ArticleMolecular endocrinology (Baltimore, Md.)2008
Control of estradiol-directed gene transactivation by an intracellular estrogen-binding protein and an estrogen response element-binding protein.
Article in Molecular endocrinology (Baltimore, Md.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- DOCTER: a genetically encoded switchable protein module for ERα-mediated transcriptional regulation.Gene therapy · 2026Article
- Extraovarian gonadotropin negative feedback revealed by aromatase inhibition in female marmoset monkeys.American journal of physiology. Endocrinology and metabolism · 2017Article
- Potential contributions of heat shock proteins and related genes in sexual differentiation in yellow catfish (Pelteobagrus fulvidraco).Fish physiology and biochemistry · 2017Article
- Integrative and comparative reproductive biology: From alligators to xenobiotics.General and comparative endocrinology · 2016Review
- WAP four-disulfide core domain protein 2 gene(WFDC2) is a target of estrogen in ovarian cancer cells.Journal of ovarian research · 2016Article
- A new regulator of osteoclastogenesis: estrogen response element-binding protein in bone.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2011Article
- Hormone response element binding proteins: novel regulators of vitamin D and estrogen signaling.Steroids · 2011Review
- Heat shock protein 27 is required for sex steroid receptor trafficking to and functioning at the plasma membrane.Molecular and cellular biology · 2010Article
- Potential contributions of heat shock proteins to temperature-dependent sex determination in the American alligator.Sexual development : genetics, molecular biology, evolution, endocrinology, embryology, and pathology of sex determination and differentiation · 2010Article
- Estradiol and tamoxifen mediate rescue of the dominant-negative effects of estrogen response element-binding protein in vivo and in vitro.Endocrinology · 2009Article
- Back to the future: a new look at 'old' vitamin D.The Journal of endocrinology · 2008Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
New World primates exhibit a form of resistance to estrogens that is associated with overexpression of an estrogen response element (ERE)-binding protein (ERE-BP) and an intracellular estradiol (E(2))-binding protein (IEBP). Both proteins suppress E(2)-mediated transcription when overexpressed in estrogen receptor-alpha (ERalpha)-positive cells. Although ERE-BP acts as a competitor for ERE occupancy by liganded ERalpha, the function of IEBP and its human homolog, heat-shock protein 27 (hsp27), is less clear. In data presented here, we have used E(2)-responsive human MCF-7 breast cancer cells to show that IEBP/hsp27 can regulate estrogen signaling as a cytosolic decoy for E(2) and as a protein chaperone for ERalpha. Furthermore, co-immunoprecipitation, colocalization, yeast two-hybrid, and glutathione S-transferase pull-down analyses indicate that IEBP/hsp27 also interacts with ERE-BP to form a dynamic complex that appears to cycle between the cytoplasm and nucleus during normal estrogen signaling. Overexpression of either IEBP/hsp27 or ERE-BP in MCF-7 cells resulted in abnormal subcellular distribution of the IEBP/hsp27 and ERE-BP, with concomitant dysregulation of ERE occupancy as determined by chromatin immunoprecipitation. We hypothesize that IEBP/hsp27 and ERE-BP not only cause hormone resistance in New World primates but are also crucial to normal estrogen signaling in human cells. This appears to involve a physical association between the two proteins to form a complex that is able to interact with both E(2) and ERalpha in cytosolic and nuclear compartments.
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Registered trials
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.