Ring finger protein 5 mediates STING degradation through ubiquitinating K135 and K155 in a teleost fish
Xiaowei Qin, Chuanrui Li, Mincong Liang, Zhen Qian, Yanlin You, Shaoping Weng, Jianguo He, Changjun Guo · 2024
Read Ring finger protein 5 mediates STING degradation through ubiquitinating K135 and K155 in a teleost fish by Xiaowei Qin, Chuanrui Li, Mincong Liang, Zhen Qian, Yanlin You, Shaoping Weng, Jianguo He, Changjun Guo (2024) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-11668637.txt.
Description
Xiaowei Qin and others studied antiviral control in mandarin fish in 2024. STING protein switches on interferon guard duty. Too much interferon harms the host though. A regulator protein tags STING for disposal. Mammal work showed one tagging site. Fish ways were still unknown here.
The fish protein used two new sites. Tagging sent STING to the proteasome. Virus-fighting action weakened after that clearing. Interferon signals fell as a result. The pathway is held down overall. Findings clarify fish immune control. Fish farming disease work may benefit later. Further teleost research is invited.
Catalog record
| CREATOR | Xiaowei Qin, Chuanrui Li, Mincong Liang, Zhen Qian, Yanlin You, Shaoping Weng, Jianguo He, Changjun Guo |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 35 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |