Chaperoning steroid hormone action

Abstract

Those that efface themselves in the action tend to be forgotten. But molecular chaperones are always there, often serving as equal partners. Because of their intrinsic functional frailty, a large number of signaling molecules have come to depend on molecular chaperones, notably the Hsp90 chaperone machine. This applies to the subset of nuclear receptors that converts steroid hormone signals to transcriptional outputs. Steroid receptors appear to rely on the Hsp90 machine for folding, regulation of the allosteric switch and recycling. This review discusses the complexities of the chaperone machinery and the diversity of regulatory options afforded by this assistance for hormone action.