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Related Experiment Video

Updated: May 11, 2026

Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells

Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells

Published on: October 4, 2017

Protein aggregation in amyotrophic lateral sclerosis.

Anna M Blokhuis¹, Ewout J N Groen, Max Koppers

¹Department of Neuroscience and Pharmacology, Rudolf Magnus Institute of Neuroscience, University Medical Center, Utrecht, The Netherlands.

Acta Neuropathologica

|May 16, 2013

Summary

Protein aggregation in amyotrophic lateral sclerosis (ALS) involves key molecules like FUS and TDP-43. Understanding these aggregates offers insights into neurodegeneration and potential therapeutic targets for ALS.

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Published on: June 26, 2018

Area of Science:

Neurobiology
Molecular Biology
Genetics

Background:

Amyotrophic lateral sclerosis (ALS) is characterized by protein aggregation in motor neurons.
Key proteins implicated include FUS, TDP-43, OPTN, UBQLN2, and C9ORF72 products.
These proteins form aggregates in both familial and sporadic ALS, and other neurodegenerative diseases.

Purpose of the Study:

To review recent advances in understanding the molecular composition, formation, and function of protein aggregates in ALS.
To explore the link between genetic alterations and aggregate characteristics.
To discuss potential mechanisms contributing to protein aggregation and neuronal dysfunction.

Main Methods:

Review of recent scientific literature on ALS and protein aggregation.
Analysis of molecular constituents and genetic associations of ALS-linked aggregates.
Discussion of proposed mechanisms like prion-like domains, RNA granule dysfunction, and protein quality control issues.

Main Results:

Identified several key proteins (FUS, TDP-43, etc.) in ALS aggregates, with mutations linked to disease pathogenesis.
Observed overlap in aggregate composition across different ALS types and other neurodegenerative disorders.
Highlighted potential aggregation mechanisms and both gain- and loss-of-function effects.

Conclusions:

Protein aggregation is central to ALS pathogenesis, involving specific molecular players and cellular processes.
Understanding aggregate formation and function provides insights into disease mechanisms.
Further research into protein aggregation may reveal novel therapeutic strategies for ALS.