Ka Young Chung
Sungkyunkwan University · 生化学・遺伝学・分子生物学
研究室紹介
Professor Ka Young Chung's research lab specializes in structural and dynamic mechanisms of G protein-coupled receptors (GPCRs) and β-arrestins, focusing on their conformational dynamics, signaling scaffolding, and interactions with intracellular effectors. The lab employs advanced biophysical techniques such as 19F NMR, hydrogen/deuterium exchange mass spectrometry, and fluorescence spectroscopy to dissect the molecular basis of GPCR activation and arrestin-mediated signaling. A key focus is understanding how receptor-ligand interactions and alternative splicing regulate signaling diversity and cellular responses, with translational implications for drug discovery and selective modulation of GPCR pathways.
Research Overview
Research Output Trend
Figures are computed from collected data and may differ slightly.
Selected Papers
15The G protein-coupled β(2)-adrenoreceptor (β(2)AR) signals through the heterotrimeric G proteins G(s) and G(i) and β-arrestin. As such, the energy landscape of β(2)AR-excited state conformers is expected to be complex. Upon tagging Cys-265 of β(2)AR with a trifluoromethyl probe, (19)F NMR was used to assess conformations and possible equilibria between states. Here, we report key differences in β(2)AR conformational dynamics associated with the detergents used to stabilize the receptor. In dodec
Arrestins were initially identified for their role in homologous desensitization and internalization of G protein-coupled receptors. Receptor-bound arrestins also initiate signaling by interacting with other signaling proteins. Arrestins scaffold MAPK signaling cascades, MAPK kinase kinase (MAP3K), MAPK kinase (MAP2K), and MAPK. In particular, arrestins facilitate ERK1/2 activation by scaffolding ERK1/2 (MAPK), MEK1 (MAP2K), and Raf (MAPK3). However, the structural mechanism underlying this scaf
G protein-coupled receptors (GPCRs) have critical roles in various physiological and pathophysiological processes, and more than 40% of marketed drugs target GPCRs. Although the canonical downstream target of an agonist-activated GPCR is a G protein heterotrimer; there is a growing body of evidence suggesting that other signaling molecules interact, directly or indirectly, with GPCRs. However, due to the low abundance in the intact cell system and poor solubility of GPCRs, identification of thes
Abstract Mammalian Na + /Ca 2+ exchangers, NCX1 and NCX3, generate splice variants, whereas NCX2 does not. The CBD1 and CBD2 domains form a regulatory tandem (CBD12), where Ca 2+ binding to CBD1 activates and Ca 2+ binding to CBD2 (bearing the splicing segment) alleviates the Na + -induced inactivation. Here, the NCX2-CBD12, NCX3-CBD12-B, and NCX3-CBD12-AC proteins were analyzed by small-angle X-ray scattering (SAXS) and hydrogen-deuterium exchange mass-spectrometry (HDX-MS) to resolve regulator