Global Identification and Characterization of Both O-GlcNAcylation and Phosphorylation at the Murine Synapse*

@article{Trinidad2012GlobalIA,
  title={Global Identification and Characterization of Both O-GlcNAcylation and Phosphorylation at the Murine Synapse*},
  author={Jonathan C. Trinidad and David T. Barkan and Brittany F Gulledge and Agnes Thalhammer and Andrej Sali and Ralf Schoepfer and Alma L. Burlingame},
  journal={Molecular \& Cellular Proteomics},
  year={2012},
  volume={11},
  pages={215 - 229}
}
O-linked N-acetylglucosamine (O-GlcNAc) is a dynamic, reversible monosaccharide modifier of serine and threonine residues on intracellular protein domains. Crosstalk between O-GlcNAcylation and phosphorylation has been hypothesized. Here, we identified over 1750 and 16,500 sites of O-GlcNAcylation and phosphorylation from murine synaptosomes, respectively. In total, 135 (7%) of all O-GlcNAcylation sites were also found to be sites of phosphorylation. Although many proteins were extensively… 

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