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    FEBS Lett. 1996 Apr 15;384(2):112-6.

    Human mineralocorticoid receptor interacts with actin under mineralocorticoid ligand modulation.

    Jalaguier S, Mornet D, Mesnier D, Léger JJ, Auzou G.

    Institut National de la Santé et de la Recherche Médicale, Unité 300, Faculté de Pharmacie, Montpellier, France.

    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 (Kd about 2 microM) 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.

    PMID: 8612804 [PubMed - indexed for MEDLINE]

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