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Updated: Jan 25, 2026

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding
Published on: September 21, 2011
Reconstitution of the Steroid Receptor Heterocomplex
Gisela I Mazaira1, Mario D Galigniana2,3
1Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina.
Abstract:
Steroid receptors are members of a subfamily of the nuclear receptor superfamily. They play a dual role of steroid hormone receptors and transcription factors. Actually, these receptors are steroid-activated transcription factors. Classical soluble receptors exist as oligomeric complexes with the Hsp90-based chaperone machinery. The steroid receptor field was born and developed along with the molecular chaperone field. Chaperones are not exclusive partners associated to these receptors, but also comprise a large variety of heterocomplexes with other proteins involved in signal transduction. By using the glucocorticoid receptor (GR) as a standard model for most Hsp90-client proteins, in this chapter we describe the functional GR·Hsp90 heterocomplex assembly system from reticulocyte lysate or purified proteins.
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