Darwich et al. suggested that the vacuolar tauopathy mutation reduces VCP disaggregase activity (21), and hence clearance of existing tau aggregates; whereas Zhu et al. proposed that VCP-mediated surveillance of damaged vesicles and lysophagy governed suppressed a-synuclein aggregation, although this was based on cation-mediated amyloid delivery to biosensors that bypassed standard endocytosis (22). This evidence concerns the gene VCP and tauopathy.