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Cited by 864

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Cloning, Chromosomal Localization, and Functional Analysis of the Murine Estrogen Receptor β

Tremblay, Gilles B., Tremblay, André, Copeland, Neal G., Gilbert, Debra J., Jenkins, Nancy A., Labrie, Fernand, Giguère, Vincent·1997·Molecular Endocrinology
DOI 10.1210/mend.11.3.9902
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Abstract

Estrogen receptor β (ERβ) is a novel steroid receptor that is expressed in rat prostate and ovary. We have cloned the mouse homolog of ERβ and mapped the gene, designated Estrb, to the central region of chromosome 12. The cDNA encodes a protein of 485 amino acids that shares, respectively, 97% and 60% identity with the DNA- and ligand-binding domains of mouse (m) ERα. Mouse ERβ binds to an inverted repeat spaced by three nucleotides in a gel mobility shift assay and transactivates promoters containing synthetic or natural estrogen response elements in an estradiol (E2)-dependent manner. Scatchard analysis indicates that mERβ has slightly lower affinity for E2 [dissociation constant (Kd) = 0.5 nm] when compared with mERα (Kd = 0.2 nm). Antiestrogens, including 4-hydroxytamoxifen (OHT), ICI 182,780, and a novel compound, EM-800, inhibit E2-dependent transactivation efficiently. However, while OHT displays partial agonistic activity with ERα on a basal promoter linked to estrogen response elements in Cos-1 cells, this effect is not observed with mERβ. Cotransfection of mERβ and H-RasV12 causes enhanced activation in the presence of E2. Mutagenesis of a serine residue (position 60), located within a mitogen-activated protein kinase consensus phosphorylation site abolishes the stimulatory effect of Ras, suggesting that the activity of mERβ is also regulated by the mitogen-activated protein kinase pathway. Surprisingly, the coactivator SRC-1 up-regulates mERβ transactivation both in the absence and presence of E2, and in vitro interaction between SRC-1 and the ERβ ligand-binding domain is enhanced by E2. Moreover, the ligand-independent stimulatory effect of SRC-1 on ERβ transcriptional activity is abolished by ICI 182,780, but not by OHT. Our results demonstrate that while ERβ shares many of the functional characteristics of ERα, the molecular mechanisms regulating the transcriptional activity of mERβ may be distinct from those of ERα.

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Metadata

Authors
Tremblay, G. B., Tremblay, A., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., Labrie, F., & Giguère, V.
Venue
Molecular Endocrinology
Publisher
The Endocrine Society
Published
1997-03-01
Volume
11
Issue
3
Pages
353-365
ISSN
  • 0888-8809 (ISSN-L)
  • 1944-9917
DOI
10.1210/mend.11.3.9902
OpenAlex
W2135723391
Cited by
864
References
3
FWCI
46.54
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Cloning, Chromosomal Localization, and Functional Analysis of the Murine Estrogen Receptor β. https://app.cochat.ai/papers/10.1210/mend.11.3.9902
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Tremblay, G. B., Tremblay, A., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., Labrie, F., & Giguère, V. (1997). Cloning, Chromosomal Localization, and Functional Analysis of the Murine Estrogen Receptor β. Molecular Endocrinology. https://doi.org/10.1210/mend.11.3.9902

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