Volume 57, Issue 4, Pages 1241-1249 (April 2000) Role of molecular chaperones in subnuclear trafficking of glucocorticoid receptors  Dr Donald B. DeFranco  Kidney International  Volume 57, Issue 4, Pages 1241-1249 (April 2000) DOI: 10.1046/j.1523-1755.2000.00957.x Copyright © 2000 International Society of Nephrology Terms and Conditions

Figure 1 Subnuclear trafficking of glucocorticoid receptor (GR). GR that is bound to hormone (H) associates with high-affinity binding sites on chromatin or with the nuclear matrix. Chromatin and the nuclear matrix are depicted as separate and distinct compartments for simplicity alone and may, in fact, be physically linked. Although it is unclear whether hormone must dissociate from receptors for their release from the nuclear matrix, adenosine 5′-triphosphate (ATP) is required for receptor release from, but not binding to, the nuclear matrix. The chaperone activity of heat shock protein 90 (hsp90) may facilitate the release of unliganded receptor from chromatin. At least three alternative processing fates are available for unliganded GR: degradation, nuclear export, and recycling. It appears that unliganded GRs are fully competent to rebind hormone and therefore likely to be assembled into a heteromeric complex. Kidney International 2000 57, 1241-1249DOI: (10.1046/j.1523-1755.2000.00957.x) Copyright © 2000 International Society of Nephrology Terms and Conditions