Yongkyu Jang
Yonsei University
研究室紹介
Professor Yongkyu Jang's research lab focuses on the epigenetic regulation of cancer progression, with a particular emphasis on DNA methylation, histone modifications, and post-translational modifications of epigenetic regulators. The lab investigates how dysregulation of cytokines like LIF and co-stimulatory molecules like CD70 contributes to immune evasion and tumor survival in breast cancer. Using isogenic MCF10 models, the lab uncovers molecular mechanisms underlying epigenetic reprogramming in cancer, including the role of enzymes such as KDM4A and their SUMOylation in modulating tumor suppressor interactions. The research bridges epigenetics, cancer biology, and immunology to identify novel therapeutic targets.
Research Overview
Research Output Trend
Figures are computed from collected data and may differ slightly.
Selected Papers
3The interleukin 6 family of cytokines including leukemia inhibitory factor (LIF) regulates the progression of several types of cancer. However, although LIF overexpression during breast cancer progression was observed in our previous report, the molecular mechanisms responsible for this deregulation remain largely unknown. Here we show that LIF expression is epigenetically up-regulated via DNA demethylation and changes in histone methylation status within its promoter region in the isogenic MCF1
To escape the immune system, tumor cells may remove surface molecules such as the major histocompatibility complex (MHC) and co-stimulatory molecules, which are essential for recognition by lymphocytes. Down-regulation of the co-stimulatory molecules CD70 (TNFSF7) and CD80 may contribute to tumor cell survival; however, the mechanism of down-regulation of the TNFSF7 gene during tumorigenesis is poorly understood. Here we present evi-dence indicating that TNFSF7 gene expression is epigen-etically
The histone demethylase lysine-specific demethylase 4A (KDM4A/Jmjd2A) has diverse functions, including involvement in gene regulation and cell cycle, and plays an oncogenic role in cancer cells. The modulation of KDM4A through post-translational modifications remains unclear. Here, we show that small ubiquitin-like modifier (SUMO) 1-mediated modification of KDM4A was required for interaction with tumor suppressor p53. Our data revealed that KDM4A is mainly sumoylated at lysine residue 471. Howev