Yonsei University · Biochemistry, Genetics and Molecular Biology
Professor Jin Won Cho's research lab focuses on the molecular mechanisms of O-GlcNAcylation—a dynamic post-translational modification influenced by nutrient and stress signals—and its roles in metabolic diseases, cancer, and cellular differentiation. The lab investigates how dysregulation of O-GlcNAc cycling affects key cellular processes such as apoptosis, insulin resistance, and cardiomyocyte development, particularly under metabolic stress like hyperglycemia or glucose deprivation. Using models ranging from cancer cells and stem cells to pancreatic beta-cells and plant systems, the lab integrates proteomics, cell biology, and metabolic analysis to uncover the functional significance of O-GlcNAc modifications in health and disease. Recent work also extends to plant nutrient sensing, highlighting the conserved role of post-translational modifications in stress adaptation across kingdoms.
Figures are computed from collected data and may differ slightly.
When cellular glucose concentrations fall below normal levels, in general the extent of protein O-GlcNAc modification (O-GlcNAcylation) decreases. However, recent reports demonstrated increased O-GlcNAcylation by glucose deprivation in HepG2 and Neuro-2a cells. Here, we report increased O-GlcNAcylation in non-small cell lung carcinoma A549 cells and various other cells in response to glucose deprivation. Although the level of O-GlcNAc transferase was unchanged, the enzyme contained less O-GlcNAc
The enzymatic addition of a single β-D-N-acetylglucosamine sugar molecule on serine and/or threonine residues of protein chains is referred to as O-GlcNAcylation. This novel form of post-translational modification, first reported in 1984, is extremely abundant on nuclear and cytoplasmic proteins and has site specific cycling dynamics comparable to that of protein-phosphorylation. A nutrient and stress sensor, O-GlcNAc abnormalities underlie insulin resistance and glucose toxicity in diabetes, ne
Increased modification of proteins with O-linked N-acetylglucosamine (O-GlcNAc) has been implicated in the development of diabetic cardiomyopathy. We used the well-characterized ES cells (Nkx2.5GFP knock-in ES cells), to investigate the role of O-GlcNAcylation in cardiomyocyte development. O-GlcNAcylation decreased in differentiating ES cells, as did the expression of O-GlcNAc transferase. Increasing O-GlcNAcylation with glucosamine or by inhibiting N-acetylglucosaminidase (streptozotocin or PUG
Mineral nutrient deficiencies constitute major limitations for plant growth on agricultural soils around the world. To identify genes that possibly play roles in plant K(+) nutrition, we employed the comparative proteome analysis for proteins isolated from Arabidopsis seedlings treated with K(+) deficiency for 3 h and 7 d. We identified genes including those encoding putative transcription factors, protein kinases, and phosphatases, proteins involved in phytohormone biosynthesis or signaling, pr
Cuticle formation and molting are critical for the development of Caenorhabditis elegans. To understand cuticle formation more clearly, we screened for suppressors in transgenic worms that expressed dominant ROL-6 collagen proteins. The suro-1 mutant, which is mild dumpy, exhibited a different ROL-6::GFP localization pattern compared to other Dpy mutants. We identified mutations in three suro-1 mutants, and found that suro-1 (ORF R11A5.7) encodes a putative zinc-carboxypeptidase homologue. The e
Porosomes are the universal secretory machinery of the cell plasma membrane, where membrane-bound secretory vesicles transiently dock and fuse to expel intravesicular contents to the environment during cell secretion. In neurons, 12- to 17-nm cup-shaped lipoprotein structures possessing a central plug are present at the presynaptic membrane, where 40-50 nm in diameter synaptic vesicles transiently dock and fuse to release neurotransmitters. The neuronal porosome complex has been isolated, its co
Tyrosine O-sulfation is one of the post-translational modification processes that occur to membrane proteins and secreted proteins in eukaryotes. Tyrosylprotein sulfotransferase (TPST) is responsible for this modification, and in this report, we describe the expression pattern and the biological role of TPST-A in the nematode Caenorhabditis elegans. We found that TPST-A was mainly expressed in the hypodermis, especially in the seam cells. Reduction of TPST-A activity by RNAi caused severe defect
Abstract A simplified scheme for considering the thickness stress of shell elements induced by contact is presented which improves the accuracy of sheet metal forming analysis. The yield function formulated on the basis of plane stress conditions is modified to incorporate the effect of transverse normal stress induced by contact forces acting on shell elements and return mapping routine is used to update in‐plane stresses at each time step. The transverse normal stress distributions in the thic
Autophagy is a degradative pathway that plays an important role in maintaining cellular homeostasis. Dysfunction of autophagy is associated with the progression of neurodegenerative diseases including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis. Although one of the typical features of brain aging is an accumulation of redox-active metals that eventually lead to neurodegeneration, a plausible link between trace metal-induced neurodegeneration and dysregulated autop
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