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Mol Cell Proteomics. 2012 Aug;11(8):215-29. doi: 10.1074/mcp.O112.018366. Epub 2012 May 29.

Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse.

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  • 1Department of Pharmaceutical Chemistry, UCSF, San Francisco, California 94158, USA.

Abstract

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 phosphorylated and minimally O-GlcNAcylated, proteins found to be extensively O-GlcNAcylated were almost always phosphorylated to a similar or greater extent, indicating the O-GlcNAcylation system is specifically targeting a subset of the proteome that is also phosphorylated. Both PTMs usually occur on disordered regions of protein structure, within which, the location of O-GlcNAcylation and phosphorylation is virtually random with respect to each other, suggesting that negative crosstalk at the structural level is not a common phenomenon. As a class, protein kinases are found to be more extensively O-GlcNAcylated than proteins in general, indicating the potential for crosstalk of phosphorylation with O-GlcNAcylation via regulation of enzymatic activity.

PMID:
22645316
PMCID:
PMC3412957
DOI:
10.1074/mcp.O112.018366
[PubMed - indexed for MEDLINE]
Free PMC Article
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