fusion, Protein Binding, Protein Structure, Tertiary, Proto-Oncogenes, Retroviridae, Trans-Activators, Transcription Factors