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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

The p34cdc2-related cyclin-dependent kinase 11 interacts with the p47 subunit of eukaryotic initiation factor 3

Jiaqi Shi1, Yongmei Feng, Anne-Christine Goulet

  • 1Department of Pathology, Arizona Cancer Center, University of Arizona, Tucson, Arizona 85724, USA.

The Journal of Biological Chemistry
|November 26, 2002
PubMed

Insights

Cyclin-dependent kinase 11 (CDK11) phosphorylates eukaryotic initiation factor 3 p47 (eIF3 p47) during apoptosis, inhibiting protein synthesis. This reveals a novel role for CDK11 in regulating cellular processes during programmed cell death.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Cyclin-dependent kinase 11 (CDK11) is implicated in cell cycle, tumorigenesis, and apoptosis.
  • Specific substrates of CDK11 during apoptosis remain unidentified.

Purpose of the Study:

  • To identify substrates of CDK11 during apoptosis.
  • To elucidate the function of CDK11-interacting proteins in apoptotic signaling.

Main Methods:

  • Yeast two-hybrid screening to identify CDK11 interacting partners.
  • In vitro and in vivo interaction assays.
  • In vitro kinase assays and reporter gene translation assays.
  • In vivo protein synthesis inhibition studies.

Main Results:

  • Eukaryotic initiation factor 3 p47 (eIF3 p47) was identified as a CDK11 interacting partner.
  • CDK11 directly phosphorylates eIF3 p47 at Serine 46 during apoptosis.
  • CDK11 inhibits reporter gene translation and cellular protein synthesis in a kinase-dependent manner.

Conclusions:

  • CDK11 directly interacts with and phosphorylates eIF3 p47 during apoptosis.
  • CDK11's kinase activity is crucial for inhibiting protein synthesis in apoptotic cells.
  • This study uncovers a novel mechanism for CDK11 in regulating protein synthesis during apoptosis.

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