Abstract
Protein phosphorylation is recognized as the primary mechanism for the transduction of extracellular stimuli into intracellular events (Cohen, 1982; Nestler et al.,1984). Ineukaryotes, for example, all of the biochemical actions of cAMP have been attributed to activation of cAMP-dependent protein kinase (Krebs and Beavo, 1979). Ca2+ has also been implicated as a second messenger by its ability to activate several calmodulin-dependent protein kinases and at least one phosphoprotein phosphatase (Cohen, 1985; Nairn et al., 1985). Another signal transduction pathway, the ubiquity of which has only recently been appreciated, is that of phosphatidylinositol (PI) turnover (Hokin and Hokin, 1953; Michell, 1975; for reviews, see Berridge, 1984; Hokin, 1985). Activation of this system causes hydrolysis of polyphosphoinositol lipids to form polyphosphoinositides, the most thoroughly studied of which is inositol-1,4,5-trisphosphate (hereafter termed IP3) and diacyglycerols (DAG). The primary role of IP3 is to stimulate the release of Ca2+ from intracellular stores, most probably the endoplasmic reticulum (Berridge, 1983; Streb et al.,1983), thus causing activation of Ca2+-dependent processes. The major function of DAGs is to activate a serine/threonine- specific protein kinase, termed protein kinase C (Takai et al., 1979a). The simultaneous formation of two second messengers by agonists of PI turnover endows this pathway with enhanced flexibility of response, greater possibilities of synergistic effects, and complex interactions with other signaling pathways, some aspects of which will be described below.
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Reference
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Woodgett, J.R., Hunter, T., Gould, K.L. (1987). Protein Kinase C and its Role in Cell Growth. In: Elson, E., Frazier, W., Glaser, L. (eds) Cell Membranes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1915-3_6
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