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 |
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Keywords
- Acetyl-CoA synthetase 1
- O-GlcNAc
- Sp1
- Sterol regulatory element binding protein 2
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Molecular Biology
Cite this
O-GlcNAc inhibits interaction between Sp1 and sterol regulatory element binding protein 2. / Lim, Kihong; Chang, Hyo-Ihl.
In: Biochemical and Biophysical Research Communications, Vol. 393, No. 2, 05.03.2010, p. 314-318.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - O-GlcNAc inhibits interaction between Sp1 and sterol regulatory element binding protein 2
AU - Lim, Kihong
AU - Chang, Hyo-Ihl
PY - 2010/3/5
Y1 - 2010/3/5
N2 - 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.
AB - 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.
KW - Acetyl-CoA synthetase 1
KW - O-GlcNAc
KW - Sp1
KW - Sterol regulatory element binding protein 2
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U2 - 10.1016/j.bbrc.2010.01.128
DO - 10.1016/j.bbrc.2010.01.128
M3 - Article
C2 - 20138838
AN - SCOPUS:77649189817
VL - 393
SP - 314
EP - 318
JO - The BMJ
JF - The BMJ
SN - 0730-6512
IS - 2
ER -