ArticleMolecular and cellular biology2001
Ligand-mediated assembly and real-time cellular dynamics of estrogen receptor alpha-coactivator complexes in living cells.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 150 citations in OpenAlex.
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- Molecular dynamics of estrogen-related receptors and their regulatory proteins: roles in transcriptional control for endocrine and metabolic signaling.Anatomical science international · 2022Review
- Endocrine disrupting chemicals differentially alter intranuclear dynamics and transcriptional activation of estrogen receptor-α.iScience · 2021Article
- Estrogen-induced transcription at individual alleles is independent of receptor level and active conformation but can be modulated by coactivators activity.Nucleic acids research · 2020Article
- The ERβ5 splice variant increases oestrogen responsiveness of ERαpos Ishikawa cells.Endocrine-related cancer · 2020Article
- Fbxo22-mediated KDM4B degradation determines selective estrogen receptor modulator activity in breast cancer.The Journal of clinical investigation · 2018Article
- Dynamic assembly and activation of estrogen receptor α enhancers through coregulator switching.Genes & development · 2017Article
- UHRF1 targets DNMT1 for DNA methylation through cooperative binding of hemi-methylated DNA and methylated H3K9.Nature communications · 2013Article
- The ligand-mediated nuclear mobility and interaction with estrogen-responsive elements of estrogen receptors are subtype specific.Journal of molecular endocrinology · 2012Article
- A novel histone H4 arginine 3 methylation-sensitive histone H4 binding activity and transcriptional regulatory function for signal recognition particle subunits SRP68 and SRP72.The Journal of biological chemistry · 2012Article
- Tetradian oscillation of estrogen receptor α is necessary to prevent liver lipid deposition.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Back to your heart: ubiquitin proteasome system-regulated signal transduction.Journal of molecular and cellular cardiology · 2012Review
- Research resource: The estrogen receptor α cistrome defined by DamIP.Molecular endocrinology (Baltimore, Md.) · 2012Article
- Live-cell fluorescence correlation spectroscopy dissects the role of coregulator exchange and chromatin binding in retinoic acid receptor mobility.Journal of cell science · 2011Article
- Liganded and unliganded activation of estrogen receptor and hormone replacement therapies.Biochimica et biophysica acta · 2011Review
- Live cell imaging of the cancer-related transcription factor RUNX2 during mitotic progression.Journal of cellular physiology · 2011Article
- Steroid signaling activation and intracellular localization of sex steroid receptors.Journal of cell communication and signaling · 2010Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Studies with live cells demonstrate that agonist and antagonist rapidly (within minutes) modulate the subnuclear dynamics of estrogen receptor alpha (ER) and steroid receptor coactivator 1 (SRC-1). A functional cyan fluorescent protein (CFP)-tagged lac repressor-ER chimera (CFP-LacER) was used in live cells to discretely immobilize ER on stably integrated lac operator arrays to study recruitment of yellow fluorescent protein (YFP)-steroid receptor coactivators (YFP-SRC-1 and YFP-CREB binding protein [CBP]). In the absence of ligand, YFP-SRC-1 is found dispersed throughout the nucleoplasm, with a surprisingly high accumulation on the CFP-LacER arrays. Agonist addition results in the rapid (within minutes) recruitment of nucleoplasmic YFP-SRC-1, while antagonist additions diminish YFP-SRC-1-CFP-LacER associations. Less ligand-independent colocalization is observed with CFP-LacER and YFP-CBP, but agonist-induced recruitment occurs within minutes. The agonist-induced recruitment of coactivators requires helix 12 and critical residues in the ER-SRC-1 interaction surface, but not the F, AF-1, or DNA binding domains. Fluorescence recovery after photobleaching indicates that YFP-SRC-1, YFP-CBP, and CFP-LacER complexes undergo rapid (within seconds) molecular exchange even in the presence of an agonist. Taken together, these data suggest a dynamic view of receptor-coregulator interactions that is now amenable to real-time study in living cells.
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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.