CDK10

CDK10, also known as cyclin-dependent kinase 10, is a member of the cyclin-dependent kinase (CDK) family of serine/threonine protein kinases. CDKs play crucial roles in regulating the cell cycle, transcription, DNA damage response, and other cellular processes. CDK10 is distinct from other CDKs due to its unique structure and limited characterization compared to better-studied family members like CDK2 or CDK4.

CDK10 is encoded by the *CDK10* gene located on chromosome 17 in humans. Unlike many CDKs, CDK10 lacks a canonical cyclin-binding domain, which suggests it may not rely on cyclin partners for activation. Instead, its activity is regulated through phosphorylation by other kinases, such as CDK7, which phosphorylates CDK10 at threonine 14 and tyrosine 15, a mechanism similar to that seen in other CDKs. This phosphorylation typically inhibits CDK10 activity, while dephosphorylation by phosphatases like PP2A can activate it.

Early research indicates that CDK10 may be involved in RNA processing, particularly in the regulation of alternative splicing. Studies suggest it interacts with components of the spliceosome, a complex responsible for splicing pre-mRNA. However, its precise biological functions remain less defined compared to other CDKs, and its role in disease or human physiology is not yet fully understood. Some research has explored its potential involvement in cancer, though findings are preliminary and inconclusive.

CDK10 is expressed in various tissues, with notable levels detected in the brain, heart, and skeletal muscle. Its expression is often upregulated in certain cancer cell lines, but its functional significance in tumorigenesis is still under investigation. Further research is needed to clarify CDK10’s specific roles in cellular processes and its potential as a therapeutic target.