Abstract
There is now convincing evidence that protein phosphorylation mediates the physiological effects of a variety of extracellular signals on their target cells, both neuronal and non-neuronal. For many years, the hypothesis (Kuo and Greengard, 1969; Greengard, 1976) that protein phosphorylation mediates certain of the actions of neurotransmitters on target neurons was based largely on correlations between the state of phosphorylation of one or another substrate protein and the state of some physiological response in target neurons. However, during the past five or six years direct evidence has been obtained for a role of protein phosphorylation in the regulation of physiological processes in nerve cells. Thus, there is now evidence, based on intracellular injection experiments, that each of the four major classes of protein:kinases listed in Table I mediates the actions of certain neurotransmitters acting on their target nerve cells.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Castellucci, V. F., Kandel, E. R., Schwartz, J. H., Wilson, F. D., Nairn, A. C. and Greengard, P. (1980). Intracellular injection of the catalytic subunit of cyclic AMP-dependent protein kinase simulates facilitation of transmitter release underlying behavioral sensitization in Aplysia. Proc. Natl. Acad. Sci. U.S.A. 77, 7492–7496.
Castellucci, V. F., Nairn, A. C., Greengard, P., Schwartz, J. H. and Kandel, E. R. (1982). Inhibitor of adenosine 3’:5’monophosphate-dependent protein kinase blocks presynaptic facilitation in Aplysia. J. Neurosci. 2, 1673–1681.
DeRiemer, S. A., Strong, J. A., Albert, K. A., Greengard, P. and Kaczmarek, L. K. (1985). Enhancement of calcium current in Aplysia neurones by phorbol ester and protein kinase C. Nature 313, 313–316.
Gordon, A. S., Davis, C. G., Milfay, D. and Diamond, I. (1977). Phosphorylation of acetylcholine receptor by endogenous membrane protein kinase in receptor-enriched membranes of Torpedo californica. Nature 267, 539–540.
Greengard, P. (1976). Possible role for cyclic nucleotides and phosphorylated membrane proteins in the postsynaptic actions of neurotransmitters. Nature 260, 101–108.
Huganir, R. L. and Greengard, P. (1983). cAMP-dependent protein kinase phosphorylates the nicotinic acetylcholine receptor. Proc. Natl. Acad. Sci. U.S.A. 80, 1130–1134.
Huganir, R. L., Albert, K. A. and Greengard, P. (1983). Phophorylation of the nicotinic acetylcholine receptor by Ca /phospholipid-dependent protein kinase, and comparison with its phosphorylation by cAMP-dependent protein kinase. Abstracts of the 13th Annual Meeting of the Society for Neuroscience, p. 578.
Huganir, R. L., Miles, K. and Greengard, P. (1984). Phosphorylation of the nicotinic acetylcholine receptor by an endogenous tyrosine-specific protein kinase. Proc. Natl. Acad. Sci. U.S.A. 81, 6968–6972.
Huganir, R. L., Delcour, A. H., Greengard, P. and Hess, G. P. (1986). Phosphorylation of the nicotinic acetylcholine receptor regulates its rate of desensitization. Nature 321, 774–776.
Kaczmarek, L. K., Jennings, K. R., Strumwasser, F., Nairn, A. C., Walter, U., Wilson, F. D. and Greengard, P. (1980). Microinjection of catalytic subunit of cyclic AMP-dependent protein kinase enhances calcium action potentials of bag cell neurons in cell culture. Proc. Natl. Acad. Sci. U.S.A. 77, 7487–7491.
Kaczmarek, L. K., Nairn, A. C. and Greengard, P. (1984). Microinjection of protein kinase inhibitor prevents enhancement of action potentials in peptidergic neurons of Aplysia. Abstracts of the 14th Annual Meeting of the Society for Neuroscience, p. 895.
Kuo, J. F. and Greengard, P. (1969). Cyclic nucleotide-dependent protein kinases IV. Widespread occurrence of adenosine 3’:5’monophosphate-dependent protein kinase in various tissues and phyla of the animal kingdom. Proc. Natl. Acad. Sci., U.S.A. 64, 1349–1355.
LlinAs, R., McGuinness, T., Leonard, C. S., Sugimori, M. and Greengard, P. (1985). Intraterminal injection of synapsin I or calcium/calmodulin-dependent protein kinase II alters neurotransmitter release at the squid giant synapse. Proc. Natl. Acad. Sci. U.S.A. 82, 3035–3039.
Paupardin-Tritsch, D., Hammond, C., Gerschenfeld, H. M. (1986a). Serotonin and. cyclic GMP both induce an increase of the calcium current in the same identified molluscan neurons. J. Neurosci. 6, 2715–2723.
Paupardin-Tritsch, D., Hammond, C., Gerschenfeld, H. M., Nairn, A.C. and Greengard, P. (1986b). cGMP-dependent protein kinase enhances Ca grrent and potentiates the serotonin-induced increase of Ca current in identified snail neurones. Nature, in press.
Teichberg, V. I., Sobel, A. and Changeux, J.-P. (1977). In vitro phosphorylation of the acetylcholine receptor. Nature 267, 540–542.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1987 The Wenner-Gren Center
About this chapter
Cite this chapter
Greengard, P. (1987). Receptor-Receptor Interactions Mediated by Protein Phosphorylation. In: Fuxe, K., Agnati, L.F. (eds) Receptor-Receptor Interactions. Wenner-Gren Center International Symposium Series. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5415-4_36
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5415-4_36
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5417-8
Online ISBN: 978-1-4684-5415-4
eBook Packages: Springer Book Archive