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Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins

A B Hittelman1, D Burakov, J A Iñiguez-Lluhí

  • 1Department of Microbiology and the Kaplan Comprehensive Cancer Center, NYU School of Medicine, 550 First Avenue, New York, NY 10016, USA.

The EMBO Journal
|October 3, 1999
PubMed

Insights

Glucocorticoid receptor (GR) transcriptional regulation involves interactions with TSG101 and DRIP150 proteins. These factors, including DRIP205, modulate GR

Area of Science:

  • Molecular Biology
  • Endocrinology
  • Gene Regulation

Background:

  • The glucocorticoid receptor (GR) is a key regulator of gene transcription.
  • GR's transcriptional activity is mediated by its N-terminal (AF-1) and C-terminal (AF-2) activation functions.
  • Understanding GR's interactions with regulatory factors is crucial for deciphering its function.

Purpose of the Study:

  • To identify proteins interacting with the GR AF-1 activation function.
  • To elucidate the roles of identified interacting proteins in GR-mediated transactivation.
  • To investigate the functional linkage between GR's AF-1 and AF-2 domains.

Main Methods:

  • Modified yeast two-hybrid screening to identify GR AF-1 interacting proteins.
  • Co-transfection assays in yeast and mammalian cells to assess transactivation.
  • Hormone-dependent interaction assays for DRIP205 and GR ligand binding domain.

Main Results:

  • TSG101 and DRIP150 were identified as specific interactors of the GR AF-1 surface.
  • TSG101 demonstrated repression, while DRIP150 showed enhancement of GR AF-1 activity.
  • DRIP205 interacted with the GR ligand binding domain and, with DRIP150, facilitated GR transactivation.

Conclusions:

  • GR AF-1 can recruit both positive (DRIP150) and negative (TSG101) regulatory factors.
  • DRIP150 and DRIP205 link the GR AF-1 and AF-2 activation functions.
  • These DRIP complex members are critical mediators of glucocorticoid receptor transcriptional enhancement.

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