热休克蛋白90
细胞生物学
信号
热休克蛋白
生物
背景(考古学)
受体
计算生物学
化学
基因
遗传学
古生物学
作者
Mariana Lagadari,Sonia A. De Leo,María Fernanda Camisay,Mario D. Galigniana,Alejandra G. Erlejman
出处
期刊:Current Molecular Pharmacology
[Bentham Science]
日期:2015-12-07
卷期号:9 (2): 99-108
被引量:18
标识
DOI:10.2174/1874467208666150519113833
摘要
The fine regulation of signalling cascades is a key event required to maintain the appropriate functional properties of a cell when a given stimulus triggers specific biological responses. In this sense, cumulative experimental evidence during the last years has shown that high molecular weight immunophilins possess a fundamental importance in the regulation of many of these processes. It was first discovered that TPR-domain immunophilins such as FKBP51 and FKBP52 play a cardinal role, usually in an antagonistic fashion, in the regulation of several members of the steroid receptor family via its interaction with the heat-shock protein of 90-kDa, Hsp90. These Hsp90-associated cochaperones form a functional unit with the molecular chaperone influencing ligand binding capacity, receptor trafficking, and hormone-dependent transcriptional activity. Recently, it was demonstrated that the same immunophilins are also able to regulate the NF-kB signalling cascade in an Hsp90 independent manner. In this article we analize these properties and discuss the relevance of this novel regulatory pathway in the context of the pleiotropic actions managed by NF-kB in several cell types and tissues.
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