Abstract
Myriad nuclear and cytoplasmic proteins in metazoans are modified on Ser and Thr residues by the monosaccharide O-linked β-N-acetylglucosamine (O-GlcNAc). The rapid and dynamic change in O-GlcNAc levels in response to extracellular stimuli, morphogens, the cell cycle and development suggests a key role for O-GlcNAc in signal transduction pathways. Modulation of O-GlcNAc levels has profound effects on the functioning of cells, in part mediated through a complex interplay between O-GlcNAc and O-phosphate. In many well-studied proteins, the O-GlcNAc modification and phosphorylation are reciprocal. That is, they occur on different subsets of the protein population, as the site of attachment occurs on the same or adjacent Ser/Thr residues. Recently, O-GlcNAc has been implicated in the etiology of type II diabetes, the regulation of stress response pathways, and in the regulation of the proteasome.
Original language | English (US) |
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Pages (from-to) | 13-28 |
Number of pages | 16 |
Journal | Biochimica et Biophysica Acta - General Subjects |
Volume | 1673 |
Issue number | 1-2 |
DOIs | |
State | Published - Jul 6 2004 |
Keywords
- BAG
- C-terminal domain
- CK II
- CTD
- ER
- ERK
- Heat shock
- Hyperglycemia
- N-acetylglucosamine
- O-GlcNAc
- Phosphorylation
- Post-translational modification
- Stress
- benzyl-α-GalNAc
- casein kinase II
- eNOS
- endothelial nitric oxide synthase
- estrogen receptor
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology