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MLL is essential for NUP98-HOXA9-induced leukemia.

Y Shima1, M Yumoto1, T Katsumoto1

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|February 18, 2017
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Summary

The NUP98-HOXA9 fusion protein drives leukemia by interacting with MLL. This interaction, specifically through the NUP98 FG repeat domain, is essential for recruiting the fusion protein to the HOXA locus and initiating leukemia.

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Area of Science:

  • Hematology
  • Molecular Biology
  • Cancer Research

Background:

  • Gene fusions involving NUP98 are implicated in acute myeloid leukemia and myelodysplastic syndromes.
  • The NUP98-HOXA9 fusion protein is a key driver in certain hematologic malignancies.

Purpose of the Study:

  • To investigate the role of the NUP98 FG repeat domain in NUP98-HOXA9-mediated leukemogenesis.
  • To elucidate the interaction between NUP98-HOXA9 and mixed lineage leukemia (MLL) and its functional significance.

Main Methods:

  • Functional assays to assess cell immortalization and leukemogenesis.
  • Co-immunoprecipitation to study protein interactions.
  • Chromatin immunoprecipitation to analyze gene locus recruitment and gene expression.

Main Results:

  • The second FG repeat domain of NUP98 is critical for NUP98-HOXA9's immortalization and leukemogenesis activities.
  • NUP98-HOXA9 interacts with MLL via its FG repeat domain.
  • MLL absence severely inhibits NUP98-HOXA9-induced cell immortalization and leukemogenesis.
  • MLL facilitates NUP98-HOXA9 recruitment to the HOXA locus and subsequent HOXA gene expression.

Conclusions:

  • The FG repeat domain of NUP98 is essential for the oncogenic function of NUP98-HOXA9.
  • MLL plays a crucial role in NUP98-HOXA9 leukemogenesis by mediating the recruitment and transcriptional activation of HOXA genes.