GPCRs can be phosphorylated on multiple sites following agonist stimulation. We show here that a range of protein kinases (not just the GRKs) are able to mediate agonist-dependent receptor phosphorylation. Furthermore, we provide evidence that different receptor kinases phosphorylate receptors on different sites and the signalling outcome of receptor phosphorylation is dependent on which receptor kinase is employed in the phosphorylation. Finally, by use of a transgenic mouse expressing a muscarinic receptor mutant that is unable to undergo phosphorylation we investigate a novel role of receptor phosphorylation in neuronal function.
Life Sciences 2007 (2007) Proc Life Sciences, SA189
Research Symposium: Novel aspects of GPCR regulation by phosphorylation
A. B. Tobin1, B. Poulin1, P. McWilliams1, R. Pawlak1
1. Cell Physiology and Pharmacology, University of Leicester, Leicester, United Kingdom.
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Where applicable, experiments conform with Society ethical requirements.