Regulation of differentiation by a PHD domain in the NUP98-PHF23 fusion protein

Leuk Res. 2010 Aug;34(8):1094-7. doi: 10.1016/j.leukres.2010.02.015. Epub 2010 Mar 12.

Abstract

Acute myeloid leukemia (AML) is frequently associated with chromosomal translocations. These translocations produce specific fusion genes that play crucial roles in leukemogenesis. We recently identified a novel NUP98-PHF23 fusion in AML. In this study, we attempt to determine the role of NUP98-PHF23 protein and its plant homeodomain (PHD) and coiled-coil domain in regulation of cellular differentiation and protein distribution. We provide evidence that NUP98-PHF23, through its PHD domain, impairs TPA-induced differentiation of K562 cells. While the fusion protein localizes to the nucleus, its deletion mutant without the PHD domain resides exclusively in the nucleolus, suggesting a potential link between chromatin-binding PHD domain and nuclear architecture.

MeSH terms

  • Animals
  • Blotting, Western
  • Cell Differentiation / drug effects
  • Cell Differentiation / physiology*
  • Cell Nucleus / metabolism
  • Flow Cytometry
  • Homeodomain Proteins / genetics*
  • Homeodomain Proteins / metabolism
  • Humans
  • K562 Cells
  • Leukemia, Myeloid, Acute / genetics*
  • Leukemia, Myeloid, Acute / metabolism
  • Leukemia, Myeloid, Acute / pathology*
  • Mice
  • NIH 3T3 Cells
  • Nuclear Pore Complex Proteins / genetics*
  • Nuclear Pore Complex Proteins / metabolism
  • Oncogene Proteins, Fusion / genetics*
  • Oncogene Proteins, Fusion / metabolism
  • Protein Structure, Tertiary
  • Pyridines / pharmacology
  • Sequence Deletion
  • Translocation, Genetic

Substances

  • Homeodomain Proteins
  • Nuclear Pore Complex Proteins
  • Nup98 protein, human
  • Oncogene Proteins, Fusion
  • PHF23 protein, human
  • Pyridines
  • tris(2-pyridylmethyl)amine