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Identification of FUSE-binding protein 1 as a regulatory mRNA-binding protein that represses nucleophosmin

M E Olanich1, B L Moss, D Piwnica-Worms

  • 1BRIGHT Institute, Washington University School of Medicine, St Louis, MO 63110, USA.

Oncogene
|August 31, 2010
PubMed

Insights

Far upstream element (FUSE)-binding protein 1 (FBP1) represses nucleophosmin (NPM) translation via its 3' untranslated region (UTR). FBP1 regulates cell growth and proliferation by controlling NPM protein levels.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Oncology

Background:

  • Nucleophosmin (NPM/B23) is a key oncoprotein regulating cell growth and proliferation.
  • The precise mechanism by which mammalian target of rapamycin (mTOR) signaling controls NPM translation remains unclear.

Purpose of the Study:

  • To elucidate the mechanism of translational regulation of NPM by mTOR signaling.
  • To identify regulatory elements and proteins involved in controlling NPM mRNA translation.

Main Methods:

  • Utilized chimeric translational reporters to assess the role of the NPM 3' untranslated region (UTR).
  • Investigated the interaction between far upstream element (FUSE)-binding protein 1 (FBP1) and the NPM 3' UTR.
  • Assessed the impact of FBP1 overexpression and depletion on NPM translation and cell proliferation.

Main Results:

  • The 3' UTR of NPM mRNA was found to be sufficient for translational modulation by mTOR signaling.
  • Far upstream element (FUSE)-binding protein 1 (FBP1) specifically binds to the NPM 3' UTR and represses translation.
  • FBP1 overexpression led to NPM translational repression, while FBP1 depletion significantly increased NPM translation and cell proliferation.

Conclusions:

  • Far upstream element (FUSE)-binding protein 1 (FBP1) acts as a crucial repressor of nucleophosmin (NPM) translation.
  • FBP1 regulates cell growth and proliferation by selectively binding the NPM 3' UTR, thereby controlling NPM protein levels.

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