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Papers In Press, published online ahead of print November 8, 2002
J. Biol. Chem, 10.1074/jbc.M208787200
Submitted on August 27, 2002
Revised on October 30, 2002
Accepted on November 8, 2002

GRK2:Galpha q/11 interaction: A novel surface on an RGS homology domain for binding Galpha subunits

Rachel Sterne-Marr, John J. G. Tesmer, Peter W. Day, RoseAnn P. Stracquatanio, Jill-Ann E. Cilente, Katharine E. O'Connor, Alexey N. Pronin, Jeffrey L. Benovic, and Philip B. Wedegaertner

Biology Department, Siena College, Loudonville, NY 12211

Corresponding Author: sternemarr{at}siena.edu

G protein-coupled receptors (GPCRs) transduce signals from hormones, neurotransmitters, light and odorants by activating heterotrimeric guanine-nucleotide binding (G) proteins. Regulation of many GPCRs is initiated by agonist-dependent phosphorylation by GPCR kinases (GRKs), such as GRK2, resulting in G protein/receptor uncoupling. GRK2 also binds Galpha q/11 and inhibits Galpha q-stimulation of the effector phospholipase Cbeta . The binding site for Galpha q/11 resides in the amino terminal domain of GRK2 and is homologous to the Regulator of G protein Signaling (RGS) family of proteins. To map the Galpha q/11 binding site on GRK2, we carried out site-directed mutagenesis of the RGS homology (RH) domain of GRK2 expressed as a GST fusion protein and identified eight residues, which when mutated, alter binding to Galpha q/11. These mutations do not alter the ability of full-length GRK2 to phosphorylate rhodopsin, an activity that also requires the amino terminal domain. Mutations causing Galpha q/11 binding defects also impair recruitment to the plasma membrane by activated Galpha q when introduced into a GRK2(RH)-green fluorescent protein fusion, and regulation of Galpha q-stimulated phospholipase Cbeta activity when introduced into full-length GRK2. We demonstrate that the Galpha q/11 binding site on the GRK2 RH domain is distinct from the Galpha binding site on RGS4 and RGS9 (“A” site) and the APC binding site on axin (“B” site), and suggest that this novel protein interaction site on an RH domain be designated the “C” site. Additionally, GRK2 binds equally well to the G188S RGS-resistant mutant of Galpha q which suggests that the residues of Galpha q that form the interface for binding GRK2 are distinct from those used for binding the RH domain of RGS proteins.


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