An involvement of molecular chaperones in the action and well-being of steroid receptors was recognized early in the "molecular" era of hormone research. However, this has continued to be a topic of much enquiry and some confusion. All steroid receptors associate with Hsp90, the main character of a series of multi-protein chaperone complexes generally referred to as the "Hsp90 chaperoning machine". Receptor association with chaperones occurs in an ordered, step-wise fashion and is necessary for the maintenance of unliganded receptor in a state ready to bind and respond to hormone. Chaperones additionally modulate how receptors respond to hormone and activate target genes. While much is known about the participants in this chaperoning process and the consequences of chaperoning, many key questions remain unanswered, particularly those concerning molecular mechanisms, cellular dynamics, and the functions of an array of co-chaperone proteins. Here, we point out several areas in need of investigation to encourage new ideas and participants in this burgeoning field.