Open AccessSteroid receptor heterodimerization demonstrated in vitro and in vivo.
Author(s) -
Weihong Liu,
Jian Wang,
Nicholas K. Sauter,
David Pearce
Publication year - 1995
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.92.26.12480
Subject(s) - glucocorticoid receptor , nuclear receptor , receptor , microbiology and biotechnology , mineralocorticoid receptor , biology , in vitro , pelp 1 , transcription factor , in vivo , steroid hormone , mineralocorticoid , transcription (linguistics) , intracellular , genetics , gene , linguistics , philosophy
The mineralocorticoid and glucocorticoid receptors (MR and GR, respectively) are members of the intracellular receptor superfamily that bind as homodimers to the same hormone response elements (HREs). Physiological evidence suggests that MR and GR interact with each other in cells that express both receptors, implying that they might directly interact in the regulation of transcription initiation. Indeed, we have found that coexpressed MR and GR interact functionally at the transcriptional level and furthermore that they interact physically through heterodimer formation at a shared HRE in vitro and in vivo. We suggest from these findings that heterodimerization may play an important role in steroid receptor transcriptional regulation.