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

Kihong Lim, Hyo Ihl Chang

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)593-597
Number of pages5
JournalBiochemical and biophysical research communications
Issue number3
Publication statusPublished - 2009 May 8

Bibliographical note

Funding Information:
We are grateful to Dr. Roberto Mantovani for providing plasmids encoding NF-Y subunits. This work was supported by a Korea University grant.

Copyright 2009 Elsevier B.V., All rights reserved.


  • NF-Y
  • O-GlcNAc
  • Sp1
  • Transcription with NF-Y

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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