Clusterin ameliorates tau pathology in vivo by inhibiting fibril formation

Aleksandra M. Wojtas, Yari Carlomagno, Jonathon P. Sens, Silvia S. Kang, Tanner D. Jensen, Aishe Kurti, Kelsey E. Baker, Taylor J. Berry, Virginia R. Phillips, Monica Casey Castanedes, Ayesha Awan, Michael DeTure, Cristhoper H.Fernandez De Castro, Ariston L. Librero, Mei Yue, Lillian Daughrity, Karen R. Jansen-West, Casey N. Cook, Dennis W. Dickson, Leonard PetrucelliJohn D. Fryer

Research output: Contribution to journalArticlepeer-review


The molecular chaperone Clusterin (CLU) impacts the amyloid pathway in Alzheimer’s disease (AD) but its role in tau pathology is unknown. We observed CLU co-localization with tau aggregates in AD and primary tauopathies and CLU levels were upregulated in response to tau accumulation. To further elucidate the effect of CLU on tau pathology, we utilized a gene delivery approach in CLU knock-out (CLU KO) mice to drive expression of tau bearing the P301L mutation. We found that loss of CLU was associated with exacerbated tau pathology and anxiety-like behaviors in our mouse model of tauopathy. Additionally, we found that CLU dramatically inhibited tau fibrilization using an in vitro assay. Together, these results demonstrate that CLU plays a major role in both amyloid and tau pathologies in AD.

Original languageEnglish (US)
Article number210
JournalActa Neuropathologica Communications
Issue number1
StatePublished - Dec 2020


  • Alzheimer’s disease
  • Clusterin
  • Tau
  • Tauopathy

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Clinical Neurology
  • Cellular and Molecular Neuroscience


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