Detection of glucocorticoid-receptor complex oligomers in nuclear extracts from cells exposed to hormone at physiological temperature

Receptor density dictates the behavior of a subset of steroid ligands in glucocorticoid receptor-mediated transrepression

“…Although GR molecules defective for DNA binding and dimerization are shown to be sufficient for transrepression [25,30], it remains a testable possibility that dimeric or oligomeric GR molecules, following agonist binding, are more effective transrepressors. In addition, dimerization or oligomerization of GR has been suggested to play a role in regulating GR function [31,32]. It is conceivable that low GR density may not allow RU486-bound GR to efficiently dimerize or oligomerize.…”