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Papers In Press, published online ahead of print October 30, 2002
Cell- and Molecular Biology, Karolinska Institutet, Stockholm S-171 77
Corresponding Author: maria.sjoberg{at}karobio.se
Estrogen receptors (ERs) efficiently potentiate the transcriptional activity of prolactin-activated Stat5b through a mechanism that involves the ER DNA-binding domain (DBD) and the hinge domain. We have identified residues within the DBD of ER that are critical for the functional interaction of ER with Stat5b. We show that disruption of the second zinc finger structure abrogates cross-talk between ER and Stat5b, while the structure of the first zinc finger is not important. Furthermore, we confirm that intact DNA-binding activity is not required for potentiation of Stat5b activity, nor seems the dimerisation of ER be involved. Ligand-bound ERs also modulate AP-1-dependent transcription and our data demonstrate that both zinc finger structures of the ER DBD are important for an intact response. We show that introduction of various point mutations within the DBD alters the response of the receptor to 17b-estradiol and to the estrogen antagonists, 4-hydroxytamoxifen and ICI 182,870, on the collagenase promoter. These findings provide new insights into the mechanisms by which ERs act in cross-talk with non-related transcription factors.
J. Biol. Chem, 10.1074/jbc.C200570200
Submitted on October 9, 2002
Revised on October 29, 2002
Accepted on October 30, 2002
Mutations in the estrogen receptor DNA-binding domain discriminate between the classical mechanism of action and cross-talk with Stat5b and AP-1
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