Robert J. Lefkowitz

TL;DR: Evidence is provided that US28 is constitutively phosphorylated by GRKs in cells and that in consequence, β-arrestin 2 is localized to the plasma membrane and this result indicates that the carboxyl terminus of US28 contains an important signaling regulatory region and mutational analysis identified serine 323 as a critical residue within this region.

TL;DR: Results indicate that the β-adrenergic receptor polypeptide contains both the ligand binding site and the site responsible for mediating stimulation of adenylate cyclase activity, presumably via interaction with the guanine nucleotide regulatory protein.

TL;DR: It is established that phosphorylation of beta ARs by beta AR kinase is an essential step in homologous desensitization of the receptors, and suggested a potential therapeutic value of inhibitors of betaAR kinase in inhibiting agonist-induced desensitized cells.

TL;DR: Results demonstrate that both purification and photoaffinity labeling identify two polypeptides in turkey erythrocyte membranes as containing a beta 1-adrenergic receptor binding site.

TL;DR: The discovery of a small-molecule negative allosteric modulator (antagonist), compound 15, exhibiting a unique chemotype and low micromolar affinity for the β2AR is reported, establishing a generally applicable, proof-of-concept strategy for screening DNA-encoded small-Molecule libraries against purified G-protein–coupled receptors (GPCRs), which holds great potential for discovering therapeutic molecules.