Casein kinase
Casein kinase is a type of protein kinase that phosphorylates serine and threonine residues in proteins. It is a ubiquitous and conserved enzyme that is involved in a wide range of cellular processes, including cell division, signal transduction, and protein synthesis.
Function[edit | edit source]
Casein kinase is named for its ability to phosphorylate the milk protein casein. However, it also phosphorylates a wide variety of other proteins, including histones, transcription factors, and structural proteins. This broad substrate specificity suggests that casein kinase plays a role in many different cellular processes.
The function of casein kinase is regulated by a variety of mechanisms. For example, the activity of the enzyme can be modulated by phosphorylation and dephosphorylation, as well as by binding to other proteins. In addition, the subcellular localization of casein kinase can also influence its function.
Types[edit | edit source]
There are two main types of casein kinase: Casein kinase 1 (CK1) and Casein kinase 2 (CK2).
CK1 is a monomeric enzyme that is involved in a variety of cellular processes, including cell cycle regulation, DNA repair, and circadian rhythm regulation. CK1 is also involved in the regulation of Wnt signaling, a key pathway in development and cancer.
CK2 is a tetrameric enzyme that consists of two catalytic subunits and two regulatory subunits. CK2 is involved in a wide range of cellular processes, including cell growth, cell differentiation, and apoptosis. CK2 is also implicated in a number of diseases, including cancer, neurodegenerative diseases, and inflammatory diseases.
Clinical significance[edit | edit source]
Given the wide range of cellular processes that casein kinase is involved in, it is not surprising that alterations in the function of this enzyme are associated with a variety of diseases. For example, overexpression of CK2 has been observed in a number of cancers, suggesting that this enzyme may play a role in tumorigenesis. In addition, mutations in CK1 have been linked to neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease.
See also[edit | edit source]
References[edit | edit source]
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