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Related Experiment Video

Updated: Dec 19, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Liquid-liquid phase separation induces pathogenic tau conformations in vitro.

Nicholas M Kanaan^1,2,3, Chelsey Hamel⁴, Tessa Grabinski⁴

¹Department of Translational Neuroscience, College of Human Medicine, Michigan State University, Grand Rapids, MI, 49503, USA. nkanaan@msu.edu.

Nature Communications

|June 6, 2020

Summary

Tau protein forms dynamic liquid droplets in vitro, a process enhanced by disease-associated modifications. This liquid-liquid phase separation may promote toxic tau conformations linked to neurodegenerative diseases.

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In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

Published on: November 20, 2018

Area of Science:

Cell Biology
Neuroscience
Biochemistry

Background:

Membrane-less organelles regulate cellular processes through liquid-liquid phase separation (LLPS).
Tau protein, implicated in Alzheimer's disease and tauopathies, undergoes LLPS, linking it to neurodegenerative diseases.

Purpose of the Study:

To investigate tau protein's ability to form dynamic liquid droplets in vitro.
To determine how disease-associated modifications affect tau droplet formation and dynamics.
To explore the consequences of extended tau phase separation on protein conformation and aggregation.

Main Methods:

In vitro formation of tau liquid droplets under physiological conditions (molecular crowding).
Assessment of droplet formation and dynamics with disease-associated tau modifications (AT8 epitope, P301L mutation).
Analysis of tau conformation and oligomerization following extended phase separation using biochemical assays.

Main Results:

Tau forms dynamic liquid droplets in vitro at physiological protein concentrations.
Disease-associated modifications (AT8, P301L) enhance tau droplet formation but reduce droplet dynamics.
Extended phase separation promotes toxic tau conformations and oligomerization, particularly in P301L tau, without inducing filamentous aggregation.

Conclusions:

Tau protein undergoes liquid-liquid phase separation in vitro, forming dynamic droplets.
Disease-associated tau modifications enhance phase separation and promote the formation of toxic, non-filamentous tau oligomers.
Tau phase separation may be a key mechanism in the pathogenesis of tauopathies.