Human mineralocorticoid receptor interacts with actin under mineralocorticoid ligand modulation

FEBS Letters
S JalaguierG Auzou

Abstract

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.

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Citations

Oct 1, 2004·The Journal of Membrane Biology·H Oberleithner
May 12, 2004·Molecular and Cellular Endocrinology·Melyssa R BrattonJose S Subauste
Feb 9, 2000·Pharmacology & Therapeutics·M K Agarwal, M Mirshahi
Jan 5, 2008·Nuclear Receptor Signaling·Say ViengchareunMarc Lombès
Sep 24, 2010·American Journal of Physiology. Renal Physiology·Nourdine FaresseOlivier Staub
May 13, 2008·American Journal of Physiology. Heart and Circulatory Physiology·Miriam WeberRalf Lösel

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