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Cyclin-dependent kinase 11(p110) activity in the absence of CK2

Nancy A Sachs1, Richard R Vaillancourt

  • 1Department of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, AZ 85721-0207, USA.

Biochimica Et Biophysica Acta
|December 4, 2003
PubMed

Insights

Cyclin-dependent kinase (CDK)11(p110) activity is regulated by the kinase CK2, which phosphorylates CDK11(p110) at Ser227. Purified CDK11(p110) retains kinase activity but does not phosphorylate RNA polymerase II CTD, unlike CK2.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • Cyclin-dependent kinase (CDK)11(p110), also known as PITSLRE, is a serine/threonine kinase implicated in transcription and RNA processing.
  • Understanding the regulation of CDK11(p110) catalytic activity is crucial for elucidating its cellular functions.

Purpose of the Study:

  • To identify proteins interacting with CDK11(p110) and investigate its regulatory mechanisms.
  • To characterize the phosphorylation of CDK11(p110) and its kinase activity.

Main Methods:

  • Protein identification using liquid chromatography and tandem mass spectrometry (LC-MS/MS).
  • Immunoprecipitation of CDK11(p110) from COS-7 cells.
  • Expression and purification of recombinant CDK11(p110) from insect cells.
  • In vitro kinase assays using histone H1 and the RNA polymerase II CTD.

Main Results:

  • The serine/threonine kinase CK2 was identified as an interacting protein and kinase for CDK11(p110).
  • CDK11(p110) was found to be phosphorylated by CK2 at Ser227.
  • Recombinant CDK11(p110) retained kinase activity and phosphorylated histone H1.
  • Purified CDK11(p110) did not phosphorylate the carboxyl-terminal domain (CTD) of RNA polymerase II (RNAP II), whereas CK2 did.

Conclusions:

  • CK2 directly regulates CDK11(p110) activity through phosphorylation at Ser227.
  • CDK11(p110) and CK2 exhibit distinct substrate specificities, with CK2 being the primary kinase for the RNAP II CTD.

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