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Endogenous Gαq-Coupled Neuromodulator Receptors Activate Protein Kinase A.

Neuron | Dec 6, 2017

Protein kinase A (PKA) integrates inputs from G-protein-coupled neuromodulator receptors to modulate synaptic and cellular function. Gαs signaling stimulates PKA activity, whereas Gαi inhibits PKA activity. Gαq, on the other hand, signals through phospholipase C, and it remains unclear whether Gαq-coupled receptors signal to PKA in their native context. Here, using two independent optical reporters of PKA activity in acute mouse hippocampus slices, we show that endogenous Gαq-coupled muscarinic acetylcholine receptors activate PKA. Mechanistically, this effect is mediated by parallel signaling via either calcium or protein kinase C. Furthermore, multiple Gαq-coupled receptors modulate phosphorylation by PKA, a classical Gαs/Gαi effector. Thus, these results highlight PKA as a biochemical integrator of three major types of GPCRs and necessitate reconsideration of classic models used to predict neuronal signaling in response to the large family of Gαq-coupled receptors.

Pubmed ID: 29154125 RIS Download

Mesh terms: Animals | Calcium Signaling | Cyclic AMP-Dependent Protein Kinases | Enzyme Activation | Female | GTP-Binding Protein alpha Subunits, Gq-G11 | HEK293 Cells | Hippocampus | Humans | Mice | Mice, Inbred C57BL | Phosphorylation | Pregnancy | Protein Kinase C | Receptors, G-Protein-Coupled | Receptors, Muscarinic | Receptors, Neurotransmitter | Signal Transduction

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