Reversible protein aggregation as cytoprotective mechanism against heat stress

Curr Genet. 2021 Dec;67(6):849-855. doi: 10.1007/s00294-021-01191-2. Epub 2021 Jun 6.

Abstract

Temperature fluctuation is one of the most frequent threats to which organisms are exposed in nature. The activation of gene expression programs that trigger the transcription of heat stress-protective genes is the main cellular response to resist high temperatures. In addition, reversible accumulation and compartmentalization of thermosensitive proteins in high-order molecular assemblies are emerging as critical mechanisms to ensure cellular protection upon heat stress. Here, we summarize representative examples of membrane-less intracellular bodies formed upon heat stress in yeasts and human cells and highlight how protein aggregation can be turned into a cytoprotective mechanism.

Publication types

  • Review

MeSH terms

  • Amyloid / metabolism
  • Cell Nucleus / metabolism
  • Cytoplasm / metabolism
  • Cytoprotection*
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism*
  • Heat-Shock Response*
  • Protein Aggregates*
  • Protein Binding
  • Solubility
  • Stress Granules / metabolism
  • Stress, Physiological
  • Yeasts / physiology*

Substances

  • Amyloid
  • Fungal Proteins
  • Protein Aggregates