Sung-hee Baek
Seoul National University · Biochemistry, Genetics and Molecular Biology
About the Lab
Professor Sung-hee Baek's research lab focuses on the molecular mechanisms underlying post-translational modifications (PTMs) and their roles in regulating protein stability, transcriptional regulation, and cellular signaling pathways. The lab investigates how PTMs such as methylation, O-GlcNAcylation, and demethylation by enzymes like LSD1 and SET7/9 modulate key transcription factors (e.g., HIF-1α, androgen receptor, Pitx2) and signaling hubs (e.g., ULK1, β-catenin) in development, cancer, and metabolic adaptation. A central theme is the dynamic interplay between PTMs and cellular stress responses, particularly under hypoxia and nutrient stress, with implications for disease mechanisms and therapeutic targeting. The lab integrates molecular biology, biochemistry, and genetic models to uncover novel regulatory nodes in disease pathways, especially in cancer and prostate cancer resistance.
Research Overview
Research Output Trend
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Selected Papers
15Post-translational modifications (PTMs) can occur on specific amino acids localized within regulatory domains of target proteins, which control a protein's stability. These regions, called degrons, are often controlled by PTMs, which act as signals to expedite protein degradation (PTM-activated degrons) or to forestall degradation and stabilize a protein (PTM-inactivated degrons). We summarize current knowledge of the regulation of protein stability by various PTMs. We aim to display the variety
Hypoxia-inducible factor-1α (HIF-1α) mediates hypoxic responses and regulates gene expression involved in angiogenesis, invasion and metabolism. Among the various HIF-1α posttranslational modifications, HIF-1α methylation and its physiological role have not yet been elucidated. Here we show that HIF-1α is methylated by SET7/9 methyltransferase, and that lysine-specific demethylase 1 reverses its methylation. The functional consequence of HIF-1α methylation is the modulation of HIF-1α stability p
Pitx2 is a bicoid-related homeodomain factor that is required for effective cell type-specific proliferation directly activating a specific growth-regulating gene cyclin D2. Here, we report that Pitx2, in response to the Wntbeta-catenin pathway and growth signals, also can regulate c-Myc and cyclin D1. Investigation of molecular mechanisms required for Pitx2-dependent proliferation, in these cases, further supports a nuclear role for beta-catenin in preventing the histone deacetylase 1-dependent
Lysine-specific demethylase 1 (LSD1) targets mono- or di-methylated histone H3K4 and H3K9 as well as non-histone substrates and functions in the regulation of gene expression as a transcriptional repressor or activator. This enzyme plays a pivotal role in various physiological processes, including development, differentiation, inflammation, thermogenesis, neuronal and cerebral physiology, and the maintenance of stemness in stem cells. LSD1 also participates in pathological processes, including c
Research Areas
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