Abstract
Many biologically important molecules including oncogenes, growth factor receptors, transcription factors, immune cell receptors, protein kinases and cytoskeletal proteins are specifically and reversibly phosphorylated in response to physiological stimuli as well as during differentiation and normal eukaryotic cell cycle progression (1–3). Phosphorylation occurs primarily on the hydroxy 1 group of serine, threonine or tyrosine residues in proteins. While other residues, including histidine, lysine and glutamic acid may be phosphorylated, these phosphoamino acids are chemically less stable and their roles in physiological processes are relatively poorly understood. Protein phosphorylation is accomplished by protein kinases, which catalyze the transfer of phosphate from a nucleotide triphosphate, usually ATP, to the substrate protein. Protein kinases traditionally are grouped by amino acid homology as protein tyrosine kinases or as protein serine/threonine kinases, although a few dual specificity tyrosine/serine/threonine kinases have been described (4,5), and recently, an evolutionarily separate group of serine/threonine kinases related to the phospholipid kinases was discovered (6). Many tyrosine-specific kinases are cell surface receptors or are associated with the plasma membrane as illustrated by the epidermal growth factor, insulin and platelet-derived growth factor receptors (7,8). Serine/threonine kinases more frequently are involved in intracellular signaling and may be linked in cascades with receptor tyrosine kinases to transmit signals from the extracellular environment to the cell nucleus.
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Sakaguchi, K., Roller, P.P., Appella, E. (1996). Chemical Synthesis and Applications of Phosphopeptides. In: Setlow, J.K. (eds) Genetic Engineering. Genetic Engineering, vol 18. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1766-9_14
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