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

TitleGlobal Identification and Characterization of Both O-GlcNAcylation and Phosphorylation at the Murine Synapse.
Publication TypeJournal Article
2012
AuthorsTrinidad, JC, Barkan, DT, Gulledge, BF, Thalhammer, A, Sali, A, Schoepfer, R, Burlingame, AL
JournalMol Cell Proteomics
Volume11
Issue8
Pagination215-29
Date Published2012 Aug
ISSN1535-9484
22645316;PMCID:PMC3412957
283

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.

10.1074/mcp.O112.018366
PubMed ID22645316
PubMed Central IDPMC3412957
Alternate JournalMol. Cell Proteomics
PubMed ID22645316
PubMed Central IDPMC3412957
Order: 
283