Parallel Identification of O-GlcNAc-Modified Proteins from Cell Lysates

HC Tai, N Khidekel, SB Ficarro, EC Peters… - Journal of the …, 2004 - ACS Publications
HC Tai, N Khidekel, SB Ficarro, EC Peters, LC Hsieh-Wilson
Journal of the American Chemical Society, 2004ACS Publications
We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins
from cell lysates. The approach permits specific proteins of interest to be rapidly interrogated
for the modification in any tissue or cell type and can be extended to peptides to facilitate the
mapping of glycosylation sites. As an illustration of the approach, we identified four new O-
GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and
two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT). The ability to …
We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates. The approach permits specific proteins of interest to be rapidly interrogated for the modification in any tissue or cell type and can be extended to peptides to facilitate the mapping of glycosylation sites. As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT). The ability to target specific proteins across various tissue or cell types complements emerging proteomic technologies and should advance our understanding of this important posttranslational modification.
ACS Publications