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Molecular Endocrinology 11 (10): 1486-1496
Copyright © 1997 by The Endocrine Society

Mouse Estrogen Receptor ß Forms Estrogen Response Element-Binding Heterodimers with Estrogen Receptor {alpha}

Katarina Pettersson, Kaj Grandien, George G. J. M. Kuiper and Jan-Åke Gustafsson

Department of Medical Nutrition and Center for Biotechnology, Karolinska Institute, S-14186 Huddinge, Sweden

The recent discovery that an additional estrogen receptor subtype is present in various rat tissues has advanced our understanding of the mechanisms underlying estrogen signaling. Here we report on the cloning of the cDNA encoding the mouse homolog of estrogen receptor-ß (ERß) and the functional characterization of mouse ERß protein. ERß is shown to have overlapping DNA-binding specificity with that of the estrogen receptor-{alpha} (ER{alpha}) and activates transcription of reporter gene constructs containing estrogen-response elements in transient transfections in response to estradiol. Using a mammalian two-hybrid system, the formation of heterodimers of the ERß and ER{alpha} subtypes was demonstrated. Furthermore, ERß and ER{alpha} form heterodimeric complexes with retained DNA-binding ability and specificity in vitro. In addition, DNA binding by the ERß/ER{alpha} heterodimer appears to be dependent on both subtype proteins. Taken together these results suggest the existence of two previously unrecognized pathways of estrogen signaling; I, via ERß in cells exclusively expressing this subtype, and II, via the formation of heterodimers in cells expressing both receptor subtypes.




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