CDK2 is highly similar to the gene products of Saccharomyces cerevisiae cdc28 and Schizosaccharomyces pombe cdc2, also known as CDK1 in humans . It acts as a catalytic subunit of the cyclin-dependent kinase complex, whose activity is tightly regulated by its association with cyclins, such as cyclin E and cyclin A . Cyclin E binds to CDK2 during the G1 phase, facilitating the transition to the S phase, while cyclin A binds to CDK2 to ensure progression through the S phase .
The activity of CDK2 is regulated by phosphorylation. Inhibitory phosphorylation occurs on threonine 14 and tyrosine 15, while activation requires phosphorylation on threonine 160 . This precise regulation ensures that CDK2 activity is restricted to specific phases of the cell cycle, preventing uncontrolled cell division.
CDK2 is essential for the proper progression of the cell cycle. It has been shown to be indispensable for the G1-S phase transition, although recent studies suggest that cells lacking CDK2 can still progress through the cell cycle, albeit with a lengthened G1 phase . CDK2 is also crucial for meiosis, as its deletion in mice leads to reproductive sterility due to the arrest of germ cells at the prophase of meiosis .
Recombinant human CDK2 is produced using genetic engineering techniques, where the CDK2 gene is cloned and expressed in suitable host cells, such as Escherichia coli or yeast. The recombinant protein is then purified for use in various research applications, including studies on cell cycle regulation, cancer research, and drug development .
CDK2 is a target for cancer research due to its role in cell cycle regulation. Inhibitors of CDK2 are being investigated as potential therapeutic agents for cancer treatment. Additionally, recombinant CDK2 is used in biochemical assays to study its interactions with cyclins and other regulatory proteins, as well as to identify potential substrates and inhibitors .