Human mineralocorticoid receptor interacts with actin under mineralocorticoid ligand modulation

FEBS Letters

Mornet, Dominique¹  Jalaguier, Stéphan¹  Mesnier, Danielle¹  Auzou, Gilles¹  Léger, Jean J.¹ 

[1] Institut National de la Santé et de la Recherche Médicale, Unité 300, Faculté de Pharmacie, 15 Avenue Charles Flahault, 34060 Montpellier, France

关键词: Mineralocorticoid receptor;    Hormone binding domain;    Actin;    Hsp;    Aldosterone;    Progesterone;    MR;    mineralocorticoid receptor;    hMR;    human mineralocorticoid receptor;    HBD;    hormone binding domain;    MBP;    maltose binding protein;    hsp;    heat shock protein;    GR;    glucocorticoid receptor;   

DOI  :  10.1016/0014-5793(96)00295-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The human mineralocorticoid receptor of the steroid receptor family contains a modular structure with domain E which is considered to be a hormone binding domain. Recombinant protein approaches enabled us to clearly determine that this domain is also able to interact with F-actin (K _d about 2 μM) and G-actin. Moreover, it was revealed that this mineralocorticoid receptor domain/actin interaction was modulated by specific mineralocorticoid ligands. Agonist (aldosterone) steroid binding almost totally (91%) abolished the interaction with F-actin, while antagonist (progesterone) binding allowed more than 30% of this binding. Steroid modulation of the interaction between domain E and actin indicated that this actin binding is specific and could be essential for cellular mineralocorticoid receptor activity.

【 授权许可】

Unknown