Human polymerase δ-interacting protein 2 (Poldip2) inhibits the formation of human tau oligomers and fibrils

Kazutoshi Kasho, Lukas Krasauskas, Vytautas Smirnovas, Gorazd Stojkovič, Ludmilla A. Morozova-Roche, Sjoerd Wanrooij

研究成果: ジャーナルへの寄稿学術誌査読

抄録

A central characteristic of Alzheimer’s disease (AD) and other tauopathies is the accumulation of aggregated and misfolded Tau deposits in the brain. Tau-targeting therapies for AD have been unsuccessful in patients to date. Here we show that human polymerase δ-interacting protein 2 (PolDIP2) interacts with Tau. With a set of complementary methods, including thioflavin-T-based aggregation kinetic assays, Tau oligomer-specific dot-blot analysis, and single oligomer/fibril analysis by atomic force microscopy, we demonstrate that PolDIP2 inhibits Tau aggregation and amyloid fibril growth in vitro. The identification of PolDIP2 as a potential regulator of cellular Tau aggregation should be considered for future Tau-targeting therapeutics.

本文言語英語
論文番号5768
ジャーナルInternational journal of molecular sciences
22
11
DOI
出版ステータス出版済み - 6月 1 2021
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 触媒
  • 分子生物学
  • 分光学
  • コンピュータ サイエンスの応用
  • 物理化学および理論化学
  • 有機化学
  • 無機化学

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