Darwich et al. suggested that the vacuolar tauopathy mutation reduces VCP’s disaggregase activity [19], and hence clearance of existing tau aggregates; whereas Zhu et al. proposed that VCP-mediated surveillance of damaged vesicles and lysophagy suppresses α-synuclein aggregation, although this was based on cationic lipid-mediated amyloid delivery to biosensors that bypassed standard endocytosis [20]. This evidence concerns the gene MAPT and tauopathy.