UBR5 forms ligand-dependent complexes on chromatin to regulate nuclear hormone receptor stability
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Nuclear hormone receptors (NRs) are ligand-binding transcription factors that are widely targeted therapeutically. Agonist binding triggers NR activation and subsequent degradation by unknown ligand-dependent ubiquitin ligase machinery. NR degradation is critical for therapeutic efficacy in malignancies that are driven by retinoic acid and estrogen receptors. Here, we demonstrate the ubiquitin ligase UBR5 drives degradation of multiple agonist-bound NRs, including the retinoic acid receptor alpha (RARA), retinoid x receptor alpha (RXRA), glucocorticoid, estrogen, liver-X, progesterone, and vitamin D receptors. We present the high-resolution cryo-EMstructure of full-length human UBR5 and a negative stain model representing its interaction with RARA/RXRA. Agonist ligands induce sequential, mutually exclusive recruitment of nuclear coactivators (NCOAs) and UBR5 to chromatin to regulate transcriptional networks. Other pharmacological ligands such as selective estrogen receptor degraders (SERDs) degrade their receptors through differential recruitment of UBR5 or RNF111. We establish the UBR5 transcriptional regulatory hub as a common mediator and regulator of NR-induced transcription.
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These basic amino side chains alter effector selectivity, recruiting E3 ligase RNF111 to the newly exposed hydrophobic tail of ERα.
“these side chains alter effector selectivity, recruiting a new e3 ligase, RNF111, to the newly exposed hydrophobic tail of eRα (tsai et al. 2023) (Figure 4B, i).”
From From serendipity to strategy: molecular glue degraders in cancer therapeutics (2025) · cites this paper as tsai et al. 2023
The Results section, “SERDs engage distinct degradation pathways to degrade ER” (page not provided), reports that SERDs with basic amino moieties use RNF111 rather than UBR5 for ER degradation. It also reports RNF111 association with ER after fulvestrant treatment. The paper does not establish that RNF111 is recruited to a newly exposed hydrophobic tail of ERα; its discussion of a hydrophobic cleft concerns UBR5 and coactivator binding. (LLM, conf=0.86)
Experimental — accuracy not yet measuredFulvestrant and more promising next-generation SERDs, like camizestrant and elacestrant, harbor basic amino side chains.
“conversely, fulvestrant and more promising next-generation SeRDs, like camizestrant and elacestrant, harbor basic amino side chains.”
From From serendipity to strategy: molecular glue degraders in cancer therapeutics (2025) · cites this paper as tsai et al. 2023
The Results section identifies elacestrant and camizestrant as SERDs with basic amino moieties. It lists fulvestrant separately and describes it as an alkyl-tail-containing SERD, so the source does not support attributing a basic amino side chain to fulvestrant. No page number is available in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredNext-generation SERDs with acrylic side chains, like brilanestrant, engage the native E3 ligase UBR5.
“genetic screens revealed next-generation SeRDs with acrylic side chains, like brilanestrant, engaged the native e3 ligase uBR5 which has been shown to degrade several nuclear receptors (tsai et al. 2023).”
From From serendipity to strategy: molecular glue degraders in cancer therapeutics (2025) · cites this paper as tsai et al. 2023
Depending on the class of SERD, different E3 effectors are recruited.
“interestingly, depending on the class of SeRD, different e3 effectors are recruited.”
From From serendipity to strategy: molecular glue degraders in cancer therapeutics (2025) · cites this paper as tsai et al. 2023
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“…cleft. while this is a signal for cofactor binding, it is also a recognized degron for the uBR5 e3 ligase to induce degradation (Nawaz et al. 1999; tsai et al. 2023). without the formation of a ternary complex, these hormones are not classically considered as molecular glues, like auxin, and…”
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Identification of Small Molecule Inhibitors of PPM1D Using a Novel Drug Discovery PlatformPreprint
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Self-citationJevtić, P., Witus, S. R., McCloud, D. M., Yang, Z., Milunovic-Jevtic, A., Roh, H., & Rapé, M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.16.732780
Induced Estrogen Receptor SUMOylation drives SERD activityPreprint
Hinterndorfer, M., Schätz, C., Schmitt, S., Schoenlein, M., Hoi, D. M., Kręcioch, I., Frommelt, F., Shlei, M., Kater, L., Pačesa, M., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.26.734426
Self-citation
- Authors
- Tsai, J. M., Aguirre, J. D., Li, Y.-D., Brown, J., Focht, V., Kater, L., Kempf, G., Sandoval, B., Schmitt, S., Rutter, J. C., Galli, P., Sandate, C. R., Cutler, J. A., Zou, C., Donovan, K. A., Lumpkin, R. J., Cavadini, S., Park, P. M. C., Sievers, Q., Hatton, C., Ener, E., Regalado, B. D., Sperling, M. T., Słabicki, M., Kim, J., Zon, R., Zhang, Z., Miller, P. G., Belizaire, R., Sperling, A. S., Fischer, E. S., Irizarry, R., Armstrong, S. A., Thomä, N. H., & Ebert, B. L.
- Affiliations
- Broad Institute (US)
- Friedrich Miescher Institute (CH)
- Harvard University (US)
- University of Basel (CH)
- Boston Children's Hospital (US)
- Massachusetts General Hospital (US)
- Brigham and Women's Hospital (US)
- Corresponding author
- Thomä, Nicolas H.
- Ebert, Benjamin L.
- ORCID
- Tsai, Jonathan M.
- Aguirre, Jacob D.
- Li, Yen-Der
- Brown, Jared
- Kempf, Georg
- Sandoval, Brittany
- Rutter, Justine C.
- Galli, Pius
- Sandate, Colby R.
- Cutler, Jevon A.
- Zou, Charles
- Donovan, Katherine A.
- Lumpkin, Ryan J.
- Cavadini, Simone
- Park, Paul M.C.
- Sievers, Quinlan
- Hatton, Charlie
- Ener, Elizabeth
- Kim, Jeonghyeon
- Zon, Rebecca
- Zhang, Zinan
- Miller, Peter G.
- Belizaire, Roger
- Sperling, Adam S.
- Fischer, Eric S.
- Irizarry, Rafael
- Armstrong, Scott A.
- Thomä, Nicolas H.
- Ebert, Benjamin L.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2023-08
- Volume
- 83
- Issue
- 15
- Pages
- 2753-2767.e10
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC11134608
- OpenAlex
- W4384926988
- Cited by
- 68
- References
- 106
- Citations by year
- 2026: 16 · 2025: 27 · 2024: 18 · 2023: 7
- FWCI
- 11.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion, cc-by)
- Funders
- National Science Foundation
- Sanofi
- Broad Institute
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (179541, 201206)
- Astellas Pharma
- National Institutes of Health (DP5OD036132)
- National Heart, Lung, and Blood Institute (R01HL082945)
- National Cancer Institute (T32CA251062, K08CA252174, R35CA253125, P50CA206963, P01CA066996, K08CA263183, R01CA262188)
- National Institute of General Medical Sciences (T32GM144273, R35GM131802)
- H2020 European Research Council (884331)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- UBR5, nuclear receptors, receptor degradation, retinoic acid receptor alpha, retinoid X receptor alpha, chromatin recruitment, cryo-EM structure, selective estrogen receptor degrader, RNF111, estrogen receptor, glucocorticoid receptor, liver X receptor, progesterone receptor, vitamin D receptor, transcriptional regulation
- MeSH terms
- Chromatin, Humans, Ligands, Transcription Factors, Ubiquitins, Receptors, Cytoplasmic and Nuclear, Ubiquitin-Protein Ligases
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