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PMID:19940149
| Citation |
Lee, J, Kim, KY, Lee, J and Paik, YK (2010) Regulation of Dauer formation by O-GlcNAcylation in Caenorhabditis elegans. J. Biol. Chem. 285:2930-9 |
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| 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. |
| Links |
PubMed PMC2823417 Online version:10.1074/jbc.M109.022665 |
| Keywords |
Acetylglucosamine/metabolism; Active Transport, Cell Nucleus; Animals; Animals, Genetically Modified; Caenorhabditis elegans; Electrophoresis, Gel, Two-Dimensional; Mass Spectrometry/methods; Models, Biological; Mutation; N-Acetylglucosaminyltransferases/genetics; Protein Processing, Post-Translational; Proteomics/methods; Signal Transduction |
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