Abstract
The phosphorylation of seryl, threonyl and tyrosyl residues is in most instances a reversible process, affecting only a minority of the whole cellular proteins and resulting from the coordinated activity of protein kinases and protein phosphatases (reviewed in 1) . Both these classes of enzymes therefore must be endowed with more or less pronounced time and substrate selectivity. Timeliness is mainly ensured by extra- and intracellular stimuli, either directly or through the generation of second messengers, like cyclic nucleotides, Ca2+, diacylglycerols etc, and by physiological inhibitors, that can modulate the activity of the phosphorylating and dephosphorylating enzymes.
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Pinna, L.A. (1988). Structural Basis for the Specificity of Protein Phosphorylation and Dephosphorylation Processes. In: Zappia, V., Galletti, P., Porta, R., Wold, F. (eds) Advances in Post-Translational Modifications of Proteins and Aging. Advances in Experimental Medicine and Biology, vol 231. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-9042-8_35
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DOI: https://doi.org/10.1007/978-1-4684-9042-8_35
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