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

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Article number5768
JournalInternational journal of molecular sciences
Volume22
Issue number11
DOIs
Publication statusPublished - Jun 1 2021
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

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