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J Biol Chem

Title:		Regulation of Dauer formation by O-GlcNAcylation in Caenorhabditis elegans
Author(s):		Lee J; Kim KY; Lee J; Paik YK;
Address:		"Yonsei Proteome Research Center, World Class University Program, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea"
Journal Title:		J Biol Chem
Year:		2010
Volume:		20091123
Issue:		5
Page Number:		2930 - 2939
DOI:		10.1074/jbc.M109.022665
ISSN/ISBN:		1083-351X (Electronic) 0021-9258 (Print) 0021-9258 (Linking)
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"
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/*genetic;"
Notes:		"MedlineLee, Jeeyong Kim, Kwang-Youl Lee, Jihyun Paik, Young-Ki eng Research Support, Non-U.S. Gov't 2009/11/27 J Biol Chem. 2010 Jan 29; 285(5):2930-9. doi: 10.1074/jbc.M109.022665. Epub 2009 Nov 23"