Abstract
Specific patterns of neuronal development in the brain are determined by complex interactions occurring at cell surfaces, but little is known about the enzymatic events that regulate these interactions. Protein phosphorylation, a ubiquitous step in intracellular pathways that produce rapid and transient changes in neuronal activity (Greengard, 1978; Nes-tler and Greengard, 1983; Ehrlich, 1984), was found to operate also as a key mechanism of molecular adaptation in processes whereby hormonal, pharmacological and behavioral inputs influence neuronal development and induce long-lasting alterations in neuronal function (Ehrlich and Routtenberg, 1975; Ehrlich et al., 1977, 1987: Neary et al., 1981; Kandel and Schwartz, 1982). The discovery of neuronal ecto-protein kinase activity (Ehrlich et al.,1986) has revealed that the powerful regulatory mechanism of protein phosphorylation operates also in the extracellular environment of the nervous system. In this location, the regulation of delicate interactions among cells, and between surface proteins and components of the extracellular matrix, can determine patterns of neuronal connectivity and thus play a significant role in processes underlying synaptic plasticity.
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Ehrlich, Y.H. et al. (1998). Surface Protein Phosphorylation by Ecto-Protein Kinases. In: Ehrlich, Y.H. (eds) Molecular and Cellular Mechanisms of Neuronal Plasticity. Advances in Experimental Medicine and Biology, vol 446. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4869-0_4
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