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

Kihong Lim, Hyo-Ihl Chang

Research output: Contribution to journalArticle

18 Citations (Scopus)

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 languageEnglish
Pages (from-to)314-318
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume393
Issue number2
DOIs
Publication statusPublished - 2010 Mar 5

Fingerprint

Sterol Regulatory Element Binding Protein 2
Acetylglucosamine
Proteins
Acetate-CoA Ligase
Lipids
Gene encoding
Monosaccharides
Biosynthesis
Threonine
Eukaryota
Serine
Gene Expression

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 journalArticle

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