What question did this study set out to answer?

Identify novel human regulatory proteins that interact with the aryl hydrocarbon receptor (AHR) in a ligand-dependent manner.

April 1, 1997Journal of Biological ChemistryOpen Access

Ligand-dependent Interaction of the Aryl Hydrocarbon Receptor with a Novel Immunophilin Homolog in Vivo

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Identify novel human regulatory proteins that interact with the aryl hydrocarbon receptor (AHR) in a ligand-dependent manner.
Screened 1.4 x 10^6 clones from a human B cell library using a yeast two-hybrid system to detect proteins binding to liganded AHR.
Conducted in vitro reticulocyte lysate assays and co-immunoprecipitation experiments with antisera targeting AHR and the 90-kDa heat shock protein.
Identified ARA9, a novel 330-amino acid protein homologous to the 52-kDa FK506-binding protein, which binds specifically to liganded AHR.
Observed an 11-fold increase in ARA9-AHR interaction in the presence of the ligand beta-naphthoflavone in yeast two-hybrid assays.
Demonstrated that ARA9 co-immunoprecipitates with both AHR and the 90-kDa heat shock protein, confirming high-affinity association in vitro.

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Implication

In vitro study uncovers ligand-dependent binding of novel immunophilin ARA9 to the aryl hydrocarbon receptor, indicating its role in receptor signaling.

Cite This Study

Carver et al. (1997) studied this question.

synapsesocial.com/papers/69d8f2841ab91f1400beda99 https://doi.org/10.1074/jbc.272.17.11452

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Implication

In vitro study uncovers ligand-dependent binding of novel immunophilin ARA9 to the aryl hydrocarbon receptor, indicating its role in receptor signaling.

Ligand-dependent Interaction of the Aryl Hydrocarbon Receptor with a Novel Immunophilin Homolog in Vivo

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Discussion

Implication

Cite This Study

Ligand-dependent Interaction of the Aryl Hydrocarbon Receptor with a Novel Immunophilin Homolog in Vivo

Key Points

Discussion

Implication

Cite This Study

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