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Related Experiment Video

Updated: Feb 5, 2026

Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy

Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy

Published on: August 3, 2021

Pour Some Sugar on TDP(-43).

Steven Boeynaems¹, Aaron D Gitler¹

¹Department of Genetics, Stanford University School of Medicine, Stanford, CA 94305, USA.

|September 8, 2018

Summary

This summary is machine-generated.

Researchers found that poly(ADP-ribose) binding controls the phase behavior of the ALS protein TDP-43. This discovery explains TDP-43 aggregation in disease and suggests a new therapeutic target.

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Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis

Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis

Published on: February 12, 2015

Area of Science:

Biochemistry
Molecular Biology
Neuroscience

Background:

Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease linked to the aggregation of the trans-active response DNA binding protein (TDP-43).
The phase behavior of proteins, including TDP-43, is crucial for cellular function and implicated in disease pathogenesis.

Purpose of the Study:

To investigate the molecular mechanisms by which poly(ADP-ribose) (PAR) binding influences the phase separation and aggregation of TDP-43.
To identify potential therapeutic strategies targeting TDP-43 aggregation in ALS.

Main Methods:

Utilized in vitro phase separation assays.
Employed biophysical techniques to characterize TDP-43-PAR interactions.
Investigated the effects of PAR binding on TDP-43 aggregation kinetics.

Main Results:

Demonstrated that poly(ADP-ribose) binding significantly alters the phase behavior of TDP-43.
Showed that PAR binding can inhibit or promote TDP-43 aggregation depending on specific conditions.
Identified key molecular interfaces involved in TDP-43-PAR interactions.

Conclusions:

Poly(ADP-ribose) acts as a critical regulator of TDP-43 phase separation and aggregation.
Modulating TDP-43-PAR interactions presents a promising therapeutic avenue for ALS treatment.