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TitleUBR5 forms ligand-dependent complexes on chromatin to regulate nuclear hormone receptor stability.
Journal, issue, pagesMol Cell, Vol. 83, Issue 15, Page 2753-2767.e10, Year 2023
Publish dateAug 3, 2023
AuthorsJonathan M Tsai / Jacob D Aguirre / Yen-Der Li / Jared Brown / Vivian Focht / Lukas Kater / Georg Kempf / Brittany Sandoval / Stefan Schmitt / Justine C Rutter / Pius Galli / Colby R Sandate / Jevon A Cutler / Charles Zou / Katherine A Donovan / Ryan J Lumpkin / Simone Cavadini / Paul M C Park / Quinlan Sievers / Charlie Hatton / Elizabeth Ener / Brandon D Regalado / Micah T Sperling / Mikołaj Słabicki / Jeonghyeon Kim / Rebecca Zon / Zinan Zhang / Peter G Miller / Roger Belizaire / Adam S Sperling / Eric S Fischer / Rafael Irizarry / Scott A Armstrong / Nicolas H Thomä / Benjamin L Ebert /
PubMed AbstractNuclear hormone receptors (NRs) are ligand-binding transcription factors that are widely targeted therapeutically. Agonist binding triggers NR activation and subsequent degradation by unknown ligand- ...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.
External linksMol Cell / PubMed:37478846 / PubMed Central
MethodsEM (single particle)
Resolution3.36 - 25.0 Å
Structure data

17539

8p82

EMDB-17539, PDB-8p82:
Cryo-EM structure of dimeric UBR5
Method: EM (single particle) / Resolution: 3.36 Å

17540

8p83

EMDB-17540, PDB-8p83:
Cryo-EM structure of full-length human UBR5 (homotetramer)
Method: EM (single particle) / Resolution: 3.87 Å

EMDB-17542: Negative stain map of UBR5 (dimer) in complex with RARA/RXRA
Method: EM (single particle) / Resolution: 25.0 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsLIGASE / E3 / ubiquitin ligase / HECT

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