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Title: Phosphorylation and regulation of a G protein-coupled receptor by protein kinase CK2
Authors: Torrecilla, Ignacio
Spragg, Elizabeth J.
Poulin, Benoit
McWilliams, Phillip J.
Mistry, Sharad C.
Blaukat, Andree
Tobin, Andrew B.
First Published: 2-Apr-2007
Publisher: Rockefeller University Press
Citation: Journal of Cell Biology, 2007, 177 (1), pp. 127-137
Abstract: We demonstrate a role for protein kinase casein kinase 2 (CK2) in the phosphorylation and regulation of the M[subscript 3]-muscarinic receptor in transfected cells and cerebellar granule neurons. On agonist occupation, specific subsets of receptor phosphoacceptor sites (which include the SASSDEED motif in the third intracellular loop) are phosphorylated by CK2. Receptor phosphorylation mediated by CK2 specifically regulates receptor coupling to the Jun-kinase pathway. Importantly, other phosphorylation-dependent receptor processes are regulated by kinases distinct from CK2. We conclude that G protein–coupled receptors (GPCRs) can be phosphorylated in an agonist-dependent fashion by protein kinases from a diverse range of kinase families, not just the GPCR kinases, and that receptor phosphorylation by a defined kinase determines a specific signalling outcome. Furthermore, we demonstrate that the M[subscript 3]-muscarinic receptor can be differentially phosphorylated in different cell types, indicating that phosphorylation is a flexible regulatory process where the sites that are phosphorylated, and hence the signalling outcome, are dependent on the cell type in which the receptor is expressed.
DOI Link: 10.1083/jcb.200610018
ISSN: 0021-9525
eISSN: 1540-8140
Version: Publisher Version
Status: Peer-reviewed
Type: Article
Rights: Copyright © 2007 Rockefeller University Press. Deposited with reference to the publisher’s archiving policy available on the SHERPA/RoMEO website.
Appears in Collections:Published Articles, Dept. of Cell Physiology and Pharmacology

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