SPOP-mediated nuclear ubiquitination degradation of p62/SQSTM1 contributes to HR repair
Xiaojuan Yang, Ying Zhou, Qing Huang, Lingli Wang, Su Zhang, Xuyang Yang, Lei Qiu, Yang Meng, Hong Wu, Bo Zhang, Kunlin Xie, Junhong Han, Qing Zhu · 2026
Read SPOP-mediated nuclear ubiquitination degradation of p62/SQSTM1 contributes to HR repair by Xiaojuan Yang, Ying Zhou, Qing Huang, Lingli Wang, Su Zhang, Xuyang Yang, Lei Qiu, Yang Meng, Hong Wu, Bo Zhang, Kunlin Xie, Junhong Han, Qing Zhu (2026) 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/PMC13384900.txt.
Description
Xiaojuan Yang and colleagues untangle how two proteins govern a DNA repair route in 2026 work. The protein SPOP tags its partner p62 for removal in the cell nucleus after DNA damage. That removal lifts levels of RAD51 and FLNA, two helpers of homologous recombination, a high-accuracy repair path.
Patient-derived changes in the p62 binding motif made cells more sensitive to radiation in lab and animal tests. Those changes cut repair helper levels and weakened repair focus formation. The authors suggest that breaking the SPOP-p62 link could help overcome radiation resistance in cancer therapy.
Catalog record
| CREATOR | Xiaojuan Yang, Ying Zhou, Qing Huang, Lingli Wang, Su Zhang, Xuyang Yang, Lei Qiu, Yang Meng, Hong Wu, Bo Zhang, Kunlin Xie, Junhong Han, Qing Zhu |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 75259 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |