Figure S12. Hypothetical mechanism of differential effects of tauopathy versus synucleinopathy on G85R-SOD1:YFP secondary aggregation in the spinal cord and cortex. In the JNPL3 spinal cord, misfolded tau occupies proteostatic factors (Factor X) that the mutant SOD1 reporter is also dependent upon for folding or degradation. In the cortex of rTg4510 mice, the levels of Factor X could be higher, or other proteostatic factors specific to brain (Factor Y) could be present to prevent the aggregation mutant SOD1. Meanwhile, misfolded αSyn occupies proteostatic factors distinct from those of tau (Factor Z), leaving a sufficient level of Factor X to prevent the aggregation of mutant SOD1. (TIF 553 kb
