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Jong-kyung Jung

Seoul National University · Biochemistry, Genetics and Molecular Biology

About the Lab

Professor Jong-kyung Jung's research lab focuses on signal transduction pathways regulating cell survival, metabolism, and homeostasis, with a particular emphasis on the roles of kinases such as Akt, STATs, and LKB1 in cellular responses to growth factors, stress, and metabolic cues. The lab investigates molecular mechanisms underlying mitophagy, apoptosis, and energy metabolism, using Drosophila models to dissect conserved signaling networks relevant to human diseases like Parkinson’s disease, cancer, and metabolic disorders. Key areas include post-translational modifications (e.g., phosphorylation, ubiquitination) of signaling proteins and their impact on cellular fate decisions. The lab integrates genetic, biochemical, and cell biological approaches to uncover novel regulators and effectors in key signaling pathways.

signal transductionkinase regulationmitophagymetabolic homeostasisDrosophila models

Research Overview

Papers
143
Total Citations
14,390
Papers (5y)
17
Primary Field
Biochemistry, Genetics and Molecular Biology

Research Output Trend

Figures are computed from collected data and may differ slightly.

Publications per year (5y)
17total
2022
2023
2024
2025
2026
Citations per year (5y)
386total
20222023202420252026

Selected Papers

15
1
Article|724 citations·1994
PDGF- and insulin-dependent pp70S6k activation mediated by phosphatidylinositol-3-OH kinase
Jongkyeong Chung, Timothy C. Grammar, Katherine P. Lemon, Andrius Kazlauskas, John Blenis
SJR Q1Nature
Molecular BiologyBiochemistry, Genetics and Molecular Biology
2
Article|622 citations·1997
STAT3 Serine Phosphorylation by ERK-Dependent and -Independent Pathways Negatively Modulates Its Tyrosine Phosphorylation
Jongkyeong Chung, Eriko Uchida, Timothy C. Grammer, John Blenis
SJR Q2Molecular and Cellular BiologyOA

Recent studies have indicated that serine phosphorylation regulates the activities of STAT1 and STAT3. However, the kinase(s) responsible and the role of serine phosphorylation in STAT function remain unresolved. In the present studies, we examined the growth factor-dependent serine phosphorylation of STAT1 and STAT3. We provide in vitro and in vivo evidence that the ERK family of mitogen-activated protein (MAP) kinases, but not JNK or p38, specifically phosphorylate STAT3 at serine 727 in respo

OncologyMedicine
3
Article|414 citations·2007
Energy-dependent regulation of cell structure by AMP-activated protein kinase
Jun Hee Lee, Hyongjong Koh, Myung-Jin Kim, Yongsung Kim, Soo Young Lee, Roger E. Karess, Sang Hee Lee, Minho Shong, Jin‐Man Kim, Jaeseob Kim, Jongkyeong Chung
SJR Q1Nature
Molecular BiologyBiochemistry, Genetics and Molecular Biology
4
Article|385 citations·2008
PINK1 controls mitochondrial localization of Parkin through direct phosphorylation
Yong Sung Kim, Jeehye Park, Sunhong Kim, Saera Song, Seok‐Kyu Kwon, Sang‐Hee Lee, Tohru Kitada, Jin‐Man Kim, Jongkyeong Chung
SJR Q2Biochemical and Biophysical Research Communications
NeurologyMedicine
5
Article|274 citations·2020
Decision between mitophagy and apoptosis by Parkin via VDAC1 ubiquitination
Su Jin Ham, D. S. Lee, Heesuk Yoo, Kyoungho Jun, Hee-Jin Shin, Jongkyeong Chung
SJR Q1Proceedings of the National Academy of SciencesOA

Significance VDAC1 transports ions and small molecules at the mitochondrial outer membrane. In this study, we discover that Parkin, a frequently mutated Parkinson disease protein, ubiquitinates VDAC1 in two different manners, poly- and monoubiquitination. Interestingly, VDAC1 defective in polyubiquitination hinders Parkin-mediated mitophagy, but VDAC1 defective in monoubiquitination induces apoptosis. When VDAC1 deficient with monoubiquitination is expressed in mammalian cells and fruit fly, we

EpidemiologyMedicine
6
Article|215 citations·2005
Drosophila DJ-1 mutants show oxidative stress-sensitive locomotive dysfunction
Jeehye Park, Sung Yun Kim, Guang‐Ho Cha, Sung Bae Lee, Sunhong Kim, Jongkyeong Chung
SJR Q2Gene
NeurologyMedicine
7
Article|184 citations·2001
Cyclic AMP Inhibits Akt Activity by Blocking the Membrane Localization of PDK1
Sunhong Kim, Kwangho Jee, Dohoon Kim, Hyongjong Koh, Jongkyeong Chung
SJR Q1Journal of Biological ChemistryOA

Akt is a protein serine/threonine kinase that plays an important role in the mitogenic responses of cells to variable stimuli. Akt contains a pleckstrin homology (PH) domain and is activated by phosphorylation at threonine 308 and serine 473. Binding of 3'-OH phosphorylated phosphoinositides to the PH domain results in the translocation of Akt to the plasma membrane where it is activated by upstream kinases such as (phosphoinositide-dependent kinase-1 (PDK1). Over-expression of constitutively ac

