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Hee-jeong Choi

Seoul National University · 生化学・遺伝学・分子生物学

研究室紹介

Professor Hee-jeong Choi's research lab specializes in structural biology and biophysics, focusing on the molecular mechanisms underlying cell adhesion and signaling pathways. The lab investigates the structural organization and dynamic interactions of key proteins such as cadherins, catenins, and receptor complexes in adherens junctions and desmosomes, with a particular emphasis on how protein conformation and binding specificity regulate cellular function. Using advanced techniques like X-ray crystallography, cryo-electron microscopy, and single-molecule force spectroscopy, the lab explores the folding and assembly of membrane proteins and the structural basis of ligand-receptor interactions in G protein-coupled receptors and Wnt signaling components. Their work provides fundamental insights into diseases such as cancer and metabolic disorders linked to disrupted cell-cell adhesion and signaling.

structural biologycell adhesionWnt signalingmembrane protein foldingGPCR-ligand interactions

Research Overview

Papers
127
Total Citations
13,296
Papers (5y)
38
Primary Field
生化学・遺伝学・分子生物学

Research Output Trend

Figures are computed from collected data and may differ slightly.

Publications per year (5y)
38total
2022
2023
2024
2025
2026
Citations per year (5y)
388total
20222023202420252026

Selected Papers

15
1
Article|559 citations·2001
Structural Basis of the Redox Switch in the OxyR Transcription Factor
Hee‐Jung Choi, Seung-Jun Kim, Partha Mukhopadhyay, Sayeon Cho, Joo-Rang Woo, Gisela Storz, Seong-Eon Ryu
SJR Q1CellOA
Molecular BiologyBiochemistry, Genetics and Molecular Biology
2
Article|159 citations·2012
αE-catenin is an autoinhibited molecule that coactivates vinculin
Hee‐Jung Choi, Sabine Pokutta, G. Cadwell, Andrey A. Bobkov, Laurie A. Bankston, Robert Liddington, William I. Weis
SJR Q1Proceedings of the National Academy of Sciences

αE-catenin, an essential component of the adherens junction, interacts with the classical cadherin-β-catenin complex and with F-actin, but its precise role is unknown. αE-catenin also binds to the F-actin-binding protein vinculin, which also appears to be important in junction assembly. Vinculin and αE-catenin are homologs that contain a series of helical bundle domains, D1-D5. We mapped the vinculin-binding site to a sequence in D3a comprising the central two helices of a four-helix bundle. The

Cell BiologyBiochemistry, Genetics and Molecular Biology
3
Article|154 citations·2005
Thermodynamics of β-Catenin-Ligand Interactions
Hee‐Jung Choi, Andrew H. Huber, William I. Weis
SJR Q1Journal of Biological ChemistryOA

beta-Catenin is a structural component of adherens junctions, where it binds to the cytoplasmic domain of cadherin cell adhesion molecules. beta-Catenin is also a transcriptional coactivator in the Wnt signaling pathway, where it binds to Tcf/Lef family transcription factors. In the absence of a Wnt signal, nonjunctional beta-catenin is present in a multiprotein complex containing the proteins axin and adenomatous polyposis coli (APC), both of which bind directly to beta-catenin. The thermodynam

Molecular BiologyBiochemistry, Genetics and Molecular Biology
4
Article|138 citations·2002
Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure
Hee‐Jung Choi, S. Park-Snyder, Lauren T. Pascoe, Kathleen J. Green, William I. Weis
Nature Structural Biology
Cell BiologyBiochemistry, Genetics and Molecular Biology
5
Article|99 citations·2004
Structure of the Armadillo Repeat Domain of Plakophilin 1
Hee‐Jung Choi, William I. Weis
SJR Q1Journal of Molecular Biology
Molecular BiologyBiochemistry, Genetics and Molecular Biology
6
Article|90 citations·2019
Watching helical membrane proteins fold reveals a common N-to-C-terminal folding pathway
Hyun-Kyu Choi, Duyoung Min, Hyunook Kang, Min Ju Shon, Sang-Hyun Rah, Hak Chan Kim, Hawoong Jeong, Hee‐Jung Choi, James U. Bowie, Tae‐Young Yoon
SJR Q1ScienceOA

