福克斯O1
乙酰化
辅活化剂
P300-CBP转录因子
交易激励
生物
乙酰转移酶
转录因子
PCAF公司
磷酸化
组蛋白乙酰转移酶
叉头转录因子
组蛋白
HDAC4型
转录调控
福克斯A2
HDAC8型
CREB结合蛋白
基因表达调控
细胞生物学
抄写(语言学)
分子生物学
转染
癌症研究
调节器
翻译后调节
基因表达
SAP30型
DNA结合蛋白
激酶
作者
Valérie Perrot,Matthew M. Rechler
摘要
The FOXO (Forkhead box class O) subgroup of forkhead transcription factors controls the expression of many genes involved in fundamental cellular processes. Until recently, studies conducted on posttranslational modifications of Forkhead proteins were restricted to their phosphorylation. In this report, we show that the coactivator p300 directly acetylates lysines in the carboxyl-terminal region of Foxo1 in vivo and in vitro, and potently stimulates Foxo1-induced transcription of IGF-binding protein-1 in transient transfection experiments. The intrinsic acetyltransferase activity of p300 is required for both activities. Our results suggest that acetylation of Foxo1 by p300 is responsible, at least in part, for its increased transactivation potency, although acetylation of histones cannot be excluded. Insulin, the major negative regulator of Foxo1-stimulated transcription, potently enhances p300 acetylation of Foxo1. Three consensus protein kinase B/Akt phosphorylation sites whose phosphorylation is stimulated by insulin are required for insulin-induced acetylation of Foxo1. In contrast to its importance in regulating the transcriptional activity of Foxo1 in the absence of insulin, acetylation plays only a minor role compared with phosphorylation in insulin inhibition of Foxo1 transcriptional activity.
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