CPEB3 selectively inhibits α-synuclein aggregation without modulating TDP-43 pathology - PubMed
3 hours ago
- #Parkinson's disease
- #neurodegenerative diseases
- #protein aggregation
- CPEB3's first prion-like domain (PRD1) selectively inhibits α-synuclein (α-Syn) aggregation.
- PRD1 interacts with the amyloid core of α-Syn, suppressing its aggregation.
- PRD1 delays liquid-liquid phase separation (LLPS)-mediated α-Syn aggregation.
- No interaction was found between PRD1 and the C-terminal domain of TDP-43 (TDP-43CTD).
- The study highlights the selective inhibition of α-Syn aggregation by PRD1 without affecting TDP-43 pathology.