30 YEARS OF THE MINERALOCORTICOID RECEPTOR: Coregulators as mediators of mineralocorticoid receptor signalling diversity

  1. Morag J Young
  1. Centre for Endocrinology and Metabolism, Hudson Institute of Medical Research and the Monash University Department of Molecular Translational Science, Clayton, Victoria, Australia
  1. Correspondence should be addressed to P J Fuller; Email: peter.fuller{at}hudson.org.au
  1. Figure 1

    Schematic representation of the human mineralocorticoid receptor (MR) structure. The MR, as with other nuclear receptors, can be divided into three principle domains: the N-terminal domain (NTD), the DNA-binding domain (DBD) and the ligand-binding domain (LBD). The DBD 11and LBD are joined by a relatively poorly conserved hinge region. Activation Functions (AFs): 1a, 1b and 2 are indicated as is the putative repressive function termed the middle domain (MD). The amino acid numbers are above the schematic with NH2 and COOH representing the N- and C-termini of the molecule, respectively.

  2. Figure 2

    Schematic representation of mineralocorticoid receptor (MR)-mediated transactivation. Ligand binding to the MR leads to a conformational change that permits nuclear transfer. Within the nucleus, MR monomers dimerize at the hormone response element (HRE). Coactivators, such as the steroid receptor coactivators (SRC) and p300/CREB-binding protein (CBP), are then recruited, and they interact with the basal transcriptional apparatus to promote expression of the target gene.

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