Molecular MetabolismGeneticsPeer-reviewed journal article
Pioneer factor Foxa2 enables ligand-dependent activation of LXRα
Jessica KainiD, Xiaolong WeiiD, Nihal A. ReddyiD, Andrew J. PriceiD, Claire E. WoodsiD, Irina M. BochkisiD
Abstract
Type II nuclear hormone receptors, such as FXR, LXR, and PPAR, which function in glucose and lipid metabolism and serve as drug targets for metabolic diseases, are permanently positioned in the nucleus regardless of the ligand status. Ligand activation of these receptors is thought to occur by co-repressor/co-activator exchange, followed by initiation of transcription. However, recent genome-wide location analysis showed that LXR and PPAR binding in the liver is largely ligand-dependent. We hypothesized that pioneer factor Foxa2 evicts nucleosomes to enable ligand-dependent receptor binding. We show that chromatin accessibility, LXR occupancy, and LXR-dependent gene expression upon ligand activation require Foxa2. Unexpectedly, Foxa2 occupancy is drastically increased when LXR is bound by an agonist. Our results suggest that Foxa2 and LXR bind DNA as an interdependent complex during ligand activation. Our model requiring pioneering activity for ligand activation challenges the existing co-factor exchange mechanism and expands current understanding of nuclear receptor biology, suggesting that chromatin accessibility needs to be considered in design of drugs targeting nuclear receptors.
- Citations
- 24
- FWCI
- 1.25
- Field percentile
- top 21%
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Pioneer factor Foxa2 mediates chromatin conformation changes in ligand-dependent activation of nuclear receptor FXR
Y. Hao, L. Han, … I. Bochkis·bioRxiv·Mar 6, 2023
- Open the LID: LXRα regulates ChREBPα transactivity in a target gene-specific manner through an agonist-modulated LBD-LID interaction
Qiong Fan, Rikke C. Nørgaard, … Thomas Sæther·CellsPeer-reviewed·May 13, 2020
- Asymmetric binding of coactivator SRC1 to FXR-RXR and allosteric communication within the complex
Yanan Sheng, Yaoting Guo, … Jinsong Liu·Communications BiologyPeer-reviewed·Mar 13, 2025
- System analysis of cross-talk between nuclear receptors reveals an opposite regulation of the cell cycle by LXR and FXR in human HepaRG liver cells
L. Wigger, C. Casals Casas, … B. Desvergne·bioRxiv·Mar 25, 2019
- Towards a unified molecular mechanism for ligand-dependent activation of NR4A-RXR heterodimers
Xiaoyu Yu, Yuanjun He, … Douglas J. Kojetin·bioRxiv·Mar 19, 2025
- The nuclear receptor LRH-1 discriminates between ligands using distinct allosteric signaling circuits
S. Mays, D. Hercules, … C. D. Okafor·bioRxiv·Jan 27, 2023