Abstract
An essential role for Ca2+- and calmodulin (CaM)-dependent events in neuronal transduction is suggested by the high amounts of this Ca2+binding protein in the central nervous system. Further, several enzymes that it modulates (adenylate cyclase, cyclic nucleotide phosphodiesterase, protein kinase and the phosphoprotein phosphatase, calcineurin) have their highest concentrations in the brain, implicating Ca2+- regulated cyclic nucleotide and phosphoprotein metabolism in intracellular signaling. Importantly, the multifunctional CaM-dependent protein kinase is known to be the major protein in post-synaptic densities1,2, consistent with a critical function for phosphoproteins in neurotransmission
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Kincaid, R.L., Martin, B.M. (1989). Characterization of the Calmodulin-Binding Domain of Calcineurin Deduced from a Complementary DNA Clone. In: Hidaka, H., Carafoli, E., Means, A.R., Tanaka, T. (eds) Calcium Protein Signaling. Advances in Experimental Medicine and Biology, vol 255. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5679-0_38
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DOI: https://doi.org/10.1007/978-1-4684-5679-0_38
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