Casein Kinase 2 (CK2) is a highly conserved serine/threonine protein kinase found in eukaryotic cells. It is known for its role in various cellular processes, including cell cycle regulation, apoptosis, and DNA repair. CK2 is unique due to its constitutive activity, meaning it does not require activation by external signals. The holoenzyme form of CK2 consists of two catalytic subunits (CK2α or CK2α’) and two regulatory subunits (CK2β), forming a tetrameric structure.
The human recombinant CK2 holoenzyme is typically produced using recombinant DNA technology. The process involves the following steps:
CK2 is known for its ability to phosphorylate a wide range of substrates, including proteins involved in signal transduction, transcription, and cell cycle control. The enzyme’s activity is characterized by its preference for acidic substrates and its resistance to inhibition by most protein kinase inhibitors.
CK2 plays a pivotal role in maintaining cellular homeostasis. Its dysregulation has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory diseases. The enzyme’s ability to phosphorylate a diverse set of substrates makes it a key player in cellular signaling networks.