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Inhibition of Cdk Activity

Inhibition of Cdk Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...

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Related Experiment Video

Updated: Dec 19, 2025

Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1

Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1

Published on: February 25, 2016

Quantifying CDK inhibitor selectivity in live cells.

Carrow I Wells¹, James D Vasta², Cesear R Corona²

¹Structural Genomics Consortium, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA.

Nature Communications

|June 4, 2020

Summary

This summary is machine-generated.

Researchers developed novel probes to measure Cyclin-Dependent Kinase inhibitor (CDKi) activity in live cells. This study offers a new method to evaluate CDKi selectivity and identifies potential new uses for existing drugs.

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Area of Science:

Biochemistry
Molecular Biology
Pharmacology

Background:

Cyclin-Dependent Kinase inhibitors (CDKi's) are crucial small molecule drugs and research tools.
Conflicting data exists regarding CDKi potency and selectivity, with a lack of systematic characterization against intracellular Cyclin-Dependent Kinases (CDKs).

Purpose of the Study:

To develop a method for quantifying target occupancy of all 21 human CDKs in live cells.
To comprehensively evaluate the intracellular potency and selectivity of 46 clinically-advanced CDKi's and tool molecules.
To provide a refined set of tool molecules for studying CDK function.

Main Methods:

Development of a panel of cell-permeable energy transfer probes.
Quantification of target occupancy for all 21 human CDKs in live cells.
Comprehensive evaluation of intracellular isozyme potency and selectivity for 46 CDKi's.

Main Results:

Observed unexpected intracellular activity profiles for several CDKi's.
Identified potential avenues for repurposing potent CDKi's as probes for previously unreported targets.
Established a broadly applicable method for evaluating CDK inhibitor selectivity in living cells.

Conclusions:

The developed method provides a robust way to assess CDK inhibitor selectivity in a cellular context.
The study refines the understanding of intracellular CDKi activity and offers new tool molecules for research.
Findings suggest potential for repurposing existing CDKi's for novel therapeutic or research applications.