Monitoring protein O-linked β-N-acetylglucosamine status via metabolic labeling and copper-free click chemistry

O-Linked β-N-acetylglucosamine (O-GlcNAc) modification found on the serine and threonine residues of intracellular proteins is an inducible post-translational modification that regulates numerous biological processes. In combination with other cell biological and biochemical approaches, a robust and...

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Bibliographic Details
Published inAnalytical biochemistry Vol. 464; pp. 70 - 72
Main Authors Teo, Chin Fen, Wells, Lance
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.11.2014
Subjects
Acetylglucosamine - metabolism
Azido sugars
Click Chemistry
Copper - chemistry
Cyclooctyne
O-GlcNAc stoichiometry
PEGylation
SPAAC
SPAAC
Azido sugars
PEGylation
O-GlcNAc stoichiometry
Cyclooctyne
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Summary:O-Linked β-N-acetylglucosamine (O-GlcNAc) modification found on the serine and threonine residues of intracellular proteins is an inducible post-translational modification that regulates numerous biological processes. In combination with other cell biological and biochemical approaches, a robust and streamlined strategy for detecting the number and stoichiometry of O-GlcNAc modification can provide valuable insights for decoding the functions of O-GlcNAc at the molecular level. Here, we report an optimized workflow for evaluating the O-GlcNAc status of proteins using a combination of metabolic labeling and click chemistry-based mass tagging. This method is strategically complementary to the chemoenzymatic-based mass-tagging method.
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ISSN:0003-2697
1096-0309
DOI:10.1016/j.ab.2014.06.010