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Direct targeting and regulation of RNA polymerase II by cell signaling kinases

Preeti Dabas1, Meritxell B Cutrona1, Wojciech Rosikiewicz2

  • 1Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, TN, USA.

Science (New York, N.Y.)
|November 6, 2025
PubMed

Insights

Researchers identified 117 kinases that phosphorylate the RNA polymerase II (Pol II) CTD, revealing a code regulating gene transcription at signal-responsive genes. This finding links kinase activity to cellular physiology and disease.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Phosphorylation of the RNA polymerase II (Pol II) carboxyl-terminal domain (CTD) is crucial for gene transcription.
  • These distinct phosphorylation marks act as a code to recruit proteins specific to each transcription stage.

Purpose of the Study:

  • To identify kinases that phosphorylate the Pol II CTD.
  • To understand the role of these kinases in regulating signal-responsive genes.

Main Methods:

  • Screened approximately 80% of the human kinome for CTD phosphorylation activity.
  • Analyzed the positional selectivity of identified kinases on the CTD.

Main Results:

  • Identified 117 kinases that phosphorylate the Pol II CTD with high positional selectivity.
  • Found that these kinases selectively regulate Pol II at signal-responsive genes.
  • Demonstrated epidermal growth factor receptor (EGFR) as an example of direct Pol II regulation by a kinase.

Conclusions:

  • The study provides a comprehensive atlas of CTD kinases.
  • Pol II is a direct regulatory target for signal-transducing kinases involved in cellular functions and diseases.

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