Please use this identifier to cite or link to this item:
|Title:||Phosphorylation and regulation of a G protein-coupled receptor by protein kinase CK2|
Spragg, Elizabeth J.
McWilliams, Phillip J.
Mistry, Sharad C.
Tobin, Andrew B.
|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.|
|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|
Files in This Item:
|10.1083_jcb.200610018.pdf||Published (publisher PDF)||3 MB||Adobe PDF||View/Open|
Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.