| The AhR , AhR nuclear translocator ( Arnt ) , and AhR / Arnt proteins were coimmunoprecipitated with 35S ERAP 140 and 35S SMRT and , in gel mobility shift assays , AhR / Arnt binding to 32P dioxin response element ( DRE ) was enhanced by ERAP 140 and inhibited by SMRT ; supershifted bands were not observed . ^^^ These results confirmed functional and physical interactions of AhR / Arnt with ERAP 140 and SMRT in breast cancer cells . . ^^^ |