Related Experiment Video
Updated: Jun 28, 2026

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
Published on: June 23, 2018
Aggresomes do not represent a general cellular response to protein misfolding in mammalian cells
Simon Beaudoin1, Kevin Goggin, Cyntia Bissonnette
1Department of Biochemistry, Faculty of Medicine, University of Sherbrooke, Sherbrooke, Québec J1H 5N4, Canada. simon.beaudoin@usherbrooke.ca
Background:
Aggresomes are juxtanuclear inclusion bodies that have been proposed to represent a general cellular response to misfolded proteins in mammalian cells. Yet, why aggresomes are not a pathological characteristic of protein misfolding diseases is unclear. Here, we investigate if a misfolded protein inevitably forms aggresomes in mammalian cells.
Results:
We show that a cytoplasmic form of the prion protein may form aggresomes or dispersed aggregates in different cell lines. In contrast to aggresomes, the formation of dispersed aggregates is insensitive to histone deacetylase 6 inhibitors and does not result in cytoskeleton rearrangements. Modulation of expression levels or proteasome inhibitors does not alter the formation of dispersed aggregates.
Conclusion:
Our results establish that aggresomes are not obligatory products of protein misfolding in vivo.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
The Unfolded Protein Response
Molecular Chaperones and Protein Folding
The...
Export of Misfolded Proteins out of the ER
Proteins: From Genes to Degradation
Transcription is the synthesis of RNA molecules by RNA...
Regulation of the Unfolded Protein Response

