Won Do Heo
Korea Advanced Institute of Science and Technology · 生化学・遺伝学・分子生物学
研究室紹介
Professor Won Do Heo's research lab specializes in cell signaling and membrane dynamics, with a focus on the spatiotemporal regulation of cellular processes through optogenetics, lipid-protein interactions, and real-time imaging of protein dynamics. The lab investigates how signaling molecules, cytoskeletal proteins, and ion channels are localized and regulated at subcellular membranes, particularly through phosphoinositide lipids and calcium signaling. A central theme is the development and application of innovative optical tools—such as light-sensitive proteins and single-molecule imaging techniques—to dissect dynamic cellular events in live cells and animal models with high precision. The lab also explores the roles of calmodulin isoforms and Rho GTPase regulators in plant and animal immune responses and morphogenesis.
Research Overview
Research Output Trend
Figures are computed from collected data and may differ slightly.
Selected Papers
15Many signaling, cytoskeletal, and transport proteins have to be localized to the plasma membrane (PM) in order to carry out their function. We surveyed PM-targeting mechanisms by imaging the subcellular localization of 125 fluorescent protein-conjugated Ras, Rab, Arf, and Rho proteins. Out of 48 proteins that were PM-localized, 37 contained clusters of positively charged amino acids. To test whether these polybasic clusters bind negatively charged phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2
The Ca2+ signal is essential for the activation of plant defense responses, but downstream components of the signaling pathway are still poorly defined. Here we demonstrate that specific calmodulin (CaM) isoforms are activated by infection or pathogen-derived elicitors and participate in Ca2+-mediated induction of plant disease resistance responses. Soybean CaM (SCaM)-4 and SCaM-5 genes, which encode for divergent CaM isoforms, were induced within 30 min by a fungal elicitor or pathogen, whereas
Protein homo-oligomerization is an important molecular mechanism in many biological processes. Therefore, the ability to control protein homo-oligomerization allows the manipulation and interrogation of numerous cellular events. To achieve this, cryptochrome 2 (CRY2) from Arabidopsis thaliana has been recently utilized for blue light-dependent spatiotemporal control of protein homo-oligomerization. However, limited knowledge on molecular characteristics of CRY2 obscures its widespread applicatio
Co-immunoprecipitation (co-IP) has become a standard technique, but its protein-band output provides only static, qualitative information about protein–protein interactions. Here we demonstrate a real-time single-molecule co-IP technique that generates real-time videos of individual protein–protein interactions as they occur in unpurified cell extracts. By analysing single Ras–Raf interactions with a 50-ms time resolution, we have observed transient intermediates of the protein–protein interacti
Pulsatile actomyosin contractility, important in tissue morphogenesis, has been studied mainly in apical but less in basal domains. Basal myosin oscillation underlying egg chamber elongation is regulated by both cell-matrix and cell-cell adhesions. However, the mechanism by which these two adhesions govern basal myosin oscillation and tissue elongation is unknown. Here we demonstrate that cell-matrix adhesion positively regulates basal junctional Rho1 activity and medio-basal ROCK and myosin act
Abstract Optogenetic approaches for controlling Ca 2+ channels provide powerful means for modulating diverse Ca 2+ -specific biological events in space and time. However, blue light-responsive photoreceptors are, in principle, considered inadequate for deep tissue stimulation unless accompanied by optic fiber insertion. Here, we present an ultra-light-sensitive optogenetic Ca 2+ modulator, named monSTIM1 encompassing engineered cryptochrome2 for manipulating Ca 2+ signaling in the brain of awake