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Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags
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Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags
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Journal Article
Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags
2010
Overview
Current methods to investigate glycosylation allow the identification of modification sites but provide limited additional information. A new strategy using polymers to label specific sugars now shows a huge variety in the occupancy of known glycosylation sites as well as unexpected interplay between post-translational modifications.
Mechanistic studies of
O
-GlcNAc glycosylation have been limited by an inability to monitor the glycosylation stoichiometries of proteins obtained from cells. Here we describe a powerful method to visualize the
O
-GlcNAc–modified protein subpopulation using resolvable polyethylene glycol mass tags. This approach enables rapid quantification of
in vivo
glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels. In addition, it establishes the glycosylation state (for example, mono-, di-, tri-) of proteins, providing information regarding overall
O
-GlcNAc site occupancy that cannot be obtained using mass spectrometry. Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods. We anticipate that this mass-tagging strategy will advance our understanding of
O
-GlcNAc glycosylation, as well as other post-translational modifications and poorly understood glycosylation motifs.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Acetylglucosamine - analysis
/ Acetylglucosamine - chemistry
/ Acetylglucosamine - metabolism
/ Chemistry and Materials Science
/ Kinetics
/ Methyl-CpG-Binding Protein 2 - genetics
/ Methyl-CpG-Binding Protein 2 - metabolism
/ Polyethylene Glycols - analysis
/ Polyethylene Glycols - chemistry
/ Protein Processing, Post-Translational - genetics
/ Proteins
