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Updated: Jun 5, 2026

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
Published on: December 17, 2021
Analyzing the aggregation of polyglutamine-expansion proteins and its modulation by molecular chaperones
Hiroshi Kubota1, Akira Kitamura, Kazuhiro Nagata
1Department of Life Science, Faculty of Engineering and Resource Science, Akita University, 1-1 Tegatagakuen-cho, Akita 010-8502, Japan. hkubota@gipc.akita-u.ac.jp
Abstract:
Polyglutamine (polyQ)-expansion proteins cause protein aggregation in the cytosol and nucleus of neuronal cells, leading to neurodegenerative diseases. For example, expansion of the polyQ tract (>40 repeats) in huntingtin (htt) proteins leads to Huntington disease, while polyQ-expanded ataxins cause several types of ataxias. PolyQ-rich inclusions are found in neuronal cells of patients, suggesting that polyQ disease is caused by protein misfolding. However, the mechanisms by which polyQ-expansion proteins exert neuronal toxicity are largely unknown. Here, we review experimental procedures to analyze the roles of molecular chaperones in preventing polyQ aggregation and toxicity as well as to measure the characteristics and dynamics of polyQ aggregation, particularly focusing on cellular models and dynamic imaging of fluorescently-labeled polyQ-expansion proteins and their modulation by chaperones.
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