Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 11, Issue 8, Pages 215-229Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.O112.018366
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Funding
- Biotechnology and Biological Sciences Research Council
- National Institutes of Health NIGMS [8P41GM103481]
- HHMI
- Dr. Miriam and Sheldon G. Adelson Medical Research Foundation
- [R01 GM083960]
- [P01 AI091575]
- [U54 GM094662]
- [P50 GM081879]
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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. Molecular & Cellular Proteomics 11: 10.1074/mcp.O112.018366, 215-229, 2012.
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