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Large scale analysis of synaptic phosphorylation and O‐GlcNAcylation reveals complex interplay between these post‐translational modifications

O‐linked N‐acetylglucosamine (O‐GlcNAc) is a dynamic, reversible monosaccharide modifier of serine‐ and threonine‐residues on intracellular protein domains. Crosstalk between O‐GlcNAc and phosphorylation signaling mechanisms has been proposed. However, to date there has not been a large scale evaluation of these two PTMs at endogenous levels in any complex biological system. Here, we identified over 1,750 GlcNAcylation and16,500 phosphorylation sites from the same mouse brain synaptosomes.