ArticleJournal of cell science2011
Live-cell fluorescence correlation spectroscopy dissects the role of coregulator exchange and chromatin binding in retinoic acid receptor mobility.
Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 50 citations in OpenAlex.
- Genome-wide chromatin profiling reveals a nonlimiting role for RXR in macrophage-like cells stimulated with multiple nuclear receptor agonists.The Journal of biological chemistry · 2026Article
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- Both the transcriptional activator, Bcd, and repressor, Cic, form small mobile oligomeric clusters.Biophysical journal · 2025Article
- Surprising features of nuclear receptor interaction networks revealed by live-cell single-molecule imaging.eLife · 2025Article
- Surprising Features of Nuclear Receptor Interaction Networks Revealed by Live Cell Single Molecule Imaging.bioRxiv : the preprint server for biology · 2024Article
- Agonist-controlled competition of RAR and VDR nuclear receptors for heterodimerization with RXR is manifested in their DNA binding.The Journal of biological chemistry · 2023Article
- Article
- Doxorubicin impacts chromatin binding of HMGB1, Histone H1 and retinoic acid receptor.Scientific reports · 2022Article
- Agonist binding directs dynamic competition among nuclear receptors for heterodimerization with retinoid X receptor.The Journal of biological chemistry · 2020Article
- Labelled regulatory elements are pervasive features of the macrophage genome and are dynamically utilized by classical and alternative polarization signals.Nucleic acids research · 2019Article
- mTORC1 Controls Phase Separation and the Biophysical Properties of the Cytoplasm by Tuning Crowding.Cell · 2018Article
- Optimizing fluorescent protein expression for quantitative fluorescence microscopy and spectroscopy using herpes simplex thymidine kinase promoter sequences.FEBS open bio · 2018Article
- Coactivators and general transcription factors have two distinct dynamic populations dependent on transcription.The EMBO journal · 2017Article
- Mapping the Dynamics of the Glucocorticoid Receptor within the Nuclear Landscape.Scientific reports · 2017Article
- Quantitative imaging of mammalian transcriptional dynamics: from single cells to whole embryos.BMC biology · 2016Review
- MHC I Expression Regulates Co-clustering and Mobility of Interleukin-2 and -15 Receptors in T Cells.Biophysical journal · 2016Article
- Intracellular kinetics of the androgen receptor shown by multimodal Image Correlation Spectroscopy (mICS).Scientific reports · 2016Article
- In vivo fluorescence correlation spectroscopy analyses of FMBP-1, a silkworm transcription factor.FEBS open bio · 2016Article
- Length of intact plasma membrane determines the diffusion properties of cellular water.Scientific reports · 2016Article
- Evidence for Homodimerization of the c-Fos Transcription Factor in Live Cells Revealed by Fluorescence Microscopy and Computer Modeling.Molecular and cellular biology · 2015Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The retinoic acid receptor (RAR) is a member of the nuclear receptor superfamily. This ligand-inducible transcription factor binds to DNA as a heterodimer with the retinoid X receptor (RXR) in the nucleus. The nucleus is a dynamic compartment and live-cell imaging techniques make it possible to investigate transcription factor action in real-time. We studied the diffusion of EGFP-RAR by fluorescence correlation spectroscopy (FCS) to uncover the molecular interactions determining receptor mobility. In the absence of ligand, we identified two distinct species with different mobilities. The fast component has a diffusion coefficient of D(1)=1.8-6.0 μm(2)/second corresponding to small oligomeric forms, whereas the slow component with D(2)=0.05-0.10 μm(2)/second corresponds to interactions of RAR with the chromatin or other large structures. The RAR ligand-binding-domain fragment also has a slow component, probably as a result of indirect DNA-binding through RXR, with lower affinity than the intact RAR-RXR complex. Importantly, RAR-agonist treatment shifts the equilibrium towards the slow population of the wild-type receptor, but without significantly changing the mobility of either the fast or the slow population. By using a series of mutant forms of the receptor with altered DNA- or coregulator-binding capacity we found that the slow component is probably related to chromatin binding, and that coregulator exchange, specifically the binding of the coactivator complex, is the main determinant contributing to the redistribution of RAR during ligand activation.
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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.