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Related Experiment Video

Updated: Sep 13, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Polyserine-tau interactions modulate tau fibrillization.

James Pratt¹, Kathleen McCann², Jeff Kuo¹

¹Department of Biochemistry, University of Colorado Boulder, Boulder, Colorado, USA.

The Journal of Biological Chemistry

|July 27, 2025

Summary

This summary is machine-generated.

Polyserine domains self-assemble and directly bind tau, creating sites for tau aggregation. This finding clarifies molecules influencing tau aggregation in neurodegenerative diseases.

Keywords:

RNA-protein interaction protein aggregation recombinant protein expression serine stress granule tau protein (tau)

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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:

Neuroscience
Biochemistry
Cell Biology

Background:

Tau aggregates are key pathological hallmarks in neurodegenerative diseases.
Molecules that modulate intracellular tau aggregation remain largely unknown.
Polyserine-rich domains were previously found to enrich in tau aggregates and promote tau pathology.

Purpose of the Study:

To investigate if polyserine domains are sufficient to create sites of tau aggregation.
To elucidate the mechanism by which polyserine domains influence tau aggregation.
To determine the role of polyserine self-assembly in tau fibrillization.

Main Methods:

In vitro biochemical assays to study polyserine-tau interactions.
Analysis of purified polyserine self-assembly.
Investigating the recruitment of RNA and tau seeds by polyserine assemblies.
Utilizing polyserine variants to separate distinct functions.

Main Results:

Polyserine domains are sufficient to define assemblies as sites of tau aggregation.
Purified polyserine self-assembles and directly interacts with monomeric and fibrillar tau.
Polyserine-tau assemblies recruit RNA, accelerating tau fibrillization in vitro.
Polyserine self-assembly, not just enrichment, is crucial for stimulating tau aggregation.

Conclusions:

Polyserine domains self-assemble into structures that directly interact with tau.
These polyserine assemblies serve as preferential sites for tau aggregation.
Understanding polyserine's role offers new insights into neurodegenerative disease mechanisms.