Functional Roles of O-Glcnac in Cell Signaling

Sujin Park, Jin Won Cho

Research output: Chapter in Book/Report/Conference proceedingChapter


Many nuclear and cytosolic proteins are modified with O-linked β-N-acetylglucosamine (O-GlcNAc) at serine or threonine residues. This O-GlcNAcylation is a dynamic posttranslational modification similar to phosphorylation. In addition, O-GlcNAcylation and phosphorylation have a reciprocal relationship to modulate the function of proteins. There are three types of dynamic interplay between O-GlcNAcylation and phosphorylation. These two modifications occur on same site of the protein or occur on two different sites nearby. Therefore, there is a competitive relationship between O-GlcNAcylation and phosphorylation. The third possibility is these two modifications occur on multiple sites of proteins, and they affect each other or not. In this case, the modification status is changed by cellular signaling. O-GlcNAc modification has vital roles in protein localization, protein degradation, protein stability, transcription, translation, cell cycle regulation, protein-protein interaction, epigenetic regulation, and various diseases including cancer, diabetes, and neurodegenerative diseases. This chapter presents an overview of the function of O-GlcNAc modification in various signaling pathways.

Original languageEnglish
Title of host publicationGlycoscience
Subtitle of host publicationBiology and Medicine
PublisherSpringer Japan
Number of pages8
ISBN (Electronic)9784431548416
ISBN (Print)9784431548409
Publication statusPublished - 2015 Jan 1

Bibliographical note

Publisher Copyright:
© Springer Japan 2015.

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)


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