Interaction of MLL amino terminal sequences with menin is required for transformation

Cancer Res. 2007 Aug 1;67(15):7275-83. doi: 10.1158/0008-5472.CAN-06-2369.

Abstract

Rearrangements of the mixed lineage leukemia gene MLL are associated with aggressive lymphoid and myeloid leukemias. The resulting MLL fusion proteins enforce high-level expression of HOX genes and the HOX cofactor MEIS1, which is pivotal for leukemogenesis. Both wild-type MLL and MLL fusion proteins interact with the tumor suppressor menin and with the Hoxa9 locus in vivo. Here, we show that MLL sequences between amino acids 5 and 44 are required for interaction with menin and for the transformation of hematopoietic progenitors. Blocking the MLL-menin interaction by the expression of a dominant negative inhibitor composed of amino terminal MLL sequences down-regulates Meis1 expression and inhibits cell proliferation, suggesting that targeting this interaction may be an effective therapeutic strategy for leukemias with MLL rearrangements.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Proliferation
  • Cell Transformation, Neoplastic*
  • Cells, Cultured
  • Chromatin Immunoprecipitation
  • Down-Regulation
  • Gene Expression
  • Histone-Lysine N-Methyltransferase
  • Homeodomain Proteins / genetics
  • Homeodomain Proteins / metabolism
  • Humans
  • Immunoprecipitation
  • Kidney / embryology
  • Leukemia, Myeloid / metabolism*
  • Myeloid Ecotropic Viral Integration Site 1 Protein
  • Myeloid-Lymphoid Leukemia Protein / metabolism*
  • Neoplasm Proteins / genetics
  • Neoplasm Proteins / metabolism
  • Polymerase Chain Reaction
  • Proto-Oncogene Proteins / metabolism*

Substances

  • Homeodomain Proteins
  • KMT2A protein, human
  • MEIS1 protein, human
  • MEN1 protein, human
  • Myeloid Ecotropic Viral Integration Site 1 Protein
  • Neoplasm Proteins
  • Proto-Oncogene Proteins
  • Myeloid-Lymphoid Leukemia Protein
  • Histone-Lysine N-Methyltransferase