Conclusion
In summary, O-GlcNAc is a major form of post-translational modification on nuclear and cytoplasmic proteins of eukaryotic cells. Several lines of evidence suggest that O-GlcNAc is a regulated modification, much like phosphorylation. We have tested a potent in vitro inhibitor of the O-GlcNAc’ase on cells in culture and demonstrated that we can significantly increase the level of glycosylation on numerous proteins. Interestingly, the PUGNAc-induced increase in the O-GlcNAc level on the transcription factor Spl is accompanied by a complementary decrease i n phosphorylation. These data support the hypothesis that O-GlcNAc and phosphorylation may compete with each other for sites on proteins. Future studies using inhibitors such as PUGNAc should help us to understand the functional implications of O-GlcNAc modification on proteins.
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Haltiwanger, R.S. (1999). Novel Forms of Protein O-Glycosylation. In: Kitagawa, Y., Matsuda, T., Iijima, S. (eds) Animal Cell Technology: Basic & Applied Aspects., vol 1. Springer, Dordrecht. https://doi.org/10.1007/0-306-46865-4_2
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DOI: https://doi.org/10.1007/0-306-46865-4_2
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