ArticleProtein science : a publication of the Protein Society2021
An apparent core/shell architecture of polyQ aggregates in the aging Caenorhabditis elegans neuron.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 13 citations in OpenAlex.
- Natural longevity modulator: aging modulatory effects of Eurycoma longifolia Jack polysaccharides in C. elegans and D. melanogaster.Biogerontology · 2026Article
- Structural Mapping of Protein Aggregates in Live Cells Modeling Huntington's Disease.Angewandte Chemie (International ed. in English) · 2024Article
- Lipid Membrane Topographies Are Regulators for the Spatial Distribution of Liquid Protein Condensates.Nano letters · 2024Article
- Article
- Intermediate filaments associate with aggresome-like structures in proteostressed C. elegans neurons and influence large vesicle extrusions as exophers.Nature communications · 2023Article
- Review
- An apparent core/shell architecture of polyQ aggregates in the aging Caenorhabditis elegans neuron.Protein science : a publication of the Protein Society · 2021Article
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5 authors at 1 institution in 1 country.
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Abstract
Huntington's disease is caused by a polyglutamine (polyQ) expansion in the huntingtin protein which results in its abnormal aggregation in the nervous system. Huntingtin aggregates are linked to toxicity and neuronal dysfunction, but a comprehensive understanding of the aggregation mechanism in vivo remains elusive. Here, we examine the morphology of polyQ aggregates in Caenorhabditis elegans mechanosensory neurons as a function of age using confocal and fluorescence lifetime imaging microscopy. We find that aggregates in young worms are mostly spherical with homogenous intensity, but as the worm ages aggregates become substantially more heterogeneous. Most prominently, in older worms we observe an apparent core/shell morphology of polyQ assemblies with decreased intensity in the center. The fluorescence lifetime of polyQ is uniform across the aggregate indicating that the dimmed intensity in the assembly center is most likely not due to quenching or changes in local environment, but rather to displacement of fluorescent polyQ from the central region. This apparent core/shell architecture of polyQ aggregates in aging C. elegans neurons contributes to the diverse landscape of polyQ aggregation states implicated in Huntington's disease.
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