Cellular strategies for controlling protein aggregation

Nat Rev Mol Cell Biol. 2010 Nov;11(11):777-88. doi: 10.1038/nrm2993. Epub 2010 Oct 14.

Abstract

The aggregation of misfolded proteins is associated with the perturbation of cellular function, ageing and various human disorders. Mounting evidence suggests that protein aggregation is often part of the cellular response to an imbalanced protein homeostasis rather than an unspecific and uncontrolled dead-end pathway. It is a regulated process in cells from bacteria to humans, leading to the deposition of aggregates at specific sites. The sequestration of misfolded proteins in such a way is protective for cell function as it allows for their efficient solubilization and refolding or degradation by components of the protein quality-control network. The organized aggregation of misfolded proteins might also allow their asymmetric distribution to daughter cells during cell division.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Autophagy / physiology
  • Cell Physiological Phenomena / physiology*
  • Heat-Shock Proteins / physiology
  • Humans
  • Models, Biological
  • Models, Molecular
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Folding*
  • Proteins / chemistry*
  • Proteins / physiology*

Substances

  • Heat-Shock Proteins
  • Proteins
  • Proteasome Endopeptidase Complex