Yonghoon Kwon

Abstract G proteins and arrestins are key transducers for G protein-coupled receptor (GPCR) signaling, mediating distinct downstream pathways. Recent evidence suggests that G proteins and β-arrestins (βarrs) can directly or functionally interact. However, the molecular details and functional consequences of Gα–βarr interactions remain poorly understood. Here, we quantify the binding affinities between βarr1 and Gαs or Gαi1 in various activation states using microscale thermophoresis (MST).

Abstract G-protein-coupled receptors (GPCRs) control various downstream signaling pathways, with multiple effectors whose interactions are subject to sophisticated regulation to achieve signaling specificity. Spatiotemporal organization of GPCR signaling is essential for efficient control of multifaceted signaling pathways.

Abstract G-protein-coupled receptors (GPCRs), the largest family of signalling receptors, as well as important drug targets, are known to activate extracellular-signal-regulated kinase (ERK)—a master regulator of cell proliferation and survival1. However, the precise mechanisms that underlie GPCR-mediated ERK activation are not clearly understood2,3,4. Here we investigated how spatially organized β2-adrenergic receptor (β2AR) signalling controls ERK.