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Serotonin stimulates phosphorylation of Protein I in the facial motor nucleus of rat brain

Nature volume 289, pages 76–79 (1981)Cite this article

Abstract

Protein I is one of the best candidates for a neuronal protein whose phosphorylation may have a functional role in synaptic activity1. It is a substrate for both cyclic AMP-dependent2 and Ca2+-dependent3 protein kinases, and these kinases show differential specificity for its multiple phosphorylation sites4. Protein I is found exclusively in the central5 and peripheral6 nervous systems, and immunohistochemical5 and subcellular fractionation7 studies suggest an association primarily with synaptic vesicles. Using slices of rat cerebral cortex incubated in vitro, Protein I was phosphorylated both by agents which increase intracellular cyclic AMP and by agents causing Ca2+ influx, although not by any putative neurotransmitters or neuromodulators8. We have now examined the facial motor nucleus and report here that serotonin produces a phosphorylation of Protein I when incubated with facial nucleus slices. Demonstration of a neurotransmitter-dependent alteration in the state of phosphorylation of a synapse-specific protein may be due to the relatively simple neuronal circuitry within the facial motor nucleus.

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Author notes

  1. Annette C. Dolphin

    Present address: Division of Neurophysiology and Neuropharmacology, National Institute for Medical Research, Mill Hill, London, NW7 1AA, UK

Authors and Affiliations

  1. Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut, 06510

    Annette C. Dolphin & Paul Greengard

Authors
  1. Annette C. Dolphin
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  2. Paul Greengard
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Dolphin, A., Greengard, P. Serotonin stimulates phosphorylation of Protein I in the facial motor nucleus of rat brain. Nature 289, 76–79 (1981). https://doi.org/10.1038/289076a0

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