Serine and threonine phosphorylation sites work in concert to provide rapid and reproducible desensitization of the G-protein coupled receptor rhodopsin.

Ligand-specific-induced conformations of M₃ muscarinic receptors reveal similar requirements for G protein-coupled receptor kinase 2 and G_q protein binding, whereas arrestin3 binding is mediated by distinct receptor conformations.

Heterotrimeric G proteins are coupled to and regulate plant receptor signaling, which allows optimum immune activation and enhances the production of reactive oxygen species.

FRET biosensor-based measurement of cAMP signaling and single-channel recording reveal that β-blockers trigger local activation of adrenergic receptors and calcium channels in primary neurons.

Signaling specifically in cilia by a cAMP generating G-protein-coupled receptor directs tissue-specific morphogenesis.

Protein kinase A regulates the rapid, activity-dependent genesis of excitatory synapses during striatal development.

TRPM3 inhibition is identified as a novel mechanism for G-protein βγ subunit signalling.

Pro-nociceptive and pro-inflammatory TRPM3 (transient receptor potential melastatin 3) channels, expressed in somatosensory neurons, are inhibited by activation of Gαi-coupled receptors, such as µ-opioid receptors, in vitro and in vivo.

In contrast with earlier conclusions, negative selection has a major role in cancer evolution.

Phosphoproteomics identifies β-arrestin 2 phosphorylation at Thr383 by MEK as a key step of GPCR-induced Erk½ activation, thus providing new insight into the molecular mechanism underlying β-arrestin-dependent GPCR-operated signaling.