Role of protein phosphorylation in neuronal signal transduction.

TitleRole of protein phosphorylation in neuronal signal transduction.
Publication TypeJournal Article
Year of Publication1989
AuthorsHemmings HC, Nairn AC, McGuinness TL, Huganir RL, Greengard P
JournalFASEB J
Volume3
Issue5
Pagination1583-92
Date Published1989 Mar
ISSN0892-6638
KeywordsAnimals, Dopamine and cAMP-Regulated Phosphoprotein 32, Nerve Tissue Proteins, Neurons, Phosphoproteins, Phosphorylation, Receptors, Nicotinic, Signal Transduction, Synapsins
Abstract

Protein phosphorylation is involved in the regulation of a wide variety of physiological processes in the nervous system. Studies in which purified protein kinases or kinase inhibitors have been microinjected into defined cells while a specific response is monitored have demonstrated that protein phosphorylation is both necessary and sufficient to mediate responses of excitable cells to extracellular signals. The precise molecular mechanisms involved in neuronal signal transduction processes can be further elucidated by identification and characterization of the substrate proteins for the various protein kinases. The roles of three such substrate proteins in signal transduction are described in this article: 1) synapsin I, whose phosphorylation increases neurotransmitter release and thereby modulates synaptic transmission presynaptically; 2) the nicotinic acetylcholine receptor, whose phosphorylation increases its rate of desensitization and thereby modulates synaptic transmission postsynaptically; and 3) DARPP-32, whose phosphorylation converts it to a protein phosphatase inhibitor and which thereby may mediate interactions between dopamine and other neurotransmitter systems. The characterization of the large number of additional phosphoproteins that have been found in the nervous system should elucidate many additional molecular mechanisms involved in signal transduction in neurons.

DOI10.1096/fasebj.3.5.2493406
Alternate JournalFASEB J
PubMed ID2493406
Grant ListMH-39327 / MH / NIMH NIH HHS / United States
MH-40899 / MH / NIMH NIH HHS / United States
NS-22789 / NS / NINDS NIH HHS / United States