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Disruptors of the Hsp90/Aha1 complex that reduce tau aggregation

Aberrant aggregation of misfolded microtubule‐associated protein tau (MAPT, tau) is a hallmark of Alzheimer’s disease (AD) and other neurodegenerative tauopathies. Recently, the ATP‐dependent molecular chaperone family has been identified as a critical mediator of the pathogenic accumulation of misfolded tau. In particular, studies have demonstrated that inhibiting the ATPase activity of Hsp90 reduces pathological tau accumulation and promotes the clearance of tau via the proteosome.