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

被引：21

作者：

Lim, Kihong ^{[1
]}

Chang, Hyo-Ihl ^{[1
]}

机构：

[1] Korea Univ, Sch Life Sci & Biotechnol, Seoul 136701, South Korea

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2009年 / 382卷 / 03期

关键词：

NF-Y; Sp1; O-GlcNAc; Transcription with NF-Y; TRANSCRIPTION FACTORS; GENE-TRANSCRIPTION; ACTIVATION; ACETYLGLUCOSAMINE; PHOSPHORYLATION; GLYCOSYLATION; PROMOTER; BINDING; PROTEASOME; EXPRESSION;

D O I：

10.1016/j.bbrc.2009.03.075

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：593 / 597

页数：5

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