ArticleMolecular biology of the cell1999
Direct visualization of the human estrogen receptor alpha reveals a role for ligand in the nuclear distribution of the receptor.
Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 260 citations in OpenAlex.
- Endothelial Estrogen Receptor Alpha Inhibits Plaque Inflammation in Both Sexes.Circulation research · 2026Article
- Smooth muscle cell estrogen receptor alpha promotes arterial stiffness in the absence of estradiol.bioRxiv : the preprint server for biology · 2026Article
- Hsp40 co-chaperone Droj2 temporally regulates EcRA dynamics during collective cell migration.Frontiers in cell and developmental biology · 2026Article
- Chemogenomics for steroid hormone receptors (NR3).Communications chemistry · 2025Article
- Review
- Heterochromatin protein 1 alpha (HP1α) undergoes a monomer to dimer transition that opens and compacts live cell genome architecture.Nucleic acids research · 2024Article
- A rapid and bidirectional reporter of neural activity reveals neural correlates of social behaviors in Drosophila.Nature neuroscience · 2023Article
- The dynamical organization of the core pluripotency transcription factors responds to differentiation cues in early S-phase.Frontiers in cell and developmental biology · 2023Article
- Phase Ib Study of the Oral Proteasome Inhibitor Ixazomib (MLN9708) and Fulvestrant in Advanced ER+ Breast Cancer Progressing on Fulvestrant.The oncologist · 2021Article
- Unraveling the molecular interactions involved in phase separation of glucocorticoid receptor.BMC biology · 2020Article
- Mediator subunit MED1 modulates intranuclear dynamics of the thyroid hormone receptor.Journal of cellular biochemistry · 2020Article
- Dynamical reorganization of the pluripotency transcription factors Oct4 and Sox2 during early differentiation of embryonic stem cells.Scientific reports · 2020Article
- Role of SUMOylation in differential ERα transcriptional repression by tamoxifen and fulvestrant in breast cancer cells.Oncogene · 2019Article
- Exploring Protein⁻Protein Interaction in the Study of Hormone-Dependent Cancers.International journal of molecular sciences · 2018Review
- Intranuclear Mobility of Estrogen Receptor: Implication for Transcriptional Regulation.Acta histochemica et cytochemica · 2018Article
- Estrogen receptor profiling and activity in cardiac myocytes.Molecular and cellular endocrinology · 2016Article
- Structural and functional characterization of aromatase, estrogen receptor, and their genes in endocrine-responsive and -resistant breast cancer cells.The Journal of steroid biochemistry and molecular biology · 2016Review
- Estrogen-related Receptor β Reduces the Subnuclear Mobility of Estrogen Receptor α and Suppresses Estrogen-dependent Cellular Function.The Journal of biological chemistry · 2015Article
- Gonadal steroid hormones and the hypothalamo-pituitary-adrenal axis.Frontiers in neuroendocrinology · 2014Review
- Reprogramming the chromatin landscape: interplay of the estrogen and glucocorticoid receptors at the genomic level.Cancer research · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The human estrogen receptor alpha (ER alpha) has been tagged at its amino terminus with the S65T variant of the green fluorescent protein (GFP), allowing subcellular trafficking and localization to be observed in living cells by fluorescence microscopy. The tagged receptor, GFP-ER, is functional as a ligand-dependent transcription factor, responds to both agonist and antagonist ligands, and can associate with the nuclear matrix. Its cellular localization was analyzed in four human breast cancer epithelial cell lines, two ER+ (MCF7 and T47D) and two ER- (MDA-MB-231 and MDA-MB-435A), under a variety of ligand conditions. In all cell lines, GFP-ER is observed only in the nucleus in the absence of ligand. Upon the addition of agonist or antagonist ligand, a dramatic redistribution of GFP-ER from a reticular to punctate pattern occurs within the nucleus. In addition, the full antagonist ICI 182780 alters the nucleocytoplasmic compartmentalization of the receptor and causes partial accumulation in the cytoplasm in a process requiring continued protein synthesis. GFP-ER localization varies between cells, despite being cultured and treated in a similar manner. Analysis of the nuclear fluorescence intensity for variation in its frequency distribution helped establish localization patterns characteristic of cell line and ligand. During the course of this study, localization of GFP-ER to the nucleolar region is observed for ER- but not ER+ human breast cancer epithelial cell lines. Finally, our work provides a visual description of the "unoccupied" and ligand-bound receptor and is discussed in the context of the role of ligand in modulating receptor activity.
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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.