Turning on a dimer: new insights into MLL chimeras.
In this issue of Cancer Cell, demonstrate a novel mechanism for the oncogenic activity of MLL chimeric proteins. By providing coiled-coil or other dimerization domains, the cytoplasmic partners of MLL fusion proteins donate a platform for MLL homodimerization, allowing recruitment of accessory factors needed to activate the critical downstream targets, including selected subsets of the major HOX genes.
Hsu
Karl
K
Harvard Medical School, Dana-Farber Cancer Institute, Boston, MA, USA.
Look
A Thomas
AT
D000818:Animals; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D019281:Dimerization; D015972:Gene Expression Regulation, Neoplastic; D011495:Histone-Lysine N-Methyltransferase; D018398:Homeodomain Proteins; D006801:Humans; D007938:Leukemia / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D051379:Mice; D051788:Myeloid-Lymphoid Leukemia Protein; D017434:Protein Structure, Tertiary; D011519:Proto-Oncogenes; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015534:Trans-Activators / Q000235:genetics; D014157:Transcription Factors; D015533:Transcriptional Activation
D004268:DNA-Binding Proteins; D018398:Homeodomain Proteins; C497422:KMT2A protein, human; D011993:Recombinant Fusion Proteins; D015534:Trans-Activators; D014157:Transcription Factors; D051788:Myeloid-Lymphoid Leukemia Protein; C088144:HoxA protein; D011495:Histone-Lysine N-Methyltransferase; C497423:Kmt2a protein, mouse