The O-GlcNAc Modification
- PMID: 35536957
- Bookshelf ID: NBK579950
- DOI: 10.1101/glycobiology.4e.19
The O-GlcNAc Modification
Excerpt
This chapter presents an overview of the dynamic modification of serine or threonine hydroxyl moieties on nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine, termed O-β-GlcNAc or simply O-GlcNAc. This seemingly simple carbohydrate modification plays key roles in cellular physiology and disease progression. Underpinning these observations are the thousands of O-GlcNAc-modified (O-GlcNAcylated) proteins that regulate cellular processes, such as epigenetics, gene expression, translation, protein degradation, signal transduction, mitochondrial bioenergetics, the cell cycle, and protein localization.
Copyright © 2022 The Consortium of Glycobiology Editors, La Jolla, California; published by Cold Spring Harbor Laboratory Press; doi:10.1101/glycobiology.4e.19. All rights reserved.
Sections
- HISTORICAL BACKGROUND
- WHY DID O-GlcNAc REMAIN UNDETECTED FOR SO LONG?
- ENZYMES CONTROLLING O-GlcNAc CYCLING
- O-GlcNAc IS A HIGHLY DYNAMIC MODIFICATION
- O-GlcNAc IS UBIQUITOUS AND ESSENTIAL IN METAZOANS
- O-GlcNAc HAS A COMPLEX DYNAMIC INTERPLAY WITH O-PHOSPHATE
- BIOLOGICAL FUNCTIONS OF O-GlcNAc
- FUTURE DIRECTIONS
- ACKNOWLEDGMENTS
- FURTHER READING
References
Publication types
LinkOut - more resources
Full Text Sources