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Published September 1, 2004 | Supplemental Material
Journal Article Open

Parallel identification of O-GlcNAc-modified proteins from cell lysates

Abstract

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.

Additional Information

© 2004 American Chemical Society. Received April 13, 2004. Publication Date (Web): August 5, 2004. We thank Drs. B. Ramakrishnan and P. Qasba for providing the mutant GalT, Dr. M. Montminy for helpful discussions, Dr. J. Hanover for OGT cDNA, and Dr. P. Snow for protein expression. This research was supported by an NIH training grant (GM07616-21), California TRDRP (13DT-0065), NSF CAREER Award (CHE-0239861), and Alfred P. Sloan Fellowship.

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