A pathway for helical membrane proteins Membrane proteins are inserted into cell membranes while they are being translated and may fold concurrently into their secondary and tertiary structures. Choi et al. describe a single-molecule force microscopy technique that allowed them to monitor folding of helical membrane proteins in vesicles and bicelles. Two helical membrane proteins, the Escherichia coli rhomboid protease GlpG and the human β 2 -adrenergic receptor, both folded from the N to the C

Molecular BiologyBiochemistry, Genetics and Molecular Biology
7
Article|88 citations·2009
Interactions of Plakoglobin and β-Catenin with Desmosomal Cadherins
Hee‐Jung Choi, Julia Christina Gross, Sabine Pokutta, William I. Weis
SJR Q1Journal of Biological ChemistryOA

Plakoglobin and beta-catenin are homologous armadillo repeat proteins found in adherens junctions, where they interact with the cytoplasmic domain of classical cadherins and with alpha-catenin. Plakoglobin, but normally not beta-catenin, is also a structural constituent of desmosomes, where it binds to the cytoplasmic domains of the desmosomal cadherins, desmogleins and desmocollins. Here, we report structural, biophysical, and biochemical studies aimed at understanding the molecular basis of se

Molecular BiologyBiochemistry, Genetics and Molecular Biology
8
Article|70 citations·2020
Sclerostin inhibits Wnt signaling through tandem interaction with two LRP6 ectodomains
Jinuk Kim, Wonhee Han, Taeyong Park, Eun‐Jin Kim, Injin Bang, Hyun Sik Lee, Yejin Jeong, Kyeonghwan Roh, Jeesoo Kim, Jong‐Seo Kim, Chanhee Kang, Chaok Seok
SJR Q1Nature CommunicationsOA

Low-density lipoprotein receptor-related protein 6 (LRP6) is a coreceptor of the β-catenin-dependent Wnt signaling pathway. The LRP6 ectodomain binds Wnt proteins, as well as Wnt inhibitors such as sclerostin (SOST), which negatively regulates Wnt signaling in osteocytes. Although LRP6 ectodomain 1 (E1) is known to interact with SOST, several unresolved questions remain, such as the reason why SOST binds to LRP6 E1E2 with higher affinity than to the E1 domain alone. Here, we present the crystal

Molecular BiologyBiochemistry, Genetics and Molecular Biology
9
Article|62 citations·2022
Structural basis of neuropeptide Y signaling through Y1 receptor
Chaehee Park, Jinuk Kim, Seung-Bum Ko, Yeol Kyo Choi, Hyeongseop Jeong, Hyeonuk Woo, Hyunook Kang, Injin Bang, Sang Ah Kim, Tae‐Young Yoon, Chaok Seok, Wonpil Im
SJR Q1Nature CommunicationsOA

Abstract Neuropeptide Y (NPY) is highly abundant in the brain and involved in various physiological processes related to food intake and anxiety, as well as human diseases such as obesity and cancer. However, the molecular details of the interactions between NPY and its receptors are poorly understood. Here, we report a cryo-electron microscopy structure of the NPY-bound neuropeptide Y1 receptor (Y 1 R) in complex with G i1 protein. The NPY C-terminal segment forming the extended conformation bi

Cellular and Molecular NeuroscienceNeuroscience
10
Article|61 citations·2011
Crystal Structure of a Rigid Four-Spectrin-Repeat Fragment of the Human Desmoplakin Plakin Domain
Hee‐Jung Choi, William I. Weis
SJR Q1Journal of Molecular Biology
Cell BiologyBiochemistry, Genetics and Molecular Biology
11
Article|53 citations·2023
Understanding the molecular mechanisms of odorant binding and activation of the human OR52 family
Chulwon Choi, Jungnam Bae, Seonghan Kim, Seho Lee, Hyunook Kang, Jinuk Kim, Injin Bang, Ki-Heon Kim, Won‐Ki Huh, Chaok Seok, Hahnbeom Park, Wonpil Im
SJR Q1Nature CommunicationsOA

