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Significance The accumulation of toxic tau protein, as in Alzheimer’s disease, is regulated by the 90-kDa heat shock protein (Hsp90) chaperone system. Inhibition of Hsp90 has been shown to reduce tau levels. However, Hsp90 inhibition can be problematic due to a lack of blood–brain barrier permeability and established toxicities. Here, we demonstrate that the Hsp90 cochaperone, ATPase homolog 1 (Aha1), dramatically increases the production of aggregated tau in vitro and in a mouse model of neurodegenerative disease. Moreover, inhibition of Aha1 reduced tau accumulation in cultured cells. These data identify Aha1 as a target for the treatment of tauopathies.

Hsp90 activator Aha1 drives production of pathological tau aggregates