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Updated: Jun 18, 2026
In Vivo Imaging of Dauer-specific Neuronal Remodeling in C. elegans
Published on: September 4, 2014
Regulation of Dauer formation by O-GlcNAcylation in Caenorhabditis elegans
Jeeyong Lee1, Kwang-Youl Kim, Jihyun Lee
1Yonsei Proteome Research Center, World Class University Program, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea.
Abstract:
Modification of proteins at serine or threonine residues with N-acetylglucosamine, termed O-GlcNAcylation, plays an important role in most eukaryotic cells. To understand the molecular mechanism by which O-GlcNAcylation regulates the entry of Caenorhabditis elegans into the non-aging dauer state, we performed proteomic studies using two mutant strains: the O-GlcNAc transferase-deficient ogt-1(ok430) strain and the O-GlcNAcase-defective oga-1(ok1207) strain. In the presence of the dauer pheromone daumone, ogt-1 showed suppression of dauer formation, whereas oga-1 exhibited enhancement of dauer formation. Consistent with these findings, treatment of wild-type N2 worms with low concentrations of daumone and the O-GlcNAcase inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) enhanced dauer formation, which was dependent on intact O-GlcNAcylation metabolism. We also found that the treatment of daumone enhanced O-GlcNAcylation in vivo. Seven proteins, identified by coupled two-dimensional electrophoresis/liquid chromatography-mass spectroscopy (LC-MS) analysis, were differentially expressed in oga-1(ok1207) worms compared with wild-type N2 worms. The identities of these proteins suggest that O- GlcNAcylation influences stress resistance, protein folding, and mitochondrial function. Using O-GlcNAc labeling with fluorescent dye combined with two-dimensional electrophoresis/LC-MS analysis, we also identified five proteins that were differentially O-GlcNAcylated during dauer formation. Analysis of these candidate O-GlcNAcylated proteins suggests that O-GlcNAcylation may regulate cytoskeleton modifications and protein turnover during dauer formation.
Insights
O-GlcNAcylation, a protein modification, regulates entry into the dauer state in C. elegans. Altering O-GlcNAc transferase or O-GlcNAc case levels impacts dauer formation, revealing O-GlcNAcylation
Area of Science:
- Molecular Biology
- Cellular Biology
- Biochemistry
Background:
- O-GlcNAcylation, the addition of N-acetylglucosamine to serine/threonine residues, is a crucial post-translational modification in eukaryotes.
- Understanding O-GlcNAcylation's role in cellular processes like aging and stress response is vital.
Purpose of the Study:
- To elucidate the molecular mechanisms of O-GlcNAcylation in regulating Caenorhabditis elegans entry into the dauer (non-aging) state.
- To identify proteins and pathways affected by O-GlcNAcylation during dauer formation.
Main Methods:
- Proteomic analysis using O-GlcNAc transferase (ogt-1) and O-GlcNAc case (oga-1) mutant strains in C. elegans.
- Two-dimensional electrophoresis coupled with liquid chromatography-mass spectroscopy (LC-MS) for protein identification and quantification.
- In vivo O-GlcNAc labeling with fluorescent dye.
Main Results:
- Mutations in ogt-1 suppressed dauer formation, while oga-1 mutations enhanced it, indicating O-GlcNAcylation's regulatory role.
- Treatment with dauer pheromone (daumone) and an O-GlcNAcase inhibitor (PUGNAc) promoted dauer formation, dependent on O-GlcNAcylation metabolism.
- Daumone treatment increased global O-GlcNAcylation levels in vivo.
- LC-MS identified differentially expressed proteins in oga-1 mutants, suggesting O-GlcNAcylation impacts stress resistance, protein folding, and mitochondrial function.
- Five proteins were identified as differentially O-GlcNAcylated during dauer formation, implicating O-GlcNAcylation in cytoskeleton modifications and protein turnover.
Conclusions:
- O-GlcNAcylation is a key regulator of entry into the C. elegans dauer state.
- The study identified specific proteins and pathways influenced by O-GlcNAcylation during dauer formation, including stress response and protein homeostasis.
- These findings provide insights into the complex role of O-GlcNAcylation in developmental transitions and aging.
