Protein Kinase in Disease 2.0

Dear Colleagues,

Protein kinases are enzymes that transfer ATP-γ-phosphate to the hydroxy groups of serine, threonine, and tyrosine residues of substrate proteins. Through phosphorylation of substrate proteins, protein kinases regulate their biological activity, cellular location, and interaction with other proteins to conduct signal transduction for cell proliferation, differentiation, and metabolism. The fine tuning of protein phosphorylation is crucial for orchestrating protein networks, which are essential for vital functions.  A total of 518 putative protein kinases have been identified in the human genome. They are divided into serine/threonine kinases and tyrosine kinases. The former group is further divided into seven subgroups (AGC, CAMK, CK1, CMGC, RGC, STE, and TKL), while the latter group is divided into two subgroups (receptor type and non-receptor type). Abnormality of protein kinases due to chromosomal mutation, translocation and deletion, aberrant splicing, and protein overexpression and loss of function is involved in developmental anomalies and various diseases such as cancers, inflammatory diseases, and metabolic disorders (e.g., diabetes mellitus). It is also related to the occurrence of cardiovascular diseases, neuronal degeneration, immune dysregulation, renal diseases, and sense organ disorders. Therapeutic strategies targeting these protein kinases are being explored. This has already led to the discovery of more than 40 protein kinase inhibitors as anticancer drugs. Further analysis of protein kinases associated with diseases and the development of novel protein kinase inhibitors may help to overcome intractable diseases.

Dr. Manae Suzuki Kurokawa
Guest Editor

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• protein kinases
• phosphorylation
• cancers
• inflammatory diseases
• protein kinase inhibitors
• anticancer drugs

• Protein Kinase in Disease in International Journal of Molecular Sciences (9 articles)