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Updated: Dec 21, 2025

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Chatterboxes: the structural and functional diversity of cyclins.
Natalie J Tatum1, Jane A Endicott1
1Cancer Research UK Newcastle Drug Discovery Unit, Newcastle Centre for Cancer, Translational and Clinical Research Institute, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom.
This review surveys human cyclin structures, focusing on their roles in cell processes and regulation via degradation. It highlights the cyclin box domain
Area of Science:
- Molecular and Structural Biology
- Cellular Biology
- Biochemistry
Background:
- Cyclins are a diverse protein family with a conserved cyclin box domain, crucial for cell cycle regulation.
- Structural characterization of cyclins is essential for understanding their diverse cellular functions.
- Only a fraction of cyclin-dependent kinase (CDK)-activating cyclins have been structurally elucidated.
Purpose of the Study:
- To review available structural data of human cyclins.
- To correlate structural features with cellular roles and regulatory mechanisms.
- To explore emerging cyclin functions beyond CDK activation.
Main Methods:
- Survey of existing X-ray crystallography and cryo-electron microscopy structural data for human cyclins.
- Analysis of molecular features and their implications in cellular processes.
- Review of literature on cyclin regulation, degradation, and non-CDK roles.
Main Results:
- Detailed examination of molecular features of structurally characterized human cyclins.
- Emphasis on the regulation of cyclin activity through degradation motif recognition and ubiquitination.
- Identification of cyclin box domains as versatile scaffolds for protein-protein interactions.
Conclusions:
- Structural insights are key to understanding cyclin functions and regulation.
- Cyclin activity is precisely controlled by degradation pathways.
- The cyclin box domain serves as a fundamental platform for diverse protein interactions, extending beyond kinase activation.
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