Abstract
O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic posttranslational modification that, analogous to phosphorylation, cycles on and off serine and/or threonine hydroxyl groups. Cycling of O-GlcNAc is regulated by the concerted actions of O-GlcNAc transferase and O-GlcNAcase. GlcNAcylation is a nutrient/stress-sensitive modification that regulates proteins involved in a wide array of biological processes, including transcription, signaling, and metabolism. GlcNAcylation is involved in the etiology of glucose toxicity and chronic hyperglycemia-induced insulin resistance, a major hallmark of type 2 diabetes. Several reports demonstrate a strong positive correlation between GlcNAcylation and the development of insulin resistance. However, recent studies suggest that inhibiting GlcNAcylation does not prevent hyperglycemia-induced insulin resistance, suggesting that other mechanisms must also be involved. To date, proteomic analyses have identified more than 600 GlcNAcylated proteins in diverse functional classes. However, O-GlcNAc sites have been mapped on only a small percentage (
Original language | English (US) |
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Journal | American Journal of Physiology - Endocrinology and Metabolism |
Volume | 295 |
Issue number | 1 |
DOIs | |
State | Published - Jul 2008 |
Keywords
- β-N-acetylglucosaminidase
- Diabetes
- Hexosamine biosynthesis
- O-linked β-N- acetylglucosamine transferase
- O-linked β-N-acetylglucosamine
ASJC Scopus subject areas
- Physiology
- Physiology (medical)
- Endocrinology, Diabetes and Metabolism
- Endocrinology
- Biochemistry