Abstract
The large size and ready identifiability of molluscan neurones have made it possible to investigate the hypothesis1,2 that cyclic AMP-dependent protein phosphorylation may regulate neuronal electrical properties. For example, it has been found recently that intracellular application of the catalytic subunit of cyclic AMP-dependent protein kinase can alter the electrical activity of various molluscan neurones (refs 3, 4; J. De Peyer, H. Reuter and I.B.L., unpublished). We have recently demonstrated5 that injection of a specific protein kinase inhibitor into identified Aplysia neurone R15 blocks the increase in K+ conductance normally elicited in R15 by serotonin6, implicating protein phosphorylation in the regulation of a specific ion channel by a neurotransmitter. We report here attempts to identify phosphoproteins which may be involved in such regulation, by measuring protein phosphorylation in R15 following the intracellular injections of γ[-32P]ATP. The results indicate that we can indeed measure protein phosphorylation inside an individual living nerve cell, and that the extent of phosphorylation of several proteins in R15 is influenced by serotonin.
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Lemos, J., Novak-Hofer, I. & Levitan, I. Serotonin alters the phosphorylation of specific proteins inside a single living nerve cell. Nature 298, 64–65 (1982). https://doi.org/10.1038/298064a0
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DOI: https://doi.org/10.1038/298064a0
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