Corticosteroid receptors as a model for the Hsp90•immunophilin-based transport machinery

MAZAIRA, GISELA I.; PIWIEN PILIPUK, GRACIELA; GALIGNIANA, MARIO D.

TRENDS IN ENDOCRINOLOGY AND METABOLISM

ELSEVIER SCIENCE LONDON

Año: 2021 vol. 32 p. 827 - 838

1043-2760

Steroid receptors form soluble heterocomplexes with the 90-kDa heat-shock protein (Hsp90) and other chaperones and co-chaperones. The assembly and composition of the oligomer is influenced by the presence and nature of the bound steroid. Although these receptors shuttle dynamically in and out of the nucleus, their primary localization in the absence of steroid can be mainly cytoplasmic, mainly nuclear, or partitioned into both cellular compartments. Upon steroid binding, receptors become localized to the nucleus via the transportosome, a retrotransport molecular machinery that comprises Hsp90, a high-molecular-weight immunophilin, and dynein motors. This molecular machinery, first evidenced in steroid receptors, can also be used by other soluble proteins. In this review, we dissect the complete model of this transport machinery system.