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Significance Frontotemporal lobar degeneration (FTLD) is second only to Alzheimer’s disease as a cause of dementia, and we find the scaffolding protein β-arrestin2 is elevated in human brains with this condition, and is responsible for accumulation of pathological tau tangles. Increased β-arrestin2 impairs tau clearance and promotes tau aggregation by impeding the autophagy cargo carrier p62/SQSTM1. Such activity requires β-arrestin2 in its oligomeric form, an assembly state that is not involved with receptor binding. Virus delivered gene therapy to the brain with dominant-negative mutant β-arrestin2s ablates pathologic tau in neurons of a mouse model of FTLD-tau, revealing a strategy to mitigate tauopathy by targeting β-arrestin2 oligomerization.

β-Arrestin2 oligomers impair the clearance of pathological tau and increase tau aggregates