Characterization of the differential coregulator binding signatures of the Retinoic Acid Receptor subtypes upon (ant)agonist action

Biochim Biophys Acta Proteins Proteom. 2017 Sep;1865(9):1195-1206. doi: 10.1016/j.bbapap.2017.06.011. Epub 2017 Jun 20.

Abstract

Retinoic Acid Receptor alpha (RARα/NR1B1), Retinoic Acid Receptor beta (RARβ/NR1B2) and Retinoic Acid Receptor gamma (RARγ/NR1B3) are transcription factors regulating gene expression in response to retinoids. Within the RAR genomic pathways, binding of RARs to coregulators is a key intermediate regulatory phase. However, ligand-dependent interactions between the wide variety of coregulators that may be present in a cell and the different RAR subtypes are largely unknown. The aim of this study is to characterize the coregulator binding profiles of RARs in the presence of the pan-agonist all-trans-Retinoic Acid (AtRA); the subtype-selective agonists Am80 (RARα), CD2314 (RARβ) and BMS961 (RARγ); and the antagonist Ro415253. To this end, we used a microarray assay for coregulator-nuclear receptor interactions to assess RAR binding to 154 motifs belonging to >60 coregulators. The results revealed a high number of ligand-dependent RAR-coregulator interactions among all RAR variants, including many binding events not yet described in literature. Next, this work confirmed a greater ligand-independent activity of RARβ compared to the other RAR subtypes based on both higher basal and lower ligand-driven coregulator binding. Further, several coregulator motifs showed selective binding to a specific RAR subtype. Next, this work showed that subtype-selective agonists can be successfully discriminated by using coregulator binding assays. Finally this study demonstrated the possible applications of a coregulator binding assay as a tool to discriminate between agonistic/antagonistic actions of ligands. The RAR-coregulator interactions found will be of use to direct further studies to better understand the mechanisms driving the eventual actions of retinoids.

Keywords: Agonist; Antagonist; Coregulator; Ligand binding domain (LBD); RAR; Subtype.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Anthracenes / pharmacology
  • Benzoates / pharmacology
  • Binding Sites
  • Chromans
  • Protein Array Analysis
  • Protein Binding
  • Protein Domains
  • Receptors, Retinoic Acid / agonists
  • Receptors, Retinoic Acid / antagonists & inhibitors
  • Receptors, Retinoic Acid / chemistry*
  • Recombinant Proteins / metabolism
  • Response Elements
  • Retinoic Acid Receptor alpha / agonists
  • Retinoic Acid Receptor alpha / antagonists & inhibitors
  • Retinoic Acid Receptor alpha / chemistry*
  • Retinoic Acid Receptor gamma
  • Retinoids / pharmacology
  • Structure-Activity Relationship
  • Tetrahydronaphthalenes / pharmacology
  • Thiophenes / pharmacology
  • Tretinoin / pharmacology

Substances

  • Anthracenes
  • BMS 961
  • Benzoates
  • CD2314
  • Chromans
  • Receptors, Retinoic Acid
  • Recombinant Proteins
  • Retinoic Acid Receptor alpha
  • Retinoids
  • Tetrahydronaphthalenes
  • Thiophenes
  • retinoic acid receptor beta
  • tamibarotene
  • Ro 41-5253
  • Tretinoin