Aggresomes do not represent a general cellular response to protein misfolding in mammalian cells

BMC Cell Biol. 2008 Oct 20:9:59. doi: 10.1186/1471-2121-9-59.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • COS Cells
  • Chlorocebus aethiops
  • Cytoplasm / metabolism
  • Fluorescent Antibody Technique
  • HeLa Cells
  • Humans
  • In Situ Hybridization, Fluorescence
  • Inclusion Bodies / metabolism*
  • Mice
  • NIH 3T3 Cells
  • Prions / analysis
  • Prions / chemistry
  • Prions / metabolism*
  • Protein Folding*


  • Prions