Steroid hormone receptor (SHR) (SHR)

Steroid hormone receptors (SHRs) are a class of ligand-activated transcription factors that belong to the nuclear receptor superfamily (Evans, 1988, Science). These receptors, including the estrogen, androgen, progesterone, glucocorticoid, and mineralocorticoid receptors, exist in the cytoplasm or nucleus as part of a multi-protein steroid receptor complex with chaperone proteins like Hsp90 and Hsp70 (Pratt & Toft, 1997, Endocrine Reviews). Upon binding to their specific steroid ligands, the receptors undergo a conformational change that triggers the dissociation of chaperones, followed by receptor dimerization and translocation into the nucleus (Kumar & Thompson, 1999, Endocrine Reviews). The activated dimer then binds to specific DNA sequences known as hormone response elements (HREs) to recruit co-activators or co-repressors, thereby regulating the transcription of target genes involved in development, metabolism, and homeostasis (Beato et al., 1995, Cell). Dysregulation of these receptors is a hallmark of several diseases, most notably hormone-dependent cancers such as breast and prostate cancer, as well as various inflammatory and endocrine disorders (Mangelsdorf et al., 1995, Cell). Consequently, they are among the most successful therapeutic targets in pharmacology, with drugs acting as agonists, antagonists, or selective modulators to treat conditions ranging from inflammation to malignancy (Burris et al., 2013, Nature Reviews Drug Discovery).

Other names

Steroid receptor complexNuclear steroid receptorSteroid hormone receptor superfamilySteroid receptor

Steroid hormone receptors function as ligand-activated transcription factors; upon ligand binding, the receptor-chaperone complex dissociates, and the receptor undergoes dimerization and nuclear translocation to bind hormone response elements (HREs) and modulate gene transcription.