ArticleMolecular and cellular biology1999
Dominant activity of activation function 1 (AF-1) and differential stoichiometric requirements for AF-1 and -2 in the estrogen receptor alpha-beta heterodimeric complex.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 137 citations in OpenAlex.
- SIRT1 mediates breast cancer development and tumorigenesis controlled by estrogen-related receptor β.Breast cancer (Tokyo, Japan) · 2024Article
- Estrogen Receptor Alpha Mutations, Truncations, Heterodimers, and Therapies.Endocrinology · 2024Review
- Estrogen receptor α dependent regulation of estrogen related receptor β and its role in cell cycle in breast cancer.BMC cancer · 2018Article
- Monitoring ligand-dependent assembly of receptor ternary complexes in live cells by BRETFect.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A Computational-Based Approach to Identify Estrogen ReceptorMolecular pharmacology · 2018Article
- Structural and functional characteristics of oestrogen receptor β splice variants: Implications for the ageing brain.Journal of neuroendocrinology · 2018Review
- Molecular mechanism of estrogen-estrogen receptor signaling.Reproductive medicine and biology · 2017Review
- Tyrosine phosphorylation regulates ERβ ubiquitination, protein turnover, and inhibition of breast cancer.Oncotarget · 2016Article
- Mechanisms of uterine estrogen signaling during early pregnancy in mice: an update.Journal of molecular endocrinology · 2016Review
- IGF-1 gene expression is differentially regulated by estrogen receptors α and β in mouse endometrial stromal cells and ovarian granulosa cells.The Journal of reproduction and development · 2014Article
- Cooperative activation of gene expression by agonists and antagonists mediated by estrogen receptor heteroligand dimer complexes.Molecular pharmacology · 2013Article
- Characterisation of human oestrogen receptor beta (ERβ) splice variants in neuronal cells.Journal of neuroendocrinology · 2012Article
- Identification of estrogen receptor β as a SUMO-1 target reveals a novel phosphorylated sumoylation motif and regulation by glycogen synthase kinase 3β.Molecular and cellular biology · 2012Article
- Identification of estrogen receptor dimer selective ligands reveals growth-inhibitory effects on cells that co-express ERα and ERβ.PloS one · 2012Article
- Novel approaches to quantify estradiol-induced loss of ERβ1 protein in older mouse ovarian surface epithelium: new tools to assess the role of ER protein subtypes in predisposing to ovarian epithelial cancer?Hormones & cancer · 2011Article
- Genome-wide dynamics of chromatin binding of estrogen receptors alpha and beta: mutual restriction and competitive site selection.Molecular endocrinology (Baltimore, Md.) · 2010Article
- Evolutionary history and functional characterization of androgen receptor genes in jawed vertebrates.Endocrinology · 2009Article
- Intermolecular interactions identify ligand-selective activity of estrogen receptor alpha/beta dimers.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- What are comparative studies telling us about the mechanism of ERbeta action in the ERE-dependent E2 signaling pathway?The Journal of steroid biochemistry and molecular biology · 2008Article
- Effects of the pesticide methoxychlor on gene expression in the liver and testes of the male largemouth bass (Micropterus salmoides).Aquatic toxicology (Amsterdam, Netherlands) · 2008Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Estrogenic responses are now known to be mediated by two forms of estrogen receptors (ER), ERalpha and ERbeta, that can function as homodimers or heterodimers. As homodimers the two have been recently shown to exhibit distinct transcriptional responses to estradiol (E2), antiestrogens, and coactivators, suggesting that the ER complexes are not functionally equivalent. However, because the three possible configurations of ER complexes all recognize the same estrogen response element, it has not been possible to evaluate the transcriptional properties of the ER heterodimer complex by transfection assays. Using ER subunits with modified DNA recognition specificity, we were able to measure the transcriptional properties of ERalpha-ERbeta heterodimers in transfected cells without interference from the two ER homodimer complexes. We first demonstrated that the individual activation function 1 (AF-1) domains act in a dominant manner within the ERalpha-ERbeta heterodimer: the mixed agonist-antagonist 4-hydroxytamoxifen acts as an agonist in a promoter- and cell context-dependent manner via the ERalpha AF-1, while activation of the complex by the mitogen-activated protein kinase (MAPK) pathway requires only the ERalpha- or ERbeta-responsive MAPK site. Using ligand-binding and AF-2-defective mutants, we further demonstrated that while the ERalpha-ERbeta heterodimer can be activated when only one E2-binding competent partner is present per dimer, two functional AF-2 domains are required for transcriptional activity. Taken together, the results of this study of a retinoid X receptor-independent heterodimer complex, the first such study, provide evidence of different stoichiometric requirements for AF-1 and -2 activity and demonstrate that AF-1 receptor-specific properties are maintained within the ERalpha-ERbeta heterodimer.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.