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PIM1 kinase is destabilized by ribosomal stress causing inhibition of cell cycle progression

V Iadevaia1, S Caldarola, L Biondini

  • 1Department of Biology, University Tor Vergata, Roma, Italy.

Oncogene
|July 20, 2010
PubMed

Insights

Ribosomal stress destabilizes PIM1 kinase, a key regulator of cell proliferation. This destabilization halts cell growth, even without p53, suggesting PIM1 acts as a ribosomal stress sensor.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • PIM1 kinase regulates cell cycle and apoptosis, and its overexpression is linked to malignancies.
  • Ribosomal stress, a defect in ribosome synthesis, typically activates a p53-dependent growth arrest response.
  • PIM1 has been observed to interact with ribosomal protein S19 and cosediment with ribosomes.

Purpose of the Study:

  • To investigate the role of PIM1 in the cellular response to ribosomal stress.
  • To determine if PIM1 can act as a sensor for ribosomal stress.

Main Methods:

  • Ribosome synthesis alterations were induced in TF-1 and K562 erythroid cell lines.
  • Ribosomal protein (RP) deficiency was induced using RNA interference and nucleolar function inhibitors.
  • PIM1 levels, cell cycle inhibitor p27(Kip1), and cell proliferation were assessed.

Main Results:

  • RP deficiency led to a significant destabilization of PIM1.
  • Reduced PIM1 levels increased the cell cycle inhibitor p27(Kip1), causing cell proliferation arrest.
  • Restoring PIM1 levels via transfection recovered cell growth, even in p53-deficient cells.

Conclusions:

  • PIM1 destabilization is a consequence of ribosomal stress.
  • PIM1 functions as a sensor for ribosomal stress, potentially independent of or in conjunction with p53-dependent pathways.
  • PIM1's role in cell cycle regulation extends to responding to ribosomal biogenesis defects.

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