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Updated: Jan 4, 2026

Combined Nucleotide and Protein Extractions in Caenorhabditis elegans
Published on: March 17, 2019
Chemoproteomic Profiling of O-GlcNAcylation in Caenorhabditis elegans
Wei Qin, Zhongyun Xie1, Jingyang Wang
1Tsinghua-Peking Center for Life Sciences, School of Life Sciences and MOE Key Laboratory for Protein Science, Tsinghua University, Beijing 100084, China.
Abstract:
Genetic studies have revealed essential functions of O-linked N-acetylglucosamine (O-GlcNAc) modification in Caenorhabditis elegans. However, large-scale identification of O-GlcNAcylated proteins and mapping the modification sites in C. elegans remain relatively unexplored. By using a chemoproteomic strategy, we herein report the identification of 108 high-confidence O-GlcNAcylated proteins and 64 modification sites in C. elegans. Furthermore, quantitative proteomics upon altering O-GlcNAcylation show that the abundance of a large number of proteins are affected by O-GlcNAc. These proteins are involved in regulating reproduction and lifespan, which may correlate with the previously observed phenotypes in genetic studies. The data set in this study reveals the O-GlcNAc modification landscape in C. elegans and provides a valuable resource for dissecting the biological function of O-GlcNAcylation.

