Phosphorylation of Non-NMDA Glutamate Receptor Ion Channels
Modulation of physiological functions by protein phosphorylation is perhaps the most common form of cellular regulation, since up to 30% of cellular proteins can be phosphorylated (Levenson et al., 1990). Cyclic adenosine monophosphate (cAMP)-dependent protein phosphorylation was pioneered in the area of glycogen metabolism (reviewed in Krebs, 1993) in the 1950s and 1960s by Edwin Krebs and Edmond Fischer. However, it was well known from the work of Earl Sutherland (reviewed in Robison et al., 1971) that the second messenger cAMP altered many physiological processes in addition to glycogen metabolism. Thus, once the cAMP-dependent protein kinase A (PKA) was purified, it was quickly determined this kinase was multifunctional and could phosphorylate numerous proteins outside of glycogen metabolism. Other multifunctional Ser/Thr protein kinases were later characterized (e.g., casein kinases, protein kinase C [PKC], and Ca++/calmodulin-dependent protein kinase II [CaM-kinase II]), and identification of new protein kinases, including tyrosine-specific protein kinases, and their substrates proliferated during the 1970–1980s (reviewed in Hanks, 1988).
KeywordsGlutamate Receptor Glycogen Metabolism Membrane Topology Glutamate Receptor Subunit Regulatory Phosphorylation Site
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