Abstract
O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine on the serine and threonine residues of nucleocytoplasmic proteins, is a novel protein modification that is ubiquitous among eukaryotes and implicated in cell regulation. Recent evidence indicates that O-GlcNAc regulates protein-protein interactions. Here we provide evidence that O-GlcNAc interrupts a known interaction between Sp1 and sterol regulatory element binding protein 2 (SREBP2), thereby inhibiting expression of the gene encoding acetyl-CoA synthetase 1, which is involved in lipid synthesis. This study suggests a novel mechanism in which lipid biosynthesis may be regulated by O-GlcNAc.
| Original language | English |
|---|---|
| Pages (from-to) | 314-318 |
| Number of pages | 5 |
| Journal | Biochemical and biophysical research communications |
| Volume | 393 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2010 Mar 5 |
Keywords
- Acetyl-CoA synthetase 1
- O-GlcNAc
- Sp1
- Sterol regulatory element binding protein 2
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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Lim, K., & Chang, H. I. (2010). O-GlcNAc inhibits interaction between Sp1 and sterol regulatory element binding protein 2. Biochemical and biophysical research communications, 393(2), 314-318. https://doi.org/10.1016/j.bbrc.2010.01.128