Human mineralocorticoid receptor interacts with actin under mineralocorticoid ligand modulation.
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.
Jalaguier
S
S
Institut National de la Santé et de la Recherche Médicale, Unité 300, Faculté de Pharmacie, Montpellier, France.
Mornet
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D
Mesnier
D
D
Léger
J J
JJ
Auzou
G
G
D000199:Actins / Q000378:metabolism*; D000450:Aldosterone / Q000378:metabolism; D001665:Binding Sites; D006360:Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D008024:Ligands; D008901:Mineralocorticoids / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D011374:Progesterone / Q000378:metabolism; D011485:Protein Binding; D018161:Receptors, Mineralocorticoid / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D000199:Actins; D006360:Heat-Shock Proteins; D008024:Ligands; D008901:Mineralocorticoids; D010446:Peptide Fragments; D018161:Receptors, Mineralocorticoid; D011993:Recombinant Fusion Proteins; D000450:Aldosterone; D011374:Progesterone