O-GlcNAc inhibits interaction between Sp1 and sterol regulatory element binding protein 2

Biochem Biophys Res Commun. 2010 Mar 5;393(2):314-8. doi: 10.1016/j.bbrc.2010.01.128. Epub 2010 Feb 6.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / metabolism*
  • Animals
  • Cell Line
  • Coenzyme A Ligases / genetics*
  • Gene Expression Regulation, Enzymologic*
  • Humans
  • Lipids / biosynthesis*
  • Lipids / genetics
  • Mice
  • Sp1 Transcription Factor / antagonists & inhibitors*
  • Sp1 Transcription Factor / metabolism
  • Sterol Regulatory Element Binding Protein 2 / antagonists & inhibitors*
  • Sterol Regulatory Element Binding Protein 2 / metabolism
  • Transcription, Genetic

Substances

  • Lipids
  • Sp1 Transcription Factor
  • Sterol Regulatory Element Binding Protein 2
  • Coenzyme A Ligases
  • acetate-CoA ligase (ADP-forming)
  • Acetylglucosamine