Regulation of FoxO activity by CBP/p300-mediated acetylation

被引：148

作者：

van der Heide, LP ^{[1
]}

Smidt, MP ^{[1
]}

机构：

[1] Univ Utrecht, Med Ctr, Rudolf Magnus Inst Neurosci, NL-3584 CG Utrecht, Netherlands

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2005年 / 30卷 / 02期

关键词：

D O I：

10.1016/j.tibs.2004.12.002

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：

Forkhead box, class O (FoxO) transcription factors are inhibited by insulin-induced FoxO phosphorylation. Recently, acetylation of FoxO factors by calcium response element-binding (CREB)-binding protein (CBP) and/or p300 has been identified as a novel regulatory pathway, although the exact consequences of acetylation remain unclear. We propose that binding of CBP/p300 to FoxO factors is essential for FoxO-mediated transcription. CBP and p300 act as FoxO cofactors by weakening histone-DNA interactions. Acetylation of FoxO factors, however, attenuates FoxO-mediated transcriptional activity by disrupting the interaction between FoxO factors and target DNA. Therefore, acetylation shifts the function of FoxO from cell-cycle arrest and protection against oxidative stress towards cell death.

引用

页码：81 / 86

页数：6

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