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| Auteurs principaux: | , , , , , , , , , , |
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| Format: | Artículo científico |
| Langue: | en |
| Publié: |
The Journal of biological chemistry
2026
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| Accès en ligne: | https://pubmed.ncbi.nlm.nih.gov/42103230/ |
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Table des matières:
- TRIM25 enhances hypoxia signaling by catalyzing K11-linked polyubiquitination and stabilization of HIF-α. Li, Ziyi Li, Jun Li, Zhi Wang, Rui Yuan, Le Song, Yanan Wang, Yanyi Yan, Runkun Lai, Fuxiang Wang, Jing Xiao, Wuhan TRIM25 is an E3 ubiquitin ligase involved in various cellular processes due to its enzymatic activity. In particular, it plays a role in antiviral innate immunity. Here, we demonstrate that TRIM25 modulates hypoxia signaling. TRIM25 interacts with HIF-1α and HIF-2α, stabilizing them. TRIM25 catalyzes K11-linked polyubiquitination of HIF-1α at K719 and K721 and of HIF-2α at K709. This results in the stabilization of the proteins and enhanced hypoxia signaling. Moreover, TRIM25-mediated augmentation of hypoxia signaling depends on HIF-1α. Trim25-deficient mice are more sensitive to hypoxia, and zebrafish lacking trim25 show a similar phenotype. These data reveal TRIM25's role in regulating hypoxia signaling and provide insight into a new mechanism that modulates the stabilization and activity of HIF-1α and HIF-2α.