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- W1970784074 abstract "G protein-coupled receptors (GPCRs) are subject to the regulation by protein kinases. By controlling the phosphorylation-dephosphorylation balance, protein kinases actively modify GPCR expression and function. In a recent study, we have identified a novel phosphorylation-dependent regulation of Gαi/o-coupled muscarinic acetylcholine receptors. A synapse-enriched protein kinase, Ca2+/calmodulin-dependent protein kinase II (CaMKIIα), binds directly and selectively to second intracellular loops of muscarinic M4 receptors (M4Rs). This Ca2+-sensitive binding enables CaMKIIα to phosphorylate M4Rs at a selective threonine residue. In rat striatal neurons which abundantly express M4Rs, rapid cytoplasmic Ca2+ rises enhance the association of CaMKIIα with M4Rs and increase threonine phosphorylation of the receptor. This CaMKIIα-mediated phosphorylation results in a potentiation of M4R activity, which is critical for controlling cellular and behavioral responsivity to dopamine stimulation. In sum, our data identify a novel kinase-GPCR interaction. Through a Ca2+/activity-sensitive manner, CaMKIIα contributes to maintaining acetylcholine-dopamine homeostasis in the basal ganglia." @default.
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- W1970784074 date "2010-09-01" @default.
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- W1970784074 title "CaMKIIα, a modulator of M4 muscarinic acetylcholine receptors" @default.
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- W1970784074 doi "https://doi.org/10.4161/cib.3.5.12476" @default.
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