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Updated: Jan 12, 2026

Evaluation of LC3-II Release via Extracellular Vesicles in Relation to the Accumulation of Intracellular LC3-positive Vesicles

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TDP-43 Phosphorylation: Pathological Modification or Protective Factor Antagonizing TDP-43 Aggregation in

Simone Mosna^1,2, Dorothee Dormann^1,3

¹Institute of Molecular Physiology, Faculty of Biology, Johannes Gutenberg University, Mainz, Germany.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology

|November 3, 2025

Summary

This summary is machine-generated.

TDP-43 protein aggregation is implicated in neurodegenerative diseases like ALS and Alzheimer's. Research suggests TDP-43 hyperphosphorylation may actually prevent harmful aggregation, offering new therapeutic insights.

Keywords:

TAR DNA binding protein of 43 kDa (TDP‐43)amyotrophic lateral sclerosis (ALS)condensates frontotemporal dementia (FTD)kinases neurodegeneration phase separation phosphorylation protein aggregation

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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:

Neuroscience
Molecular Biology
Biochemistry

Background:

TDP-43, an RNA-binding protein, aggregates in neurodegenerative diseases.
Aggregated TDP-43 is hyperphosphorylated, unlike its normal unphosphorylated state.

Purpose of the Study:

To review current knowledge on TDP-43 phosphorylation in disease.
To explore the role of kinases and phosphatases in regulating TDP-43 phosphorylation.
To discuss the impact of TDP-43 phosphorylation on its aggregation and toxicity.

Main Methods:

Literature review of existing research on TDP-43 phosphorylation.
Analysis of studies investigating kinases and phosphatases involved with TDP-43.
Examination of evidence linking TDP-43 phosphorylation to phase separation and aggregation.

Main Results:

TDP-43 hyperphosphorylation is observed in neurodegenerative conditions.
Recent evidence indicates hyperphosphorylation may antagonize TDP-43 aggregation.
The precise role of phosphorylation in TDP-43 pathology remains under investigation.

Conclusions:

TDP-43 phosphorylation is a critical post-translational modification in neurodegeneration.
Hyperphosphorylation may serve a protective role against TDP-43 aggregation.
Further research is needed to elucidate the complex relationship between TDP-43 phosphorylation, aggregation, and disease.