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.
Research Overview
Research Output Trend
Figures are computed from collected data and may differ slightly.
Selected Papers
15Recent 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
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
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
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
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
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
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
Research Areas
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