Proteostasis impairment in protein-misfolding and -aggregation diseases

Trends Cell Biol. 2014 Sep;24(9):506-14. doi: 10.1016/j.tcb.2014.05.003. Epub 2014 Jun 16.

Abstract

Cells possess an extensive network of components to safeguard proteome integrity and maintain protein homeostasis (proteostasis). When this proteostasis network (PN) declines in performance, as may be the case during aging, newly synthesized proteins are no longer able to fold efficiently and metastable proteins lose their functionally active conformations, particularly under conditions of cell stress. Apart from loss-of-function effects, a critical consequence of PN deficiency is the accumulation of cytotoxic protein aggregates, which are also associated with many age-dependent neurodegenerative diseases and other medical disorders. Here we discuss recent evidence that the chronic production of aberrantly folded and aggregated proteins in these diseases is harmful by overtaxing PN capacity, setting in motion a vicious cycle of increasing proteome imbalance that eventually leads to PN collapse and cell death.

Keywords: degradation; molecular chaperones; neurodegenerative disease; protein (mis)folding; protein aggregation; proteostasis.

Publication types

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

MeSH terms

  • Aging / genetics
  • Aging / pathology
  • Homeostasis
  • Humans
  • Molecular Chaperones / genetics
  • Protein Aggregation, Pathological / genetics*
  • Protein Folding*
  • Proteins / genetics*
  • Proteins / metabolism
  • Proteolysis
  • Proteostasis Deficiencies / genetics*
  • Proteostasis Deficiencies / pathology

Substances

  • Molecular Chaperones
  • Proteins