Julie A. Pitcher

TL;DR: This review focuses on the regulation of GRK activity by a variety of allosteric and other factors: agonist-stimulated GPCRs, beta gamma subunits of heterotrimeric GTP- binding proteins, phospholipid cofactors, the calcium-binding proteins calmodulin and recoverin, posttranslational isoprenylation and palmitoylation, autophosphorylation, and protein kinase C-mediated GRK phosphorylation.

TL;DR: The rate and extent of the agonist-dependent phosphorylation of beta 2-adrenergic receptors and rhodopsin by Beta ARK are markedly enhanced on addition of G protein beta gamma subunits, suggesting that the enzyme preferentially binds specific beta gamma complexes.

TL;DR: It is reported here a direct agonist-promoted association of the β2-adrenergic receptor with the Na+/H+ exchanger regulatory factor (NHERF), a protein that regulates the activity of the Na-H- exchanger type 3 (NHE3).

TL;DR: It is demonstrated that glutathione S-transferase-fusion proteins, containing sequences encompassing the PH domain of nine proteins from this group, bind G beta gamma to varying extents, indicating that protein-protein interactions between G beta Gamma and PH domain-containing proteins may play a significant role in cellular signaling analogous to that previously demonstrated for Src homology 2 and 3 domains.

TL;DR: It is suggested that a conformational change in the receptor induced by acidification of the endosomal vesicles is the key determinant regulating receptor dephosphorylation and resensitization.