Molecular BiologyBiochemistry, Genetics and Molecular Biology
8
Review|182 citations·2002
Akt: Versatile Mediator of Cell Survival and Beyond
Dohoon Kim, Jongkyeong Chung
SJR Q1BMB ReportsOA

The serine/threonine kinase Akt has been intensely studied for its role in growth factor-mediated cell survival for the past 5 years. On the other hand, the ongoing research effort has recently uncovered novel regulatory mechanisms and downstream effectors of Akt that demonstrate the involvement of Akt in other cellular functions such as cell cycle progression, angiogenesis, and cancer cell invasion/metastasis. Furthermore, recent studies using whole model organisms suggest additional roles for

Molecular BiologyBiochemistry, Genetics and Molecular Biology
9
Article|179 citations·2008
The PINK1–Parkin pathway is involved in the regulation of mitochondrial remodeling process
Jeehye Park, Gina Lee, Jongkyeong Chung
SJR Q2Biochemical and Biophysical Research Communications
NeurologyMedicine
10
Article|159 citations·2007
Loss of LRRK2/PARK8 induces degeneration of dopaminergic neurons in Drosophila
Sung Bae Lee, Won-Ho Kim, Sungkyu Lee, Jongkyeong Chung
SJR Q2Biochemical and Biophysical Research Communications
NeurologyMedicine
11
Article|129 citations·2010
A metazoan ortholog of SpoT hydrolyzes ppGpp and functions in starvation responses
Dawei Sun, Gina Lee, Jun Hee Lee, Hye Yeon Kim, Hyun‐Woo Rhee, Seung‐Yeol Park, Kyung Jin Kim, Yongsung Kim, Bo Yeon Kim, Jong In Hong, Chankyu Park, Hyon E. Choy
SJR Q1Nature Structural & Molecular Biology
Materials ChemistryMaterials Science
12
Article|117 citations·2000
Extracellular Zinc Activates p70 S6 Kinase through the Phosphatidylinositol 3-Kinase Signaling Pathway
Sunhong Kim, Young-Sun Jung, Dohoon Kim, Hyongjong Koh, Jongkyeong Chung
SJR Q1Journal of Biological ChemistryOA

We have studied a possible role of extracellular zinc ion in the activation of p70S6k, which plays an important role in the progression of cells from the G(1) to S phase of the cell cycle. Treatment of Swiss 3T3 cells with zinc sulfate led to the activation and phosphorylation of p70S6k in a dose-dependent manner. The activation of p70S6k by zinc treatment was biphasic, the early phase being at 30 min followed by the late phase at 120 min. The zinc-induced activation of p70S6k was partially inhi

Nutrition and DieteticsNursing
13
Article|98 citations·2016
Identification of a Peptidergic Pathway Critical to Satiety Responses in Drosophila
Soohong Min, Hyo-Seok Chae, Yong-Hoon Jang, Sekyu Choi, Sion Lee, Yong Taek Jeong, Walton D. Jones, Seok Jun Moon, Young‐Joon Kim, Jongkyeong Chung
SJR Q1Current BiologyOA
Cellular and Molecular NeuroscienceNeuroscience
14
Article|92 citations·2015
Feeding and Fasting Signals Converge on the LKB1-SIK3 Pathway to Regulate Lipid Metabolism in Drosophila
Sekyu Choi, Dae‐Sik Lim, Jongkyeong Chung
SJR Q1PLoS GeneticsOA

LKB1 plays important roles in governing energy homeostasis by regulating AMP-activated protein kinase (AMPK) and other AMPK-related kinases, including the salt-inducible kinases (SIKs). However, the roles and regulation of LKB1 in lipid metabolism are poorly understood. Here we show that Drosophila LKB1 mutants display decreased lipid storage and increased gene expression of brummer, the Drosophila homolog of adipose triglyceride lipase (ATGL). These phenotypes are consistent with those of SIK3

Molecular BiologyBiochemistry, Genetics and Molecular Biology
15
Article|77 citations·2003
In vivo p53 function is indispensable for DNA damage‐induced apoptotic signaling in Drosophila
Jun Hee Lee, Eunji Lee, Jeehye Park, Euysoo Kim, Jaeseob Kim, Jongkyeong Chung
SJR Q1FEBS LettersOA

p53 is a representative tumor suppressor whose dysfunction is a major cause of human cancer syndrome. Here we isolated flies lacking Dmp53, which encodes the single Drosophila orthologue of mammalian p53 family. Dmp53 null mutants well developed into adults, only displaying mild defects in longevity and fertility. However, genomic stability and viability of Dmp53 mutants dramatically decreased upon ionizing irradiation. Moreover, mutating Dmp53 abolished irradiation-induced apoptosis and reaper

OncologyMedicine

Research Areas

Molecular BiologyNeurologyOncologyCellular and Molecular NeuroscienceEpidemiologyImmunology

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