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Updated: Aug 9, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
Published on: December 19, 2018
Activation function 1 domain plays a negative role in dimerization of estrogen receptor beta
Daniel Detka1, Katarzyna Kalita, Leszek Kaczmarek
1Laboratory of Molecular Neurobiology, Nencki Institute of Experimental Biology, Pasteura 3, Warsaw 02-093, Poland.
Abstract:
Transcriptional potential of estrogen receptor beta (ERbeta) depends on the ligand binding and subsequent dimerization of the receptor protein. In order to examine the role of N-terminally located activation function 1 (AF-1) protein domain in the dimerization process of ERbeta, we used yeast SOS-Recruitment System (SRS). Two variants of ERbeta protein were expressed in the yeast cells: full length receptor and a truncated form, lacking AF-1. We observed that upon 17beta-estradiol treatment only the shorter form of the receptor dimerized, whereas the full-length one did not. This result suggests an inhibitory function of AF-1 in dimer formation and supports previous studies showing that N-terminal domain of ERbeta suppresses transcriptional activity.
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