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Updated: May 5, 2026
Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
Published on: December 17, 2021
Modelling FUSopathies: focus on protein aggregation
Abstract:
The discovery of a causative link between dysfunction of a number of RNA-binding proteins with prion-like domains and the development of certain (neuro)degenerative diseases has completely changed our perception of molecular mechanisms instigating pathological process in these disorders. Irreversible aggregation of these proteins is a crucial pathogenic event delineating a type of proteinopathy. FUS (fused in sarcoma) is a prototypical member of the class, and studies into the causes and consequences of FUSopathies have been instrumental in characterizing the processes leading to deregulation of RNA metabolism in neurodegeneration. In vivo models of FUSopathy have provided critical insights into the mechanisms of FUS toxicity and clues on the role of non-amyloid aggregates, which are hallmarks of these diseases. The present review summarizes the data on FUS aggregation signatures in available model organisms on the basis of overexpression of FUS variants.
Insights
RNA-binding proteins like FUS (fused in sarcoma) are linked to neurodegenerative diseases. This review details FUS aggregation in model organisms, offering insights into FUSopathies and RNA metabolism deregulation.
Area of Science:
- Neuroscience
- Molecular Biology
- Genetics
Background:
- Dysfunction of RNA-binding proteins with prion-like domains is linked to neurodegenerative diseases.
- Protein aggregation, specifically FUS (fused in sarcoma) aggregation, defines a class of proteinopathies known as FUSopathies.
- Understanding FUS aggregation is crucial for elucidating RNA metabolism deregulation in neurodegeneration.
Purpose of the Study:
- To review and summarize data on FUS aggregation signatures.
- To analyze aggregation in various model organisms.
- To understand the role of FUS variants in disease pathogenesis.
Main Methods:
- Review of existing literature on FUS aggregation.
- Analysis of data from in vivo models of FUSopathy.
- Focus on models utilizing overexpression of FUS variants.
Main Results:
- FUS aggregation is a key pathogenic event in FUSopathies.
- In vivo models provide insights into FUS toxicity mechanisms.
- Non-amyloid aggregates are characteristic hallmarks of these diseases.
Conclusions:
- FUS aggregation signatures in model organisms are informative for understanding FUSopathies.
- Studies on FUS aggregation contribute to understanding neurodegeneration and RNA metabolism.
- Further research in model systems can reveal therapeutic targets for FUS-related disorders.
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