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Updated: Aug 12, 2026

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists
Published on: November 15, 2013
The novel co-activator CRABPII binds to RARalpha and RXRalpha via two nuclear receptor interacting domains and does
J N Bastie1, G Despouy, N Balitrand
1Laboratoire de Biologie Cellulaire Hématopoïétique, Hôpital Saint-Louis, Paris, France.
Abstract:
We identify the RARalpha, RXRalpha and CRABPII domains required for the physical interaction of these proteins. On RARalpha and RXRalpha, the sequences correspond to the DEF and DE domains, respectively, but the interaction with CRABPII does not require the AF-2AD 'core'. On CRABPII, two interacting domains are identified (NRID1 and NRID2), one of which contains the only enhancement transactivation domain of CRABPII. The interaction is ligand-independent and does not require the ligand-binding domain of CRABPII. These results further stress that interaction of CRABPII with the nuclear receptors defines a novel level of transcriptional control.
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