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

Kihong Lim, Hyo-Ihl Chang

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

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
Volume382
Issue number3
DOIs
Publication statusPublished - 2009 May 8

Fingerprint

Transcription
Transcriptional Activation
Acetylglucosamine
Threonine
Serine
Sp1 Transcription Factor
Protein Interaction Maps
Proteins
Monosaccharides
Genes
Glutamine
Gene expression
Chemical activation

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y. / Lim, Kihong; Chang, Hyo-Ihl.

In: Biochemical and Biophysical Research Communications, Vol. 382, No. 3, 08.05.2009, p. 593-597.

Research output: Contribution to journalArticle

@article{c58be7c59f654735b521db51f33673c7,
title = "O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y",
abstract = "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.",
keywords = "NF-Y, O-GlcNAc, Sp1, Transcription with NF-Y",
author = "Kihong Lim and Hyo-Ihl Chang",
year = "2009",
month = "5",
day = "8",
doi = "10.1016/j.bbrc.2009.03.075",
language = "English",
volume = "382",
pages = "593--597",
journal = "The BMJ",
issn = "0730-6512",
publisher = "Kluwer Academic Publishers",
number = "3",

}

TY - JOUR

T1 - O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y

AU - Lim, Kihong

AU - Chang, Hyo-Ihl

PY - 2009/5/8

Y1 - 2009/5/8

N2 - 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.

AB - 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.

KW - NF-Y

KW - O-GlcNAc

KW - Sp1

KW - Transcription with NF-Y

UR - http://www.scopus.com/inward/record.url?scp=64049092248&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=64049092248&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2009.03.075

DO - 10.1016/j.bbrc.2009.03.075

M3 - Article

VL - 382

SP - 593

EP - 597

JO - The BMJ

JF - The BMJ

SN - 0730-6512

IS - 3

ER -