ArticleMolecular and cellular biology1997
AF-2 activity and recruitment of steroid receptor coactivator 1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptors.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 213 citations in OpenAlex.
- Characterization of novel small molecule inhibitors of estrogen receptor-activation function 2 (ER-AF2).Breast cancer research : BCR · 2024Article
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- A novel human glucocorticoid receptor SNP results in increased transactivation potential.Biochemistry and biophysics reports · 2017Article
- Tetrahydro-iso-alpha Acids Antagonize Estrogen Receptor Alpha Activity in MCF-7 Breast Cancer Cells.International journal of endocrinology · 2016Article
- A new class of small molecule estrogen receptor-alpha antagonists that overcome anti-estrogen resistance.Oncotarget · 2015Article
- Ncoa3 functions as an essential Esrrb coactivator to sustain embryonic stem cell self-renewal and reprogramming.Genes & development · 2012Article
- Article
- BRCA1 regulates acetylation and ubiquitination of estrogen receptor-alpha.Molecular endocrinology (Baltimore, Md.) · 2010Article
- Apurinic/apyrimidinic endonuclease 1 alters estrogen receptor activity and estrogen-responsive gene expression.Molecular endocrinology (Baltimore, Md.) · 2009Article
- FOXP3 and the regulation of Treg/Th17 differentiation.Microbes and infection · 2009Review
- A novel mechanism whereby BRCA1/1a/1b fine tunes the dynamic complex interplay between SUMO-dependent/independent activities of Ubc9 on E2-induced ERalpha activation/repression and degradation in breast cancer cells.International journal of oncology · 2009Article
- The nuclear receptor transcriptional coregulator RIP140.Nuclear receptor signaling · 2006Article
- Article
- The repressor DREAM acts as a transcriptional activator on Vitamin D and retinoic acid response elements.Nucleic acids research · 2005Article
- A permissive retinoid X receptor/thyroid hormone receptor heterodimer allows stimulation of prolactin gene transcription by thyroid hormone and 9-cis-retinoic acid.Molecular and cellular biology · 2004Article
- Electrostatic modulation in steroid receptor recruitment of LXXLL and FXXLF motifs.Molecular and cellular biology · 2003Article
- MAP kinase/estrogen receptor cross-talk enhances estrogen-mediated signaling and tumor growth but does not confer tamoxifen resistance.Oncogene · 2002Article
- The PHD type zinc finger is an integral part of the CBP acetyltransferase domain.Molecular and cellular biology · 2002Article
- Mutant BRCA1 genes antagonize phenotype of wild-type BRCA1.Oncogene · 2001Article
- Ligand-mediated assembly and real-time cellular dynamics of estrogen receptor alpha-coactivator complexes in living cells.Molecular and cellular biology · 2001Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hormone-dependent transcriptional activation by nuclear receptors depends on the presence of a conserved C-terminal amphipathic alpha-helix (helix 12) in the ligand-binding domain. Here we show that a lysine residue, which is conserved in most nuclear receptors in the predicted helix 3, is also required for estrogen-dependent transactivation. The replacement of lysine 366 with alanine appreciably reduced activation function 2 (AF-2) activity without affecting steroid- or DNA-binding activity in the mouse estrogen receptor. The mutation dramatically reduced the ability of the receptor to bind steroid receptor coactivator 1 (SRC-1) but had no effect on receptor-interacting protein 140 (RIP-140) binding, indicating that while their sites of interaction overlap, they are not entirely consistent and in keeping with the proposal that the recruitment of coactivators, such as SRC-1, is required for AF-2 activity. Although the function of RIP-140 remains to be established, RIP-140 appears to be capable of recruiting the basal transcription machinery, since overexpression of the protein markedly increased the transcriptional activity of the mutant receptor. Since the lysine residue is conserved, we propose that it is required, together with residues in helix 12, to form the surface by which members of the nuclear receptor family interact with coactivators.
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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.