Sungkyunkwan University · 生化学・遺伝学・分子生物学
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 mechanisms underlying GPCR activation and arrestin-mediated signaling. A key research direction involves developing innovative strategies—like using high-density lipoprotein (HDL) particles—to study low-abundance, membrane-embedded signaling complexes in physiologically relevant environments. The lab also explores the functional diversity of ion transporter splice variants and the societal impact of transnational media, particularly the Korean Wave (Hallyu), on North Korean defectors.
Figures are computed from collected data and may differ slightly.
The 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
Tissue-specific splice variants of Na(+)/Ca(2+) exchangers contain 2 Ca(2+)-binding regulatory domains (CBDs), CBD1 and CBD2. Ca(2+) interaction with CBD1 activates sodium-calcium exchangers (NCXs), and Ca(2+) binding to CBD2 alleviates Na(+)-dependent inactivation. A combination of mutually exclusive (A, B) and cassette (C-F) exons in CBD2 raises functionally diverse splice variants through unknown mechanisms. Here, the effect of exons on CBDs backbone dynamics were investigated in the 2-domain
Open papers in the app to read, cite, and organize with AI.
