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Updated: Jul 2, 2025

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Structural basis of Cdk7 activation by dual T-loop phosphorylation.
Robert Düster1,2, Kanchan Anand1, Sophie C Binder1
1Institute of Structural Biology, University of Bonn, Venusberg-Campus 1, 53127 Bonn, Germany.
Cyclin-dependent kinase 7 (Cdk7) dual T-loop phosphorylation regulates its activity. Phosphorylation at S164 supports complex formation, while T170 enhances kinase activity towards transcription substrates like RNA polymerase II.
Area of Science:
- Molecular Biology
- Biochemistry
- Structural Biology
Background:
- Cyclin-dependent kinase 7 (Cdk7) is crucial for cell-cycle progression and transcription.
- Cdk7 functions as a CDK-activating kinase (CAK) and a component of transcription factor TFIIH.
- Cdk7 activity is modulated by phosphorylation within its activation segment (T loop).
Conclusions:
- Dual T-loop phosphorylation fine-tunes Cdk7 activity and substrate specificity.
- pS164 facilitates tripartite complex formation and potentially Cdk7 processivity.
- pT170 boosts kinase activity toward key transcriptional substrates.
- The sequential phosphorylation of S164 followed by T170 represents a novel regulatory mechanism for Cdk7 in transcription.
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