O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y

Biochem Biophys Res Commun. 2009 May 8;382(3):593-7. doi: 10.1016/j.bbrc.2009.03.075. Epub 2009 Mar 18.


O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation. Sp1 transcription factor is multiply modified by O-GlcNAc within its serine/threonine-rich region and glutamine-rich transactivation domain. In the present study, we show that O-GlcNAc of Sp1 serine/threonine-rich region interrupts a physical interaction between Sp1 and NF-YA, thus inhibiting Sp1-NF-Y cooperative activation of gene transcription. Our results strengthen the notion that O-GlcNAc regulates gene transcription by modulating the protein-protein interaction network among transcription regulatory proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / metabolism*
  • Acylation
  • CCAAT-Binding Factor / metabolism*
  • Cell Line
  • Humans
  • Immunoprecipitation
  • Promoter Regions, Genetic
  • Protein Structure, Tertiary
  • Sp1 Transcription Factor / metabolism*
  • Transcription, Genetic
  • Transcriptional Activation*


  • CCAAT-Binding Factor
  • NFYA protein, human
  • Sp1 Transcription Factor
  • Acetylglucosamine