Acetylation regulates transcription factor activity at multiple levels

被引：246

作者：

Soutoglou, E ^{[1
]}

Katrakili, N ^{[1
]}

Talianidis, I ^{[1
]}

机构：

[1] Fdn Res & Technol Hellas, Inst Mol Biol & Biotechnol, Heraklion 71110, Greece

来源：

MOLECULAR CELL | 2000年 / 5卷 / 04期

关键词：

D O I：

10.1016/S1097-2765(00)80253-1

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：

CREB-binding protein (CBP) possesses an intrinsic acetyltransferase activity capable of acetylating nucleosomal histones as well as several nonhistone proteins. Here, it is shown that CBP can acetylate hepatocyte nuclear factor-4 (HNF-4), a member of the nuclear hormone receptor family, at lysine residues within the nuclear localization sequence. CBP-mediated acetylation is crucial for the proper nuclear retention of HNF-4, which is otherwise transported out to the cytoplasm via the CRM1 pathway. Acetylation also increases HNF-4 DNA binding activity and its affinity of interaction with CBP itself and is required for target gene activation. The results show that acetylation is a key posttranslational modification that may affect several properties of a transcription factor critical for the execution of its biological functions.

引用

页码：745 / 751

页数：7

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