Fig. 8: Scheme of αSynO−huPrP cluster formation.
From: Clustering of human prion protein and α-synuclein oligomers requires the prion protein N-terminus
a–c Cluster formation observed in this study. HuPrP clusters with αSynO through the intrinsically disordered huPrP N-terminus (a). The huPrP N-terminus is sufficient for αSynO condensation (b). αSynO and AβO cocluster with huPrP (c). d–e Potential cluster formation of PrPC or its N-terminal fragment N1 in vivo. PrPC cluster formation may affect neurotoxic signaling of αSynO by promoting assembly of higher-order signaling complexes (d). Removal of neurotoxic amyloid oligomers by cluster formation may contribute to the neuroprotective activity of N1 (e).
