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CDK11p46 and RPS8 associate with each other and suppress translation in a synergistic manner

Yuqing Hao1, Xiangfei Kong, Yuanyuan Ruan

  • 1Department of Biochemistry and Molecular Biology, Shanghai, Medical College, Fudan University, Shanghai, PR China.

Biochemical and Biophysical Research Communications
|March 5, 2011
PubMed

Insights

The study reveals that CDK11p46 interacts with ribosomal protein S8 (RPS8), inhibiting translation and enhancing apoptosis. This discovery offers new insights into cell death regulation.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • CDK11p46, an isoform of the PITSLRE kinase family, is implicated in apoptosis, but its precise mechanism is unclear.
  • Understanding the molecular players and pathways regulating apoptosis is crucial for developing targeted therapies.

Purpose of the Study:

  • To elucidate the mechanism by which CDK11p46 mediates apoptosis.
  • To identify novel interacting partners of CDK11p46 involved in apoptosis regulation.

Main Methods:

  • His pull-down assay and mass spectrometry were employed to identify CDK11p46 interacting partners.
  • In vitro and in vivo association studies confirmed the interaction between CDK11p46 and RPS8.
  • Functional assays assessed the impact of CDK11p46 and RPS8 on translation and apoptosis.

Main Results:

  • Ribosomal protein S8 (RPS8) was identified as a novel interacting partner of CDK11p46.
  • CDK11p46 and RPS8 were found to associate both in vitro and in vivo.
  • RPS8 is not a substrate of CDK11p46.
  • The combined action of CDK11p46 and RPS8 inhibits both cap-dependent and IRES-dependent translation.
  • CDK11p46 and RPS8 sensitize cells to Fas ligand-induced apoptosis.

Conclusions:

  • CDK11p46 plays a novel role in regulating protein translation.
  • CDK11p46 and RPS8 cooperate to inhibit translation and promote apoptosis.
  • This study provides new mechanistic insights into CDK11p46-mediated apoptosis.

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