Back

Circular RNA aptamers act as superb sub-stoichiometric chaperones to prevent cytosolic TDP-43 condensation

Wu, H.; Luan, P.-F.; Hu, J.; Nan, F.; Li, L.; Pan, Y.-Y.; Jiang, B.-W.; Chen, J.-W.; Wang, X.; Liu, J.; Xu, G.; Liu, C.; Chen, L.-L.

2026-06-02 molecular biology
10.64898/2026.06.01.729436 bioRxiv
Show abstract

Pathological protein misfolding and aggregation underlie many devastating human diseases, yet strategies to selectively neutralize aggregation-prone protein states without perturbing their normal functions remain limited. Here we identify loosely structured circular RNA (cRNA) aptamers, circT3 and its minimized 116-nt variant circT3-M3, as superb sub-stoichiometric RNA chaperones that suppress pathological assembly of TAR DNA-binding protein 43 (TDP-43), a defining feature of amyotrophic lateral sclerosis and frontotemporal dementia, in vitro and in cells. Rather than acting through simple stoichiometric sequestration, these cRNA aptamers engage TDP-43 transiently and iteratively through functionally and pathologically important residues in the RRM1 domain. Such interaction enables a single cRNA aptamer to promote rapid and multiple RRM1-dependent homomeric assembly, thereby stabilizing TDP-43 in a soluble oligomeric state to outcompete the C-terminal prion-like domain-driven condensation and supersaturation. Together, our findings establish cRNA aptamers as highly efficient subcellular RNA chaperones with exceptionally potent low-dose activity and highlight their promise as next-generation RNA therapeutics for certain protein-aggregation disorders.

Matching journals

The top 3 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.