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Related Experiment Video

Updated: Jul 25, 2025

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry

Published on: December 8, 2015

DnaJC7 specifically regulates tau seeding.

Valerie Ann Perez¹, David W Sanders¹, Ayde Mendoza-Oliva¹

¹Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, United States.

|June 30, 2023

Summary

This summary is machine-generated.

The J domain protein DnaJC7 specifically binds tau, preventing toxic protein aggregation in neurodegenerative diseases. Its J domain is crucial for stimulating Hsp70 activity, highlighting a key mechanism in tauopathy regulation.

Keywords:

DnaJC7 J domain protein amyloid biochemistry chaperones chemical biology human neuroscience seeding tau

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Last Updated: Jul 25, 2025

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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Area of Science:

Neurobiology
Molecular Biology
Protein Biochemistry

Background:

Neurodegenerative tauopathies result from toxic tau protein accumulation.
Chaperone proteins like Hsp70s and J domain proteins (JDPs) regulate protein folding, including tau.
The specific JDPs involved in coordinating tau folding and aggregation remain largely unknown.

Purpose of the Study:

To investigate the role of JDPs in regulating intracellular tau aggregation.
To determine if DnaJC7's interaction with tau is specific or shared by other JDPs.
To elucidate the mechanism by which DnaJC7 inhibits tau aggregation.

Main Methods:

Proteomics analysis in a cell model to identify proteins interacting with tau.
Cellular assays to assess the impact of JDP knockout on tau aggregation and seeding.
Site-directed mutagenesis to evaluate the functional importance of DnaJC7's J domain and substrate-binding site.

Main Results:

DnaJC7 was found to co-purify with insoluble tau and colocalize with tau aggregates.
Knockout of DnaJC7 led to decreased aggregate clearance and increased intracellular tau seeding.
Mutations in DnaJC7's J domain or substrate-binding site abolished its protective function against tau aggregation.

Conclusions:

DnaJC7 specifically regulates tau aggregation through cooperation with Hsp70.
The J domain of DnaJC7 is essential for stimulating Hsp70 ATPase activity, which is critical for its anti-aggregation function.
Disease-associated mutations in DnaJC7 impair its ability to regulate tau aggregation, suggesting a potential therapeutic target.