Abstract Structural and mechanistic studies on human odorant receptors (ORs), key in olfactory signaling, are challenging because of their low surface expression in heterologous cells. The recent structure of OR51E2 bound to propionate provided molecular insight into odorant recognition, but the lack of an inactive OR structure limited understanding of the activation mechanism of ORs upon odorant binding. Here, we determined the cryo-electron microscopy structures of consensus OR52 (OR52 cs ), a

Sensory SystemsNeuroscience
12
Review|53 citations·2014
Structural Features of β2 Adrenergic Receptor: Crystal Structures and Beyond
Injin Bang, Hee‐Jung Choi
SJR Q1Molecules and CellsOA

The beta2-adrenergic receptor (β2AR) family, which is the largest family of cell surface receptors in humans. Extra attention has been focused on the human GPCRs because they have been studied as important protein targets for pharmaceutical drug development. In fact, approximately 40% of marketed drugs directly work on GPCRs. GPCRs respond to various extracellular stimuli, such as sensory signals, neurotransmitters, chemokines, and hormones, to induce structural changes at the cytoplasmic surfac

Molecular BiologyBiochemistry, Genetics and Molecular Biology
13
Article|46 citations·2020
Ultraviolet Photoactivated Room Temperature NO2 Gas Sensor of ZnO Hemitubes and Nanotubes Covered with TiO2 Nanoparticles
Hee‐Jung Choi, Soon-Hwan Kwon, Wonseok Lee, Kwang-Gyun Im, Tae Hyun Kim, Beom-Rae Noh, Sunghoon Park, Semi Oh, Kyoung‐Kook Kim
SJR Q1NanomaterialsOA

Prolonged exposure to NO2 can cause lung tissue inflammation, bronchiolitis fibrosa obliterans, and silo filler’s disease. In recent years, nanostructured semiconducting metal oxides have been widely used to fabricate gas sensors because of their unique structure and surface-to-volume ratio compared to layered materials. In particular, the different morphologies of ZnO-based nanostructures significantly affect the detection property of NO2 gas sensors. However, because of the large interaction e

Electrical and Electronic EngineeringEngineering
14
Article|30 citations·2015
A Conserved Phosphorylation Switch Controls the Interaction between Cadherin and β-Catenin In Vitro and In Vivo
Hee‐Jung Choi, Timothy Loveless, Allison M. Lynch, Injin Bang, Jeff Hardin, William I. Weis
SJR Q1Developmental CellOA
Molecular BiologyBiochemistry, Genetics and Molecular Biology
15
Article|29 citations·2017
Structural and functional characterization of Caenorhabditis elegans α-catenin reveals constitutive binding to β-catenin and F-actin
Hyunook Kang, Injin Bang, Kyeong Sik Jin, Boyun Lee, Junho Lee, Xiangqiang Shao, Jonathon A. Heier, Adam V. Kwiatkowski, W. James Nelson, Jeff Hardin, William I. Weis, Hee‐Jung Choi
SJR Q1Journal of Biological ChemistryOA

Intercellular epithelial junctions formed by classical cadherins, β-catenin, and the actin-binding protein α-catenin link the actin cytoskeletons of adjacent cells into a structural continuum. These assemblies transmit forces through the tissue and respond to intracellular and extracellular signals. However, the mechanisms of junctional assembly and regulation are poorly understood. Studies of cadherin-catenin assembly in a number of metazoans have revealed both similarities and unexpected diffe

Molecular BiologyBiochemistry, Genetics and Molecular Biology

Research Areas

Molecular BiologyCell BiologyGeneticsMaterials ChemistryCellular and Molecular NeuroscienceCancer Research

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